stunning news: Immunity from MadCow Disease; the model of Manufacturing

Discussion in 'Health and medical' started by Archimedes Plut, Jun 7, 2004.

  1. --- quoting in part from Reuters --- Scientists Produce Cow
    Immune to Mad Cow Disease

    23 minutes ago Reuters

    TOKYO (Reuters) - Kirin Brewery Co, Japan's number-two beer
    maker, has succeeded in producing a cow that is immune to
    mad cow disease, but experts said it was too early for
    livestock producers to celebrate.

    Kirin officials said on Monday the company had produced
    jointly with a U.S. company a cow that carried none of the
    "prion" proteins that cause the brain-wasting disease, also
    known as bovine spongiform encephalopathy (BSE (news - web
    sites)). BSE is passed on by an infectious protein particle
    called a prion. Neither a living organism nor a virus, it is
    a misshapen protein that can convert other proteins to the
    deadly form by touching them. --- end quoting ---

    Stunning news for it completely flys above and beyond
    current ideas and models of BSE and prion disease. It is as
    if someone reported immunity for Cancer yet without even
    knowing what causes and the details of the cancer. It is
    like Faraday reporting not just a law of electrodynamics in
    the 1800s but delivering a electric power station.

    If the above is true in part or whole then we begin to see
    that there never was any real use or function for prion
    proteins in animal bodies and that all prions are what cause
    the disease. The moment an animal body produces prions then
    that animal is sick.

    The above is true proves that the Prusiner Model is false
    because it is the manufacturing of prions by the body itself
    that creates the disease.

    And whereas in Alzheimers there are two proteins involved
    which are needed for the disease to accelerate of the tau
    and betaamyloids. So that in Prion disease, if an animal
    starts producing or manufacturing so called "good prions"
    the animal is already highly sick. Then when something else
    happens of the addition of another prion the disease is
    accelerated.

    Are tau and betaamyloids naturally occurring in humans
    or are these two proteins found only in Alzheimers
    sick persons?

    Is alphasynuclein of Parkinsons a naturally occurring
    protein in humans or is it found only in persons with
    Parkinsons disease.

    If we create a cow that cannot synthesize prion proteins and
    obviously the cow can live without the protein, then, can
    humans live without synthesizing tau and betaamyloids and
    alphasynuclein so that they are immune to Alzheimers and
    Parkinsons.

    This was a huge trouble with Prion disease way back in the
    1980s for it was never resolved in all these decades what
    the use or function of the protein ever was.

    I hope this Kirin report is true and accurate and it is a
    beautiful way of flying over and above all of the "psuedo
    science of prion disease". In one stroke the Kirin report
    eliminates thousands of worthless science reports of prion
    proteins, especially the silly yeast prion having any
    connection to animal prions.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
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  2. Mark Thorson

    Mark Thorson Guest

    Archimedes Plutonium wrote:

    > Stunning news for it completely flys above and beyond
    > current ideas and models of BSE and prion disease. It is
    > as if someone reported immunity for Cancer yet without
    > even knowing what causes and the details of the cancer. It
    > is like Faraday reporting not just a law of
    > electrodynamics in the 1800s but delivering a electric
    > power station.

    No, the announcement is totally in-line with everything we
    know about MCD, except that they perhaps shouldn't have used
    the word "immune" because that would imply an involvement
    with the immune system. PrP-null mice were developed years
    ago, so it is no surprise that someone would undertake to
    develop PrP-null cattle. They would not be subject to MCD,
    because they have no PrP to infect.

    > If the above is true in part or whole then we begin to see
    > that there never was any real use or function for prion
    > proteins in animal bodies and that all prions are what
    > cause the disease. The moment an animal body produces
    > prions then that animal is sick.

    Just because we don't know what PrP does, doesn't mean it
    does nothing. However, whatever its role is, it can't be
    too important, because PrP-null mice appear to be
    perfectly healthy.

    > The above is true proves that the Prusiner Model is false
    > because it is the manufacturing of prions by the body
    > itself that creates the disease.

    It is the catalytic conversion of healthy forms of PrP to
    the diseased form which is MCD. That is the model. Nothing
    you've cited contradicts it. In fact, if these cattle indeed
    cannot be infected, this is additional evidence to support
    the model.
     
  3. Mon, 31 May 2004 11:44:36 -0500 Archimedes Plutonium wrote:

    > --- quoting in part from Reuters --- Scientists Produce
    > Cow Immune to Mad Cow Disease
    >
    > 23 minutes ago Reuters
    >
    > TOKYO (Reuters) - Kirin Brewery Co, Japan's number-two
    > beer maker, has succeeded in producing a cow that is
    > immune to mad cow disease, but experts said it was too
    > early for livestock producers to celebrate.
    >
    > Kirin officials said on Monday the company had produced
    > jointly with a U.S. company a cow that carried none of the
    > "prion" proteins that cause the brain-wasting disease,

    Stunning news, if true for it suggests that all prion
    proteins in animal bodies are of no use or no function.
    Suggests that there is no difference between good prions
    and bad prions for all prions are disease ridden. It
    suggests that the body Manufacturing Sites have gone awry
    as what causes and creates the disease. It suggests that
    the start of Prion sickness is when any prion can be found
    in the body and that a person free of prion disease has no
    prions in the body.

    Now, can we apply that to Alzheimers and to Parkinsons?

    Can we say that a person who has any tau or betaamyloid
    proteins in the body that the person has Alzheimers? Can we
    say that a person who has none of these two proteins is free
    and clear of Alzheimers? Can we say that Manufacturing sites
    of a person creates the tau and betaamyloids and the moment
    those appear the person is sick? Can we find an immunity to
    Alzheimers in the same manner as Kirin found for prion?

    Likewise for Parkinsons disease and its protein of
    alphasynuclein. We ask the same questions as above.

    It is stunning news because it forces us to think that
    these proteins never really had any function or purpose and
    that when the brain produces or creates a prion molecule or
    a tau or betaamyloid or a alphasynuclein molecule that the
    person is already sick with the disease. And that the cure
    for the diseases of Alzheimers or Parkinsons and of Prion
    is to force the body to stop producing these proteins. For
    none of these proteins has a purpose or role or function or
    use, and that all of these proteins are a sign that the
    body is diseased.

    I suppose we can look at this in the analogy of a cancer
    cell. To think that a single cancer cell had some purpose
    or use or function for a health body was a silly and
    ridiculous notion and that the single cancer cell could
    multiply and create a cancer disease. So in this analogy,
    why did the medical community ever think that the first
    appearance of a single prion protein was ever a "good
    thing" or the appearance of tau or betaamyloid or of
    alphasynuclein as a "good thing". The appearance of any
    single cancer cells is the harbinger of a whole entire
    disease and why we never considered that the appearance of
    prion or tau or betaamyloid or alphasynuclein were the
    start of a sickening disease.

    And that the cure of cancer is to stop and eliminate all
    cancer cells and the cure for Alzheimers, Parkinsons, or
    Prion is to stop and eliminate all tau/betaamyloids
    proteins, and all alphasynuclein proteins and all prion
    proteins. None of these proteins has any useful good
    function just as all cancer cells are disease entities.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  4. Bob

    Bob Guest

    On Mon, 31 May 2004 11:44:36 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >--- quoting in part from Reuters --- Scientists Produce Cow
    >Immune to Mad Cow Disease
    >
    > 23 minutes ago Reuters
    >
    >
    >TOKYO (Reuters) - Kirin Brewery Co, Japan's number-two beer
    >maker, has succeeded in producing a cow that is immune to
    >mad cow disease, but experts said it was too early for
    >livestock producers to celebrate.
    >
    >Kirin officials said on Monday the company had produced
    >jointly with a U.S. company a cow that carried none of the
    >"prion" proteins that cause the brain-wasting disease, also
    >known as bovine spongiform encephalopathy (BSE (news - web
    >sites)). BSE is passed on by an infectious protein particle
    >called a prion. Neither a living organism nor a virus, it
    >is a misshapen protein that can convert other proteins to
    >the deadly form by touching them. --- end quoting ---
    >
    >Stunning news

    Actually it is mostly old news -- except for it being
    specifically in cows. This was done with mice long ago, and
    was key evidence for the prion model. That is, animals
    lacking the prion gene cannot acquire the prion disease.
    (Note that in general there may be many reasons why an
    animal with a mutation is not susceptible to a disease. But
    in this case, the gene is that for the "known" toxic
    protein. So what this really did was to lay to rest the
    virus model; it solved the apparent self-replication of the
    prion protein, by showing that the host makes
    it.)

    Note that the term immune is used here very loosely, not
    referring to antibodies, but just to lack of susceptibility.

    I believe it has also been done for sheep.

    >for it completely flys above and beyond current ideas and
    >models of BSE and prion disease.

    Exactly what was expected, which is why they did it. It was
    just a matter of doing the genetic engineering, not so easy
    with cows.

    >It is as if someone reported immunity for Cancer yet
    >without even knowing what causes and the details of
    >the cancer.

    Huh? Not cancer, but all early immunization work was done
    without knowledge of the infection process or of immunity
    per se. Smallpox immunization was done long before people
    even knew what a virus was.

    However, in the current case, the result was predicted, and
    they did the work precisely because of considerable optimism
    it would work.

    >It is like Faraday reporting not just a law of
    >electrodynamics in the 1800s but delivering a electric
    >power station.
    >
    >If the above is true in part or whole then we begin to see
    >that there never was any real use or function for prion
    >proteins in animal bodies and that all prions are what
    >cause the disease.

    It does show that the prion protein appears to be non-
    essential, just as we have discussed before from the
    mouse work.

    However, there is some reservation about this. The protein
    is quite conserved among the mammals. This really suggests
    it is important. Yet deleting it is without (apparent)
    effect. Odd. In fact, some subtle neurological effects have
    been reported (for mice?). Maybe these are of significance.

    >The moment an animal body produces prions then that
    >animal is sick.

    Welllllll (and ignoring the posisble natural role, mentined
    above)... that might be a semantic point. Unless "somethign
    happens", no they do not seem to be sick.

    >
    >Are tau and betaamyloids naturally occurring in humans
    >or are these two proteins found only in Alzheimers
    >sick persons?

    I think natural role for the beta amyloid precursor protein
    is known. Don't recall details.

    >
    >Is alphasynuclein of Parkinsons a naturally occurring
    >protein in humans or is it found only in persons with
    >Parkinsons disease.
    >
    >If we create a cow that cannot synthesize prion proteins
    >and obviously the cow can live without the protein, then,
    >can humans live without synthesizing tau and betaamyloids
    >and alphasynuclein so that they are immune to Alzheimers
    >and Parkinsons.
    >

    no reason to assume that. But it is testable in mice (and
    probably has been tested?)

    >This was a huge trouble with Prion disease way back in the
    >1980s for it was never resolved in all these decades what
    >the use or function of the protein ever was.

    It has long been known that it is non-essential, from the
    mouse work. This has been noted on a number of occasions in
    our discussions. But there is the reservation noted above.

    bob
     
  5. Mon, 31 May 2004 20:27:17 -0700 Bob wrote:

    > On Mon, 31 May 2004 11:44:36 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >--- quoting in part from Reuters --- Scientists Produce
    > >Cow Immune to Mad Cow Disease
    > >
    > > 23 minutes ago Reuters
    > >
    > >
    > >TOKYO (Reuters) - Kirin Brewery Co, Japan's number-two
    > >beer maker, has succeeded in producing a cow that is
    > >immune to mad cow disease, but experts said it was too
    > >early for livestock producers to celebrate.
    > >
    > >Kirin officials said on Monday the company had produced
    > >jointly with a U.S. company a cow that carried none of
    > >the "prion" proteins that cause the brain-wasting
    > >disease, also known as bovine spongiform encephalopathy
    > >(BSE (news - web sites)). BSE is passed on by an
    > >infectious protein particle called a prion. Neither a
    > >living organism nor a virus, it is a misshapen protein
    > >that can convert other proteins to the deadly form by
    > >touching them. --- end quoting ---
    > >
    > >Stunning news
    >
    > Actually it is mostly old news -- except for it being
    > specifically in cows. This was done with mice long ago,
    > and was key evidence for the prion model. That is, animals
    > lacking the prion gene cannot acquire the prion disease.
    > (Note that in general there may be many reasons why an
    > animal with a mutation is not susceptible to a disease.
    > But in this case, the gene is that for the "known" toxic
    > protein. So what this really did was to lay to rest the
    > virus model; it solved the apparent self-replication of
    > the prion protein, by showing that the host makes
    > it.)
    >
    > Note that the term immune is used here very loosely, not
    > referring to antibodies, but just to lack of
    > susceptibility.
    >
    > I believe it has also been done for sheep.
    >
    > >for it completely flys above and beyond current ideas and
    > >models of BSE and prion disease.
    >
    > Exactly what was expected, which is why they did it. It
    > was just a matter of doing the genetic engineering, not so
    > easy with cows.
    >
    > >It is as if someone reported immunity for Cancer yet
    > >without even knowing what causes and the details of the
    > >cancer.
    >
    > Huh? Not cancer, but all early immunization work was done
    > without knowledge of the infection process or of immunity
    > per se. Smallpox immunization was done long before people
    > even knew what a virus was.
    >
    > However, in the current case, the result was predicted,
    > and they did the work precisely because of considerable
    > optimism it would work.
    >
    > >It is like Faraday reporting not just a law of
    > >electrodynamics in the 1800s but delivering a electric
    > >power station.
    > >
    > >If the above is true in part or whole then we begin to
    > >see that there never was any real use or function for
    > >prion proteins in animal bodies and that all prions are
    > >what cause the disease.
    >
    > It does show that the prion protein appears to be non-
    > essential, just as we have discussed before from the
    > mouse work.
    >
    > However, there is some reservation about this. The protein
    > is quite conserved among the mammals. This really suggests
    > it is important. Yet deleting it is without (apparent)
    > effect. Odd. In fact, some subtle neurological effects
    > have been reported (for mice?). Maybe these are of
    > significance.
    >
    > >The moment an animal body produces prions then that
    > >animal is sick.
    >
    > Welllllll (and ignoring the posisble natural role,
    > mentined above)... that might be a semantic point. Unless
    > "somethign happens", no they do not seem to be sick.
    >
    > >
    > >Are tau and betaamyloids naturally occurring in humans or
    > >are these two proteins found only in Alzheimers sick
    > >persons?
    >
    > I think natural role for the beta amyloid precursor
    > protein is known. Don't recall details.
    >
    > >
    > >Is alphasynuclein of Parkinsons a naturally occurring
    > >protein in humans or is it found only in persons with
    > >Parkinsons disease.
    > >
    > >If we create a cow that cannot synthesize prion proteins
    > >and obviously the cow can live without the protein, then,
    > >can humans live without synthesizing tau and betaamyloids
    > >and alphasynuclein so that they are immune to Alzheimers
    > >and Parkinsons.
    > >
    >
    > no reason to assume that. But it is testable in mice (and
    > probably has been tested?)
    >
    > >This was a huge trouble with Prion disease way back in
    > >the 1980s for it was never resolved in all these decades
    > >what the use or function of the protein ever was.
    >
    > It has long been known that it is non-essential, from
    > the mouse work. This has been noted on a number of
    > occasions in our discussions. But there is the
    > reservation noted above.
    >
    > bob

    I failed to notice any such warnings or indications that all
    prions, whether of so called good form or bad form were all
    nonessential to animal bodies. I suppose if I was a
    researcher in medicine and had familiarity with Prion
    disease I would have known outright that all prion proteins
    were nonfunctional and nonessential. It is to be expected
    that for me to pick up on essential facts about Prion
    disease would take a "Kirin" report to make clear to me.

    I do not remember any "noted on a number of occasions". And
    of course these

    conversations go back to about 1997 and are about 7 years
    old. I do remember clearly reading that the purpose and
    function of prion proteins was cell wall. Something to do
    with cell walls. But that looks like a falsehood.

    Bob, do you know the people who claimed prion proteins
    had some role in cell wall and whether claims like that
    are debunked.

    I think it is more important to focus on whether immunity
    for Alzheimers and Parkinsons is near at hand rather than
    focus on details of Prion disease. It is the cross
    referencing of these Family Related Diseases of Alzheimers,
    Parkinsons and Prion that I feel takes priority over
    details of prion.

    One such cross reference is that in Prion disease we have so
    called normal or good prions and then we have the alleged
    "bad prion". In Alzheimers we have the tau and we have the
    betaamyloid and we still are uncertain as to the connection
    between tau and betaamyloid. But with the Kirin report
    suggesting that all prion proteins are bad and that any
    prion protein that shows up in animal bodies is a sign that
    the disease is already existing. Suggests that in Alzheimers
    that the moment one tau or one betaamyloid molecule is found
    in an animal body, then that animal has Alzheimers.

    It is safe to say that the moment any animal has one cancer
    cell, then that animal has cancer.

    Cross referencing to Parkinsons is more important than
    details of Prion. Is alphasynuclein have any function or
    role? Or is it like prions of the Kirin report that all
    alphasynuclein is of no use. Which implies that one
    alphasynuclein molecule in an animal body means the animal
    has Parkinsons disease.

    Bob, I feel if any of the above comments are correct in
    part or in whole, then all three of these diseases of
    Alzheimers, Parkinsons and Prion are brain diseases created
    by malfunctioning manufacturing sites that spew out a
    protein that the body does not need or want and thus the
    disease is borne. All three are hereditary diseases
    indicating that manufacturing sites gone awry are
    genetically based. Prion is contagious by eating, but is it
    a protein molecule that alters the shape of other protein
    molecules? The Kirin report suggests otherwise. That it is
    the prion protein that somehow alters the manufacturing
    site of protein synthesis. So it is not prion X altering
    prion Y. It is prion X which lodges in the synthesis
    channels and then spews out more prion X.

    And if the Kirin report is accurate, then the tough problem
    of assigning how much of the disease is production and how
    much is due to body inability to remove unwanted waste
    proteins is answered. In cancer we do not ask why the body
    cannot remove the cancer cells. We ask in Cancer why the
    body produces the cancer cell in the first place. Cancer is
    borne the moment a single cancer cell comes into existence.
    Likewise for Alzheimers is borne the moment a tau or
    betaamyloid comes into existence. Parkinsons is borne the
    moment a single alphasynuclein molecule appears. And CJD is
    borne the moment a single prion protein molecule appears
    regardless as to whether the prion protein is one of many
    variants or even the benign prion. All prion molecules are
    useless and nonessential to animals and the moment a single
    prion occurs in the brain of an animal, that animal is sick
    of the disease.

    So it looks as though the cure for Alzheimers and Parkinsons
    is just around the corner. The cure is to alter the
    Manufacturing Sites such that they cannot produce tau or
    betaamyloid or alphasynuclein.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  6. Archimedes Plutonium wrote:

    > Mon, 31 May 2004 20:27:17 -0700 Bob wrote:
    >
    > > On Mon, 31 May 2004 11:44:36 -0500, Archimedes Plutonium
    > > <[email protected]> wrote:
    > >
    > > >--- quoting in part from Reuters --- Scientists Produce
    > > >Cow Immune to Mad Cow Disease
    > > >
    > > > 23 minutes ago Reuters
    > > >
    > > >
    > > >TOKYO (Reuters) - Kirin Brewery Co, Japan's number-two
    > > >beer maker, has succeeded in producing a cow that is
    > > >immune to mad cow disease, but experts said it was too
    > > >early for livestock producers to celebrate.
    > > >
    > > >Kirin officials said on Monday the company had produced
    > > >jointly with a U.S. company a cow that carried none of
    > > >the "prion" proteins that cause the brain-wasting
    > > >disease, also known as bovine spongiform encephalopathy
    > > >(BSE (news - web sites)). BSE is passed on by an
    > > >infectious protein particle called a prion. Neither a
    > > >living organism nor a virus, it is a misshapen protein
    > > >that can convert other proteins to the deadly form by
    > > >touching them. --- end quoting ---
    > > >
    > > >Stunning news
    > >
    > > Actually it is mostly old news -- except for it being
    > > specifically in cows. This was done with mice long ago,
    > > and was key evidence for the prion model. That is,
    > > animals lacking the prion gene cannot acquire the prion
    > > disease. (Note that in general there may be many reasons
    > > why an animal with a mutation is not susceptible to a
    > > disease. But in this case, the gene is that for the
    > > "known" toxic protein. So what this really did was to
    > > lay to rest the virus model; it solved the apparent self-
    > > replication of the prion protein, by showing that the
    > > host makes
    > > it.)
    >

    I disagree Bob. The Prion Model has you believe prion X
    converts prionY into more prionX. When that could be utterly
    wrong. In that when Prion X enters the body it merely alters
    the site of Synthesis or Manufacturing of proteins and thus
    results in the increase in more prion proteins. In the
    ManufacturingSite Model there is no conversion by prion X of
    any other prions.

    The only thing in common with the Prusiner Model and the
    Manufacturing Site Model is that both would agree a prion
    protein is or can be an infectious agent.

    I wonder if there are other molecules or agents which when
    eaten or drunk can alter a Manufacturing Site. Asbestos is
    such an agent. If it is drunk or eaten or even breathed then
    the asbestos molecule does not make other asbestos molecules
    such as what Prusiner would like to have happen. Instead,
    the asbestos molecule alters the ManufacturingSite of a cell
    by its sharp point of cutting or altering a cell such that
    the cell then becomes cancerous. So in this example,
    asbestos is like a infectious prion in that it creates
    cancer disease from being eaten and thence alters the
    ManufacturingSite of a individual cell that creates more
    cancer cells.

    There are many variants of badprions. But in asbestos, many
    variants of cancer can result by the way in which the sharp
    point stabs the cell or what type of cell is stabbed. So the
    explanation of variants of CJD or other prion diseases is
    answered not by the Prusiner Model for it is deaf dumb and
    silent in regards to variants.

    But I wonder if the tau molecule associated to the
    betaamyloid in Alzheimers is acting like the bad-prion. I
    wonder if tau is contagious by drinking or eating.

    In Alzheimers there are 2 molecules involved. In Parkinsons
    there seems to be only 1 molecule. In Prion there are 2
    molecules.

    >
    > > However, there is some reservation about this. The
    > > protein is quite conserved among the mammals. This
    > > really suggests it is important. Yet deleting it is
    > > without (apparent) effect. Odd. In fact, some subtle
    > > neurological effects have been reported (for mice?).
    > > Maybe these are of significance.
    > >
    > > >The moment an animal body produces prions then that
    > > >animal is sick.
    > >
    > > Welllllll (and ignoring the posisble natural role,
    > > mentined above)... that might be a semantic point.
    > > Unless "somethign happens", no they do not seem to
    > > be sick.

    I disagree. If the mice and the cattle in the Kirin report
    are healthy by the absence of all prion proteins then these
    proteins are of no function whatsoever. And the presence of
    one single molecule of prions implies the animal is sick.

    The prescence of one single cancer cell in an animal
    body will create a fullblown cancer unless the body
    stops that cell.

    In CJD caused by eating infected meat, some prions have a
    better chance of gumming up the manufacturingsite.

    We do not argue that a cancer cell has some use or function
    in the animal body once it is created. We argue that unless
    that cancer cell is gotten rid of or stopped or killed that
    the cancer cell will multiply. It is that view that suggests
    itself on tau and betaamyloid and alphasynuclein. That the
    prescence of these proteins means the individual is sick
    with the disease.

    About the only great difference between Alzheimers,
    Parkinsons versus Prion is that it seems as though prion is
    the infectious disease, but researchers have never really
    investigated the extent to which Alzheimers and Parkinsons
    are infectious from person to person. It may be that the
    proteins involved in Alzheimers and Parkinsons do not
    survive as easily in the process of eating that prions do.
    But if a tau molecule or betaamyloid molecule or
    alphasynuclein molecule of a diseased individual were
    transferred to a healthy individual who then contracts the
    disease some months later would be proof that Alzheimers and
    Parkinsons is contagious just as Prion is contagious to a
    lesser degree admittedly.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  7. Bob

    Bob Guest

    On Wed, 02 Jun 2004 01:37:03 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >
    >Bob, do you know the people who claimed prion proteins had
    >some role in cell wall and whether claims like that are
    >debunked.

    No one has ever claimed that (mammalian) prions have
    anything to do with cell walls. That would make no sense.
    Animal cells do not have walls -- as we have noted before.

    I mention this partly as an example of a continuing problem
    with the discussion. You have this thing about making
    vituperative remarks about work you do not understand at all
    (with this cell wall point merely being one specific example
    at hand). It's fun to discuss science-in-progress, limits of
    current work and knowledge, alternatives, etc. But none of
    us here are in any position to make any real contribution to
    the field, and none of us can claim any great expertise that
    allows us to broadly disrespect well-accepted work. It also
    makes the discussion less fun.

    The prion protein is a membrane protein. That stands.
    Whether it has any function is an open question. It appears
    to be non-essential, by the test that deleting it leads to
    live and apparently normal animals. However, do not
    interpret that to mean it has no function. The test for "non-
    essential" means within the constraints of that test. There
    are many examples from microbes (easier to study!) where
    genes that appeared to be non-essential were later found to
    be essential under certain conditions. Further, a gene may
    be non-essential, but still have a role. There have been
    reports of some differences with prion-deficient mice. Not
    clear to me that any are well accepted.

    As noted before, the gene is highly conserved, which
    suggests (but does not prove) that it is there for a reason.

    BTW, as I understand it, the Kirin group has not yet
    actually created any real cows, only embryos at this point.
    Is that correct? If so, we lack info about whether there
    might be any effects on adult cows.

    (I am amused at this work on engineered cows being done at
    Kirin. If they are to develop novel cows, I would have
    thought they would try to make a cow that produces beer.)

    >
    >I think it is more important to focus on whether immunity

    let's try not to propagate that usage of immunity. As you
    know, an immunological approach to alz was tried -- with
    mixed results. What we are talking about here is
    susceptibility/resistance, not immunity.

    >for Alzheimers and Parkinsons is near at hand rather than
    >focus on details of Prion disease.

    ?? By the same approach? I doubt that all the underlying
    proteins are non-essential. (That means I do not know, but I
    suspect it is known.)

    And the approach used above is not really suitable for
    humans. (Though I suppose that "drug" treatments to reduce
    production of the protein might be within the general spirit
    of the same approach -- and might even work with an
    essential protein.)

    >It is the cross referencing of these Family Related
    >Diseases of Alzheimers, Parkinsons and Prion that I feel
    >takes priority over details of prion.
    >
    >One such cross reference is that in Prion disease we have
    >so called normal or good prions and then we have the
    >alleged "bad prion". In Alzheimers we have the tau and we
    >have the betaamyloid and we still are uncertain as to the
    >connection between tau and betaamyloid. But with the Kirin
    >report suggesting that all prion proteins are bad and that
    >any prion protein that shows up in animal bodies is a sign
    >that the disease is already existing. Suggests that in
    >Alzheimers that the moment one tau or one betaamyloid
    >molecule is found in an animal body, then that animal has
    >Alzheimers.
    >

    I am quite sure you will find that is known to be untrue.

    >
    >Bob, I feel if any of the above comments are correct in
    >part or in whole, then all three of these diseases of
    >Alzheimers, Parkinsons and Prion are brain diseases created
    >by malfunctioning manufacturing sites that spew out a
    >protein that the body does not need or want and thus the
    >disease is borne. All three are hereditary diseases
    >indicating that manufacturing sites gone awry are
    >genetically based. Prion is contagious by eating, but is it
    >a protein molecule that alters the shape of other protein
    >molecules? The Kirin report suggests otherwise.

    How so? It is exactly the result predicted by the prion
    model. (which does not mean that it could not also be
    predicted by some other model.)

    >
    >And if the Kirin report is accurate, then the tough problem
    >of assigning how much of the disease is production and how
    >much is due to body inability to remove unwanted waste
    >proteins is answered. In cancer we do not ask why the body
    >cannot remove the cancer cells.

    We most certainly do! Elimination of small cancers by
    the immune system is still thought to be important, so
    far as I know.

    bob
     
  8. Sun, 06 Jun 2004 20:32:09 -0700 Bob wrote:

    > On Wed, 02 Jun 2004 01:37:03 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >
    > >Bob, do you know the people who claimed prion proteins
    > >had some role in cell wall and whether claims like that
    > >are debunked.
    >
    > No one has ever claimed that (mammalian) prions have
    > anything to do with cell walls. That would make no sense.
    > Animal cells do not have walls -- as we have noted before.

    Perhaps it was prions in yeast and yeast cell wall so that
    idea got transfered to animal cell wall or membrane.

    >
    >
    > I mention this partly as an example of a continuing
    > problem with the discussion. You have this thing about
    > making vituperative remarks about work you do not
    > understand at all (with this cell wall point merely being
    > one specific example at hand). It's fun to discuss science-in-
    > progress, limits of current work and knowledge,

    I admit there is much that I do not know and one of the
    reasons I post to the Internet is to bridge that unknown.

    As for the vituperation, I admit that also and it is more
    irrational than rational but it must provide some sort of
    energy to continue for it cannot be 100% bad, otherwise we
    would be robots or automotons doing science.

    >
    > alternatives, etc. But none of us here are in any position
    > to make any real contribution to the field, and none of us
    > can claim any great expertise that allows us to broadly
    > disrespect well-accepted work. It also makes the
    > discussion less fun.

    I beg to differ. Granted we are not "hands on into prion
    research or Alzheimers or Parkinsons", however, we can
    contribute to the LOGICS of these sciences by being off-to-the-side-
    thinkers. Those researchers and scientists directly in the
    field of study often have a small field of vision of their
    work and are unable to put the pieces into a broad
    perspective.

    Case in point is Fusion Engineering where only those that
    dogmatically believe that a machine can reach breakeven and
    surpass breakeven are allowed to do JET and now ITER. A
    scientist that believes and has data showing that Fusion is
    impossible to reach breakeven is flunked out of all programs
    dealing with Fusion.

    Another Case in point is Stonethrowing theory in
    Anthropology. Those in the field believe in Darwin's
    Savannah or hybrid Savannah for bipedalism. None of them
    believe that Stonethrowing preceded bipedalism and created
    bipedalism. None of them believe that Stonethrowing is the
    difference between being human and being an ape.
    Anthropology is so clubhouse of a science that the owners of
    the bones of prehumans dating back to Oreopithecus and
    further back are not allowed to be examined for
    Stonethrowing evidence.

    My point Bob is that people on the side who think
    Theoretically about these problems can often make a larger
    contribution than the people inside working on these
    problems because of LOGICS and unfettered and no constraints
    as to thoughts.

    People on the inside of a science subject are pushed and
    pulled by a large organization that put them there and this
    organization is what is going to shape their thoughts, their
    actual research and their reporting of what their research
    uncovered.

    People on the outside thinking about these problems not only
    can have a better LOGIC but can even steer the people on the
    inside because these outsiders are independent of politics,
    of money, of personality clashes of a organization.

    People on the outside have really just one major motivator--
    get the truth. Whereas people on the inside have their
    jobs to think about and truth is just one element on a
    line of many.

    >
    >
    > The prion protein is a membrane protein. That stands.
    > Whether it has any function is an open question. It
    > appears to be non-essential, by the test that deleting it
    > leads to live and apparently normal animals.

    You said it Bob. Now take the Logical step by saying that
    there is no normal or good prion. All prions are diseased.
    And that the moment a person has a single prion, whether bad
    PrP or whether a alleged good form of prion has the disease.

    The Prusiner Model is dependent on there being a good
    form of prion and a bad form of prion. The Prusiner
    Model is dependent on the good form of prion to be of a
    bodily function that is produced continually by the body
    in all ages.

    When we find out that the prion molecule is nonessential
    in all forms of the molecule Logically tells us that all
    prion molecules are a sign of a disease and the moment
    one is detected in an animal brain means the animal has
    the disease.

    >
    > However, do not interpret that to mean it has no function.
    > The test for "non-essential" means within the constraints
    > of that test. There

    My major contribution to these discussions over the years is
    that I feel it is to lump a new disease into a old class of
    Family Related Diseases and via this Methodology, one begins
    to develop a Model of that particular disease relative to
    the Family Related diseases.

    I do not call it vituperation, Bob, although I can
    sympathesize with the accusation, to say that in 1970s or
    1980s that Mr. Prusiner should not have isolated his Prion
    disease as a "unique disease" and constructed a Model around
    it just from ruminations of prions. Instead, Mr. Prusiner
    should have said to himself, what Family RElated Diseases
    exists similar to Prion? He would have said Alzheimers and
    Parkinsons and lumped them together as a class of diseases
    for which no model yet exists. He would not have theorized a
    Prusiner Model because the understanding of Alzheimers and
    Parkinsons was even more primitive than prion in the 1970s
    and 1980s. In fact, one can say that not until the late
    1990s up to 2004 has some light been shed on Alzheimers and
    Parkinsons.

    So, Bob, the Prusiner Model invented decades ago is more of
    a handicapp and thwarting of the field of disease, because
    it was so premature and it is having a harmful affect on
    understanding of prion disease. This is an assessment and
    hope Bob does not see it as vituperation.

    Mr. Prusiner was a lone-wolf in the 1980s when he acted to
    come upon his prion model. What I am saying is that if
    he had acted better, he would have adopted a Methodology
    that was not lone-wolfish. The Methodology that when you
    encounter a new disease, never before investigated, that
    we do not saddle this new disease with "new mechanisms
    and novel features". Instead, as responsible scientists,
    we adopt the Methodology that first we find a Family
    RElated Class of Diseases for which we then place this
    new disease into that category. We then feed off of the
    interrelations and analogies and similarities between
    those diseases. Only after such a Methodology of Family
    Related do we then construct a Model as to how that
    particular disease is working.

    Ms. Prusiner was a lone-wolf and his Prion Model is a lone
    wolf model and I feel that it is hindering science and
    not helping.

    >
    > are many examples from microbes (easier to study!) where
    > genes that appeared to be non-essential were later found
    > to be essential under certain conditions. Further, a gene
    > may be non-essential, but still have a role. There have
    > been reports of some differences with prion-deficient
    > mice. Not clear to me that any are well accepted.

    Bob, you have carped at me often for not accepted the facts
    and data. It seems on the issue of "prion protein
    nonessentialness" that you yourself is not accepting of the
    data that it is nonessential.

    >
    >
    > As noted before, the gene is highly conserved, which
    > suggests (but does not prove) that it is there for a
    > reason.

    When the mouse that has no prion production and not the
    Kirin cow that has no prion production should be enough of a
    "proof" that prion proteins are nonessential. The logical
    next step is that Prion disease exists when one single prion
    protein is manufactured in a animal body.

    >
    >
    > BTW, as I understand it, the Kirin group has not yet
    > actually created any real cows, only embryos at this
    > point. Is that correct? If so, we lack info about whether
    > there might be any effects on adult cows.
    >
    > (I am amused at this work on engineered cows being done at
    > Kirin. If they are to develop novel cows, I would have
    > thought they would try to make a cow that produces beer.)
    >
    > >
    > >I think it is more important to focus on whether immunity
    >
    > let's try not to propagate that usage of immunity. As you
    > know, an immunological approach to alz was tried -- with
    > mixed results. What we are talking about here is
    > susceptibility/resistance, not immunity.

    I think we use these terms not so much for precision or
    clarity but for ease. The word disease itself is overused
    but it does not stopp us.

    >
    > >for Alzheimers and Parkinsons is near at hand rather than
    > >focus on details of Prion disease.
    >
    > ?? By the same approach? I doubt that all the underlying
    > proteins are non-essential. (That means I do not know, but
    > I suspect it is known.)
    >

    This is the Methodology in action. We have a question as to
    Prion disease and we immediately transpose that question
    onto Alzheimers and Parkinsons and then try to glean a
    meaningful answer. It all prion molecules are useless and
    nonessential would imply that tau and betaamyloid in
    Alzheimers and alphasynuclein in Parkinsons are also
    nonessential. Apparently Bob knows of no case where tau or
    betaamyloid or alphasynuclein exists in a normal healthy
    body doing some useful and purposeful work. These molecules
    exist only in a diseased body.

    This is what I mean Bob, by saying let the Methodology
    figure out the Model for the disease, not a thousand
    scientists isolated in their corners with thousands of
    different viewpoints.

    Let Alzheimers and Parkinsons help solve the Prion Model.
    Let Prion and Parkinsons help solve the Alzheimers Model.
    etc etc. Get away from the thousands of lone-wolf scientists
    eager with their lone-wolf model.

    >
    > And the approach used above is not really suitable for
    > humans. (Though I suppose that "drug" treatments to reduce
    > production of the protein might be within the general
    > spirit of the same approach -- and might even work with an
    > essential protein.)
    >
    > >It is the cross referencing of these Family Related
    > >Diseases of Alzheimers, Parkinsons and Prion that I feel
    > >takes priority over details of prion.
    > >
    > >One such cross reference is that in Prion disease we have
    > >so called normal or good prions and then we have the
    > >alleged "bad prion". In Alzheimers we have the tau and we
    > >have the betaamyloid and we still are uncertain as to the
    > >connection between tau and betaamyloid. But with the
    > >Kirin report suggesting that all prion proteins are bad
    > >and that any prion protein that shows up in animal bodies
    > >is a sign that the disease is already existing. Suggests
    > >that in Alzheimers that the moment one tau or one
    > >betaamyloid molecule is found in an animal body, then
    > >that animal has Alzheimers.
    > >
    >
    > I am quite sure you will find that is known to be untrue.

    Well, a qualified assertion of a minimum amount of the
    protein to make the disease confirmed. In the case of
    cancer, theoretically one cancer cell can lead to the
    disease but often the body removes the cancer so that it
    does not become established. So let us say a minimum set of
    protein molecules. And theoretically, it takes just one
    protein molecule to have the disease of Alzheimers,
    Parkinsons, Prion.

    >
    >
    > >
    > >Bob, I feel if any of the above comments are correct in
    > >part or in whole, then all three of these diseases of
    > >Alzheimers, Parkinsons and Prion are brain diseases
    > >created by malfunctioning manufacturing sites that spew
    > >out a protein that the body does not need or want and
    > >thus the disease is borne. All three are hereditary
    > >diseases indicating that manufacturing sites gone awry
    > >are genetically based. Prion is contagious by eating, but
    > >is it a protein molecule that alters the shape of other
    > >protein molecules? The Kirin report suggests otherwise.
    >
    > How so? It is exactly the result predicted by the prion
    > model. (which does not mean that it could not also be
    > predicted by some other model.)

    Well, no. The Prusiner Model predicts bad proteins altering
    good proteins. Alzheimers and Parkinsons imply that the body
    itself is pumping out proteins that it cannot rid itself.
    That means the Prion disease is more like Alzheimers and
    Parkinsons than it is according to anything said in the
    tenets of the Prusiner Model. About the only feature of the
    Prusiner Model that is truthful is the contagious aspect,
    for there is ample evidence of a contagious factor, but all
    the other tenets of the Prusiner Model are probably
    falsehoods.

    It is still unknown as to whether Alzheimers and Parkinsons
    are contagious and if not, why not. Perhaps the prion
    protein is so less complex than tau or betaamyloid or
    alphasynuclein that it can survive transfer by eating
    whereas the complex proteins of Alzheimers and Parkinsons
    cannot survive a transfer, but if transfered artificially by
    a researcher, then perhaps these diseases are also
    contagious just as prion is.

    >
    >
    > >
    > >And if the Kirin report is accurate, then the tough
    > >problem of assigning how much of the disease is
    > >production and how much is due to body inability to
    > >remove unwanted waste proteins is answered. In cancer we
    > >do not ask why the body cannot remove the cancer cells.
    >
    > We most certainly do! Elimination of small cancers by
    > the immune system is still thought to be important, so
    > far as I know.
    >
    > bob

    In all of these years of discussion, Bob, it is not a matter
    of who is vituperative but a matter of learning and of
    interest in the subject. Not a matter of not being a hands
    on worker in a lab of these proteins for a on the sidelines
    Logic can contribute. And it is those on the sidelines who
    can step back away from the organization and contribute
    immensely to the Logics of the science.

    I have invested over 7 years of my time on Prion and
    Alzheimers and Parkinsons and am in no mood to quit now.

    If nothing else, I have contributed the idea that the key to
    understanding Prion is by cross examining Alzheimers and
    Parkinsons as a Family Related Class of diseases. If I
    happen to step on Mr. Prusiners toes in reaching for the
    goal of understanding, so be it.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  9. Sun, 06 Jun 2004 20:32:09 -0700 Bob wrote:

    > On Wed, 02 Jun 2004 01:37:03 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >
    > >Bob, do you know the people who claimed prion proteins
    > >had some role in cell wall and whether claims like that
    > >are debunked.
    >
    > No one has ever claimed that (mammalian) prions have
    > anything to do with cell walls. That would make no sense.
    > Animal cells do not have walls -- as we have noted before.
    >
    > I mention this partly as an example of a continuing
    > problem with the discussion. You have this thing about
    > making vituperative remarks about work you do not
    > understand at all (with this cell wall point merely being
    > one specific example at hand). It's fun to discuss science-in-
    > progress, limits of current work and knowledge,
    > alternatives, etc. But none of us here are in any position
    > to make any real contribution to the field, and none of us
    > can claim any great expertise that allows us to broadly
    > disrespect well-accepted work. It also makes the
    > discussion less fun.
    >
    > The prion protein is a membrane protein. That stands.
    > Whether it has any function is an open question. It
    > appears to be non-essential, by the test that deleting it
    > leads to live and apparently normal animals. However, do
    > not interpret that to mean it has no function. The test
    > for "non-essential" means within the constraints of that
    > test. There are many examples from microbes (easier to
    > study!) where genes that appeared to be non-essential were
    > later found to be essential under certain conditions.
    > Further, a gene may be non-essential, but still have a
    > role. There have been reports of some differences with prion-
    > deficient mice. Not clear to me that any are well
    > accepted.
    >

    As I said earlier, these discussions for the last 7 years
    lend and contribute to the Logic behind the Disease Model.
    And Bob is correct in saying that neither one of us can
    contribute to the details because we are not lab researchers
    involved with prion proteins or Alzheimer or Parkinson
    proteins, what we can contribute is the logic and
    commonsense of it all.

    And to give an example by using Mr. Bob Bruner himself. I
    have only recently been made aware that all prion proteins
    of whatever variety or type are nonessential. I had thought
    until June of 2004 that prions are routinely produced in
    healthy animal bodies and have a key function or role. Then
    the Kirin report of bioengineering a cow that can never
    produce prion proteins comes along. I never really
    understood that about the mouse bioengineering. Apparently
    Bob knew of it when the mouse was reported in the science
    journals. So, apparently Bob knew about the nonessentialness
    of all prion proteins many years ago, whereas I come to
    learn about the nonessentialness only a matter of a few
    weeks ago.

    So, with the fact of Nonessentialness of any and all types
    of prion proteins, why did not Mr. Bob Bruner then take the
    logical steps forward years ago. Why did not Mr. Bruner
    question the Prusiner Model for it is convoluted to think
    that there is a good prion and a bad prion and that when a
    person eats enough bad prions that they will then begin to
    alter the shape of the good-prions to become more bad-
    prions. But Mr. Bruner had the mouse data implying that all
    prions are nonessential. So why did not Mr. Bruner take the
    logical steps and say that the Prusiner Model is convoluted
    in that it assumes a store supply of good-prions already
    existing in the body in order for the bad-prions to work
    upon. The straight logic would say that since all prions are
    nonessential that the animal is already sick if it has good
    prions and the animal is on the way to dying regardless if
    it ever gets a bad-prion into the body. Just the buildup of
    good-prions is the disease in progress.

    Mr. Bruner should have then really questioned the Prusiner
    Model for it is dependent on animal bodies having good
    prions which are useful and needed and have a plenty
    store of them and that the disease comes into
    existence once a bad-prion is introduced into this
    environment of loads of good-prions waiting to be
    altered by the bad prions.

    I wish I had known of the Nonessentialness of all prions
    when the mouse report came out for then I would have
    launched this logic, hopefully, soon thereafter.
    Unfortunately, I learned of the nonessentialness via the
    Kirin cow report of a few weeks ago.

    The message and theme I want to hammer and hammer is that we
    are best as scientists of medicine when we construct a Model
    or theory of a disease only after placing a novel new
    disease into a Family Related Group of Diseases. Mr.
    Prusiner, if he had been wiser, would have not constructed a
    Model of prion disease in the 1980s (or whenever he did so)
    but instead had placed prion disease into the Family of
    Diseases that contained Alzheimers and Parkinsons and
    through the ensuing years would have borrowed the
    similarities and analogies and details of one compared to
    the other two and only after finding a confident

    mechanism of how these 3 diseases really work to transpose
    that model onto the other disease.

    For example, it appears that prion does have variants or
    types of prion proteins. But Alzheimers has not just amyloid
    proteins but also tau proteins. Yet we still do not know
    what relationship tau has with amyloid in Alzheimers.
    Likewise in Prion we have two or more prion variants. So in
    Mr. Prusiners model to say that PrP alters the shape of
    other prion proteins is rather ridiculous of a claim
    considering that in Alzheimers there are tau and amyloid and
    commonsense logic shows that tau is not altering shape of
    amyloid or vice versa.

    What is clear is that tau and amyloid in Alzheimers and
    alphasynuclein in Parkinsons and all types of prions are all
    useless and nonessential in animal bodies. That implies that
    the disease begins when any of these proteins are detected
    in small quantity.

    To tell if a person has Alzheimers, all we need do is detect
    any tau or amyloid present. For Parkinsons, to detect a
    small amount of alphasynuclein.

    So, Bob is wrong when he says that neither one of us is in a
    position to contribute to these diseases. And Bob clearly
    shows a lack of logic for the past several years starting
    with the bioteched mouse that was engineered never to
    manufacture a prion molecule. I failed to understand that
    mouse, but Bob understood it. But Bob then failed to put
    Logic to that mouse.

    If Bob had put Logic to that mouse instead of me putting
    logic to the Kirin cow, then maybe Bob would be advancing
    the progress of understanding these 3 diseases.

    >
    >
    > >
    > >Bob, I feel if any of the above comments are correct in
    > >part or in whole, then all three of these diseases of
    > >Alzheimers, Parkinsons and Prion are brain diseases
    > >created by malfunctioning manufacturing sites that spew
    > >out a protein that the body does not need or want and
    > >thus the disease is borne. All three are hereditary
    > >diseases indicating that manufacturing sites gone awry
    > >are genetically based. Prion is contagious by eating, but
    > >is it a protein molecule that alters the shape of other
    > >protein molecules? The Kirin report suggests otherwise.
    >
    > How so? It is exactly the result predicted by the prion
    > model. (which does not mean that it could not also be
    > predicted by some other model.)
    >

    Bob has accused me of vituperation. I plead guilty.
    Guilty because scientists hate to be found lacking on
    points of logic.

    Example: even though there is substantial evidence that all
    prion molecules are nonessential in animal bodies, Bob still
    does not accept that data because it undermines the Prusiner
    Model. So apparently Bob is more interested in bulwarking
    the Prusiner Model than in accepting hard data that
    undermines the Prusiner Model. And when I point out these
    logical gaps of the Prusiner Model or the logical gaps of
    Mr. Bob Bruner, then I am called out as vituperative.

    IMportant Exploration: I do not dispute that prion molecules
    when eaten are contagious and can lead to a form of CJD or
    prion disease. The only tenet in the Prusiner Model that is
    true is the contagiousness of eaten prion molecules. But the
    other tenets of the Prusiner Model such as the bad-prion
    altering the shape of good-prions is ridiculous in the
    biotech mouse and now the Kirin cow. So that leaves the
    Logic that it is the manufacturing sites of proteins in the
    brain that is corrupted to the point where the brain is
    spewing out more prions or more amyloid or tau in Alzheimers
    or more alphasynuclein in Parkinsons. So the important
    question is can the mere presence of a protein *induce or
    incite* the body to produce more proteins similar to that
    one? If we planted a amyloid or tau protein in a brain that
    is free of those proteins, will the brain somehow become
    corrupted to spew out more of those proteins? Unlike the
    Prusiner Model of proteins changing similar proteins, in the
    Manufacturing Site Gone Awry Model, it is the mere presence
    or introduction of a foreign protein that somehow gums up
    the site to spew out more.

    I know the immune system has a sort of *copycat or Xerox or
    photocopy capacity". What I am looking for is how a healthy
    body begins to spew out copies of a protein that was
    introduced into the body.

    The Prusiner Model is wrong because it would suggest that
    there are 2 forms of alphasynuclein and the one form is
    essential and the other is a bad form that alters the shape
    of good-alphasynuclein. Likewise for Alzheimers. Instead,
    the better model or theory is that protein manufacturing
    sites have gone heywire and pumping out these nonessential
    proteins that fill the brain and kill the animal.

    The mistake Mr. Bruner is making is that he is failing to
    ever apply Logic to the data, and instead has taken a sort
    of hero-worship of Mr. Prusiner and his model. And the
    moment I show the huge cracks in the Prusiner Model, then I
    am called out as vituperative and never able to contribute.
    The mistake Mr. Bruner has made is that he abandons logic
    over that of hero worship.

    I am not mad at Bob, and hopes he continues in this
    discussion. It will take months and years for the 3 diseases
    of Alzheimers, Parkinsons, Prion to feed off of one another
    and finally solve their mechanisms and inner workings.

    And I hope most scientists can be honest with themselves by
    saying the Prusiner Model is wrong and abandon it because
    all scientists should lean on the pole of Logic and not that
    ugly pole of hero worship or fame seekers.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  10. Bob

    Bob Guest

    On Mon, 07 Jun 2004 12:27:33 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >
    >Perhaps it was prions in yeast and yeast cell wall so that
    >idea got transfered to animal cell wall or membrane.
    >

    The yeast prions are all cytoplasmic, I think.

    >As for the vituperation, I admit that also and it is more
    >irrational than rational but it must provide some sort of
    >energy to continue for it cannot be 100% bad, otherwise we
    >would be robots or automotons doing science.
    >

    But it can be pleasant. I often find it helps to save draft
    messages and edit them a little later.

    In the case of prion model, there is much still to be
    learned, but that does not disparage the basic prion model
    (and Prusiner's contribution). It is clear that there is
    more to mammalian prions than the simple Prusiner model.
    OTOH, all elements of that model have been basically
    validated. So, the story is incomplete. Normal science.
    Ideas evolve. The incompleteness is not particularly a
    criticism of the original model; that model addressed the
    issue of that time (which was mainly the virus or not
    question). There is no reason to suggest that the model need
    be abandoned (as distinct from being adjusted/updated).

    >>
    >> alternatives, etc. But none of us here are in any
    >> position to make any real contribution to the field, and
    >> none of us can claim any great expertise that allows us
    >> to broadly disrespect well-accepted work. It also makes
    >> the discussion less fun.
    >
    >I beg to differ. Granted we are not "hands on into prion
    >research or Alzheimers or Parkinsons", however, we can
    >contribute to the LOGICS of these sciences by being off-to-the-side-
    >thinkers. Those researchers and scientists directly in the
    >field of study often have a small field of vision of their
    >work and are unable to put the pieces into a broad
    >perspective.
    >

    Yes, perhaps. But only if someone relevant reads it, and
    finds it thought provoking. Not too likely. My main point is
    to not get too upset at what others choose to do.

    >
    >>
    >>
    >> The prion protein is a membrane protein. That stands.
    >> Whether it has any function is an open question. It
    >> appears to be non-essential, by the test that deleting it
    >> leads to live and apparently normal animals.
    >
    >You said it Bob.

    But, but, but. See below.

    >Now take the Logical step by saying that there is no normal
    >or good prion. All prions are diseased. And that the moment
    >a person has a single prion, whether bad PrP or whether a
    >alleged good form of prion has the disease.
    >
    >The Prusiner Model is dependent on there being a good
    >form of prion and a bad form of prion. The Prusiner
    >Model is dependent on the good form of prion to be of a
    >bodily function that is produced continually by the body
    >in all ages.
    >

    Not really. All it requires is that the protein be present
    (or perhaps, is being actively made). It makes no
    assumptions/demands about the role of PrC.

    The adjectives good/bad are for our convenience, and are
    not inherent in the model. In yeast, the converted protein
    is "good". At its heart, the prion model is about protein
    conformational conversion; per se it is not about disease
    or good/bad.

    >When we find out that the prion molecule is nonessential
    >in all forms of the molecule Logically tells us that all
    >prion molecules are a sign of a disease and the moment
    >one is detected in an animal brain means the animal has
    >the disease.
    >
    >>
    >> However, do not interpret that to mean it has no
    >> function. The test for "non-essential" means within the
    >> constraints of that test. There
    >
    >My major contribution to these discussions over the years
    >is that I feel it is to lump a new disease into a old class
    >of Family Related Diseases and via this Methodology, one
    >begins to develop a Model of that particular disease
    >relative to the Family Related diseases.
    >
    >I do not call it vituperation, Bob, although I can
    >sympathesize with the accusation, to say that in 1970s or
    >1980s that Mr. Prusiner should not have isolated his Prion
    >disease as a "unique disease" and constructed a Model
    >around it just from ruminations of prions. Instead, Mr.
    >Prusiner should have said to himself, what Family RElated
    >Diseases exists similar to Prion? He would have said
    >Alzheimers and Parkinsons and lumped them together as a
    >class of diseases for which no model yet exists.

    I doubt that that grouping would have been apparent at
    that time.

    But... it is one thing to say that these diseases are
    showing signs of similarity with respect to role of
    protein aggregation, but that does not mean that there is
    any similarity in how the culprit protein is made. Those
    are essentially independent modules. The prion model does
    not (attempt to) explain how the protein is pathogenic.
    Comparative studies of the several neurodegenerative
    diseases that seem to involve protein aggregates will feed
    each other. How much similarity they have in pathogenesis
    remains to be seen. But origin of the protein is a
    distinct question.

    >
    >So, Bob, the Prusiner Model invented decades ago is more of
    >a handicapp and thwarting of the field of disease, because
    >it was so premature and it is having a harmful affect on
    >understanding of prion disease. This is an assessment and
    >hope Bob does not see it as vituperation.

    What the prion model tried to do was to explain how a "pure-
    protein" which seemed to act as an infectious agent could do
    so. This seemed to violate the role of (need for) nucleic
    acids. When it became understood that the gene for this
    protein was a host gene, that problem was eliminated. The
    "cost" was the role of protein conformational conversion.
    While in general terms this was reasonable, the specifics
    were novel. But now all of the issues of the model have been
    shown to hold -- though not specifically for mammalian
    prions. There is circumstantial evidence which would suggest
    it holds there, but evidence for conversion is lacking. So
    this remains open for further testing. But, as you have
    noted, it may be more interesting at this point to worry
    about how the protein causes its ill effect than about
    exactly how it is produced.

    So, everything Prusiner said has been shown to be true --
    but we are still not sure exactly what is happening with the
    mammalian prions.

    How conversion occurs, including possible involvement of
    other factors and possible requirement that it be done at a
    particular step, are open. So is the issue of pathogenesis,
    but that is a separate question. Conversion is apparently
    elusive, and the exptal system is more complex to study.

    With some reservation (BSE, CWD), prion diseases are the
    least common/important of these various
    neurodegenerative diseases.

    It may well be that exploration of possible drugs will be
    where useful info comes from.

    >
    >Mr. Prusiner was a lone-wolf in the 1980s when he acted to
    > come upon his prion model. What I am saying is that if
    > he had acted better, he would have adopted a
    > Methodology that was not lone-wolfish. The Methodology
    > that when you encounter a new disease, never before
    > investigated, that we do not saddle this new disease
    > with "new mechanisms and novel features".

    He was faced with a novel feature -- "transmission" by
    a protein.

    >
    >>
    >> are many examples from microbes (easier to study!) where
    >> genes that appeared to be non-essential were later found
    >> to be essential under certain conditions. Further, a gene
    >> may be non-essential, but still have a role. There have
    >> been reports of some differences with prion-deficient
    >> mice. Not clear to me that any are well accepted.
    >
    >Bob, you have carped at me often for not accepted the facts
    >and data. It seems on the issue of "prion protein
    >nonessentialness" that you yourself is not accepting of the
    >data that it is nonessential.

    First, there is nothing inherent in the prion model that the
    host protein does or does not have any particular function.
    So this is really an irrelevant issue -- except as it
    relates to the question of whether or not deleting the host
    prion gene will really be an acceptable solution to the
    prion disease problem.

    Second, we need to be careful with our terms. (non)Essential
    has a very specific meaning. A protein may be non-essential,
    yet still be important or useful. In fact, it may even be
    essential if a more complete test of essentiality were done
    -- a well known and understood situation.

    Third, it is not me but the community that has reservations
    about the (lack of) role of normal prion protein. That the
    gene is highly conserved certainly suggests that it is there
    for a reason. I am not in any position to judge the reports
    showing some role for it, so I just leave it as open -- esp
    since it really doesn't matter (though it certainly is
    interesting).

    >
    >>
    >>
    >> As noted before, the gene is highly conserved, which
    >> suggests (but does not prove) that it is there for a
    >> reason.
    >
    >When the mouse that has no prion production and not the
    >Kirin cow that has no prion production should be enough of
    >a "proof" that prion proteins are nonessential.

    See above. Key points are that... that does not mean it does
    not have an important function, and that it really doesn’t
    matter anyway.

    [ As noted in previous msg, not sure the Kirin cow actually
    exists yet (??). ]

    >The logical next step is that Prion disease exists when one
    >single prion protein is manufactured in a animal body.

    Why? It is a normal protein, found in neuron cells of all
    higher animals.

    >
    >>
    >> >for Alzheimers and Parkinsons is near at hand rather
    >> >than focus on details of Prion disease.
    >>
    >> ?? By the same approach? I doubt that all the underlying
    >> proteins are non-essential. (That means I do not know,
    >> but I suspect it is known.)
    >>
    >
    >This is the Methodology in action. We have a question as to
    >Prion disease and we immediately transpose that question
    >onto Alzheimers and Parkinsons and then try to glean a
    >meaningful answer. It all prion molecules are useless and
    >nonessential

    which is questionable at best

    >would imply that tau and betaamyloid in Alzheimers and
    >alphasynuclein in Parkinsons are also nonessential.

    which is, I am fairly sure, known to be not true.

    Anyway, so what? Whether the normal protein is good, bad or
    indifferent has nothing to do with the disease.

    (Sickle cell is a nice example of a single protein being
    both good and bad.)

    >Apparently Bob knows of no case where tau or betaamyloid or
    >alphasynuclein exists in a normal healthy body doing some
    >useful and purposeful work. These molecules exist only in a
    >diseased body.

    That I do not know is not very relevant. (I have not made
    any particular effort to find out -- and/or do not
    remember if I have come across anything.) There are lots
    of protein whose function is not known. Most proteins. As
    noted earlier, there was a recent report on the normal
    function of AB.

    I assume that they exist for a reason -- though of course
    that may not be true in any specific case. And even if there
    was a test for essentiality (I do not know that for these),
    that does not say they do not have a role.

    >> >
    >> >Bob, I feel if any of the above comments are correct in
    >> >part or in whole, then all three of these diseases of
    >> >Alzheimers, Parkinsons and Prion are brain diseases
    >> >created by malfunctioning manufacturing sites that spew
    >> >out a protein that the body does not need or want and
    >> >thus the disease is borne. All three are hereditary
    >> >diseases indicating that manufacturing sites gone awry
    >> >are genetically based. Prion is contagious by eating,
    >> >but is it a protein molecule that alters the shape of
    >> >other protein molecules? The Kirin report suggests
    >> >otherwise.
    >>
    >> How so? It is exactly the result predicted by the prion
    >> model. (which does not mean that it could not also be
    >> predicted by some other model.)
    >
    >Well, no.

    Well, yes. The prion model has the host gene for the protein
    is essential to have disease. Delete the host gene, and you
    cannot have the disease. That is exactly what the data says.
    There may be some other model that also makes that
    prediction, but the deletion test is exactly in agreement
    with the prion model.

    >The Prusiner Model predicts bad proteins altering good
    >proteins.

    good proteins made by the host -- thus predicting that
    the host gene for that protein is required in order to
    have disease.

    bob
     
  11. Bob

    Bob Guest

    On Wed, 09 Jun 2004 02:39:47 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >
    >And to give an example by using Mr. Bob Bruner himself. I
    >have only recently been made aware that all prion proteins
    >of whatever variety or type are nonessential.

    That is not a valid conclusion.

    >I had thought until June of 2004 that prions are routinely
    >produced in healthy animal bodies

    they are

    >and have a key function or role.

    they may, perhaps depending on what key means.

    >Then the Kirin report of bioengineering a cow that can
    >never produce prion proteins comes along.

    Again, let's be cautious here. The cow does not yet exist,
    as I understand it. It is merely an embryo at this point. So
    it remains to be seen how normal the cow is.

    >I never really understood that about the mouse
    >bioengineering. Apparently Bob knew of it when the mouse
    >was reported in the science journals. So, apparently Bob
    >knew about the nonessentialness of all prion proteins many
    >years ago, whereas I come to learn about the
    >nonessentialness only a matter of a few weeks ago.
    >
    >So, with the fact of Nonessentialness of any and all types
    >of prion proteins, why did not Mr. Bob Bruner then take the
    >logical steps forward years ago. Why did not Mr. Bruner
    >question the Prusiner Model for it is convoluted to think
    >that there is a good prion and a bad prion and that when a
    >person eats enough bad prions that they will then begin to
    >alter the shape of the good-prions to become more bad-
    >prions. But Mr. Bruner had the mouse data implying that all
    >prions are nonessential. So why did not Mr. Bruner take the
    >logical steps and say that the Prusiner Model is convoluted
    >in that it assumes a store supply of good-prions already
    >existing in the body in order for the bad-prions to work
    >upon. The straight logic would say that since all prions
    >are nonessential that the animal is already sick if it has
    >good prions and the animal is on the way to dying
    >regardless if it ever gets a bad-prion into the body. Just
    >the buildup of good-prions is the disease in progress.
    >

    Simple enough. The role of the normal cellular prion protein
    is of NO relevance in the prion model. Further, we do not
    know what the role
    is. Even with one sign pointing to it being "non-essential",
    that does not mean it is not important. This is
    discussed more in msg sent earlier this evening.

    So your premise is both irrelevant and factually
    questionable, so there is no need to proceed with this line
    of argument.

    bob
     
  12. Wed, 09 Jun 2004 18:28:14 -0700 Bob wrote:

    > On Mon, 07 Jun 2004 12:27:33 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >
    > >Perhaps it was prions in yeast and yeast cell wall so
    > >that idea got transfered to animal cell wall or membrane.
    > >
    >
    > The yeast prions are all cytoplasmic, I think.
    >
    > >As for the vituperation, I admit that also and it is more
    > >irrational than rational but it must provide some sort of
    > >energy to continue for it cannot be 100% bad, otherwise
    > >we would be robots or automotons doing science.
    > >
    >
    > But it can be pleasant. I often find it helps to save
    > draft messages and edit them a little later.
    >
    > In the case of prion model, there is much still to be
    > learned, but that does not disparage the basic prion model
    > (and Prusiner's contribution). It is clear that there is
    > more to mammalian prions than the simple Prusiner model.
    > OTOH, all elements of that model have been basically
    > validated. So, the story is incomplete. Normal science.
    > Ideas evolve. The incompleteness is not particularly a
    > criticism of the original model; that model addressed the
    > issue of that time (which was mainly the virus or not
    > question). There is no reason to suggest that the model
    > need be abandoned (as distinct from being
    > adjusted/updated).
    >
    > >>
    > >> alternatives, etc. But none of us here are in any
    > >> position to make any real contribution to the field,
    > >> and none of us can claim any great expertise that
    > >> allows us to broadly disrespect well-accepted work. It
    > >> also makes the discussion less fun.
    > >
    > >I beg to differ. Granted we are not "hands on into prion
    > >research or Alzheimers or Parkinsons", however, we can
    > >contribute to the LOGICS of these sciences by being off-to-the-side-
    > >thinkers. Those researchers and scientists directly in
    > >the field of study often have a small field of vision of
    > >their work and are unable to put the pieces into a broad
    > >perspective.
    > >
    >
    > Yes, perhaps. But only if someone relevant reads it, and
    > finds it thought provoking. Not too likely. My main point
    > is to not get too upset at what others choose to do.
    >
    > >
    > >>
    > >>
    > >> The prion protein is a membrane protein. That stands.
    > >> Whether it has any function is an open question. It
    > >> appears to be non-essential, by the test that deleting
    > >> it leads to live and apparently normal animals.
    > >
    > >You said it Bob.
    >
    > But, but, but. See below.
    >
    > >Now take the Logical step by saying that there is no
    > >normal or good prion. All prions are diseased. And that
    > >the moment a person has a single prion, whether bad PrP
    > >or whether a alleged good form of prion has the disease.
    > >
    > >The Prusiner Model is dependent on there being a good
    > >form of prion and a bad form of prion. The Prusiner
    > >Model is dependent on the good form of prion to be of a
    > >bodily function that is produced continually by the body
    > >in all ages.
    > >
    >
    > Not really. All it requires is that the protein be present
    > (or perhaps, is being actively made). It makes no
    > assumptions/demands about the role of PrC.
    >
    > The adjectives good/bad are for our convenience, and are
    > not inherent in the model. In yeast, the converted protein
    > is "good". At its heart, the prion model is about protein
    > conformational conversion; per se it is not about disease
    > or good/bad.
    >
    > >When we find out that the prion molecule is nonessential
    > >in all forms of the molecule Logically tells us that all
    > >prion molecules are a sign of a disease and the moment
    > >one is detected in an animal brain means the animal has
    > >the disease.
    > >
    > >>
    > >> However, do not interpret that to mean it has no
    > >> function. The test for "non-essential" means within the
    > >> constraints of that test. There
    > >
    > >My major contribution to these discussions over the years
    > >is that I feel it is to lump a new disease into a old
    > >class of Family Related Diseases and via this
    > >Methodology, one begins to develop a Model of that
    > >particular disease relative to the Family Related
    > >diseases.
    > >
    > >I do not call it vituperation, Bob, although I can
    > >sympathesize with the accusation, to say that in 1970s or
    > >1980s that Mr. Prusiner should not have isolated his
    > >Prion disease as a "unique disease" and constructed a
    > >Model around it just from ruminations of prions. Instead,
    > >Mr. Prusiner should have said to himself, what Family
    > >RElated Diseases exists similar to Prion? He would have
    > >said Alzheimers and Parkinsons and lumped them together
    > >as a class of diseases for which no model yet exists.
    >
    > I doubt that that grouping would have been apparent at
    > that time.

    It would be interesting to me to go back and try to follow
    what the German, Mr. Alzheimer ever conjectured about his
    disease when he first discovered it. Whether he felt a need
    to provide a Model and mechanism for his disease. Whether he
    invoked viruses or bacteria. Whether he saw the inheritable
    Alzheimers.

    And likewise it would be interesting to follow the history
    of Parkinsons.

    In fact, that would make an excellent history of science for
    the next 50 years is to weave together the history of these
    3 diseases that should have been connected as a Family
    Related Group of diseases.

    >
    >
    > But... it is one thing to say that these diseases are
    > showing signs of similarity with respect to role of
    > protein aggregation, but that does not mean that there is
    > any similarity in how the culprit protein is made. Those
    > are essentially independent modules. The prion model does
    > not (attempt to) explain how the protein is pathogenic.
    > Comparative studies of the several neurodegenerative
    > diseases that seem to involve protein aggregates will feed
    > each other. How much similarity they have in pathogenesis
    > remains to be seen. But origin of the protein is a
    > distinct question.
    >
    > >
    > >So, Bob, the Prusiner Model invented decades ago is more
    > >of a handicapp and thwarting of the field of disease,
    > >because it was so premature and it is having a harmful
    > >affect on understanding of prion disease. This is an
    > >assessment and hope Bob does not see it as vituperation.
    >
    > What the prion model tried to do was to explain how a "pure-
    > protein" which seemed to act as an infectious agent could
    > do so. This seemed to violate the role of (need for)
    > nucleic acids. When it became understood that the gene for
    > this protein was a host gene, that problem was eliminated.
    > The "cost" was the role of protein conformational
    > conversion. While in general terms this was reasonable,
    > the specifics were novel. But now all of the issues of the
    > model have been shown to hold -- though not specifically
    > for mammalian prions. There is circumstantial evidence
    > which would suggest it holds there, but evidence for
    > conversion is lacking. So this remains open for further
    > testing. But, as you have noted, it may be more
    > interesting at this point to worry about how the protein
    > causes its ill effect than about exactly how it is
    > produced.
    >
    > So, everything Prusiner said has been shown to be true --
    > but we are still not sure exactly what is happening with
    > the mammalian prions.

    No, I would say the only thing Prusiner has said that has
    been shown true is that the protein has the ability to
    infect, or infectious agent. The entire Conversion aspect
    is doubtful. It may happen that once a prion enters the
    brain, a PrP forms a scissors. Call it a PrP scissors
    having compounded with other molecules to form a scissors
    and this scissors like the APP in Alzheimers cuts proteins
    and leaves fragments that form plaques. So the Prusiner
    Conversion is wrong.

    >
    >
    > How conversion occurs, including possible involvement of
    > other factors and possible requirement that it be done at
    > a particular step, are open. So is the issue of
    > pathogenesis, but that is a separate question. Conversion
    > is apparently elusive, and the exptal system is more
    > complex to study.
    >
    > With some reservation (BSE, CWD), prion diseases are the
    > least common/important of these various neurodegenerative
    > diseases.
    >

    Least important in terms of death rates and affliction
    numbers, but Prion disease maybe as important as Alzheimers
    or Parkinsons in answering the questions about all 3
    diseases. Because prion is rare, we do not want to put it on
    the backshelf because its theory may solve Alzheimers or
    Parkinsons faster than without.

    >
    > It may well be that exploration of possible drugs will be
    > where useful info comes from.
    >
    > >
    > >Mr. Prusiner was a lone-wolf in the 1980s when he acted
    > > to come upon his prion model. What I am saying is
    > > that if he had acted better, he would have adopted a
    > > Methodology that was not lone-wolfish. The
    > > Methodology that when you encounter a new disease,
    > > never before investigated, that we do not saddle this
    > > new disease with "new mechanisms and novel features".
    >
    > He was faced with a novel feature -- "transmission" by a
    > protein.

    I lived through that history as well as you did Bob and I
    suspect he was not faced with a novel feature but rather
    instead his personality to be a "maverick".

    Because Prusiner could have just said it was a "virus" too
    small to measure or a viral debris particle and I suspect
    that the state of resolution of CJD today would be about the
    same and perhaps better off. Because the legacy of Mr.
    Prusiner is a massive literature on yeast proteins. And Bob,
    you seem to like the word "irrelevant". I suspect in 50
    years from now when these diseases are resolved that the
    years spent from 1990-2004 with oceans of reports on yeast
    prions will all have been seen as a gigantic waste of time
    and irrelevant.

    Why could not Mr. Prusiner have acted like Mr. Alzheimer or
    Mr. Parkinson and realized that any model was going to end
    up being 90% wrong and the wise route was to let the world
    community of scientists solve the problem in the next 50 to
    100 years. If we checkout the history of Mr. Alzheimer and
    compare it to Mr. Prusiner, it is easy to spot the
    pretentious one.

    >
    >
    > >
    > >>
    > >> are many examples from microbes (easier to study!)
    > >> where genes that appeared to be non-essential were
    > >> later found to be essential under certain conditions.
    > >> Further, a gene may be non-essential, but still have a
    > >> role. There have been reports of some differences with
    > >> prion-deficient mice. Not clear to me that any are well
    > >> accepted.
    > >
    > >Bob, you have carped at me often for not accepted the
    > >facts and data. It seems on the issue of "prion protein
    > >nonessentialness" that you yourself is not accepting of
    > >the data that it is nonessential.
    >
    > First, there is nothing inherent in the prion model that
    > the host protein does or does not have any particular
    > function. So this is really an irrelevant issue -- except
    > as it relates to the question of whether or not deleting
    > the host prion gene will really be an acceptable solution
    > to the prion disease problem.

    Bob, I am afraid that I will always remember your name and
    associate one word and that of "irrelevant". Irrelevant is
    an important concept for science.

    Suppose in 50 years from now we cure Alzheimers and
    Parkinsons and Prion. And the cure is that we snip or
    delete or alter a few genes in the body at birth. Just like
    the Kirin cow. We delete the gene that makes amyloid/tau
    and thus the person will never contract Alzheimers. We
    delete the gene that makes alphasynuclein and thus the
    person never gets Parkinsons. We delete the gene that makes
    prion molecules and thus never worry about getting CJD. So,
    every person is like a Kirin cow by 2050 where we know
    which genes will cause Alzheimers Parkinsons and Prion and
    we delete them.

    If that comes true, that the cure is a Kirin cow procedure,
    then all facets of the Prusiner Model were wrong except for
    possible transmission. And it maybe that the PrP is not the
    infectious agent after all but that some viral-debris
    particle that is stuck with the PrP molecules is the
    infectious agent and thus the Prusiner Model is not just 90%
    wrong but a full 100% wrong.

    Bob, I think what you should be discussing about the
    Prusiner Model is not its features or tenets, but rather
    instead the amount of time, money and work put into yeast
    prions. Whereas Alzheimers has made great strides of real
    progress in the last 10 years.

    >
    >
    > Second, we need to be careful with our terms.
    > (non)Essential has a very specific meaning. A protein may
    > be non-essential, yet still be important or useful. In
    > fact, it may even be essential if a more complete test of
    > essentiality were done -- a well known and understood
    > situation.
    >
    > Third, it is not me but the community that has
    > reservations about the (lack of) role of normal prion
    > protein. That the gene is highly conserved certainly
    > suggests that it is there for a reason. I am not in any
    > position to judge the reports showing some role for it, so
    > I just leave it as open -- esp since it really doesn't
    > matter (though it certainly is interesting).
    >
    > >
    > >>
    > >>
    > >> As noted before, the gene is highly conserved, which
    > >> suggests (but does not prove) that it is there for a
    > >> reason.
    > >
    > >When the mouse that has no prion production and not the
    > >Kirin cow that has no prion production should be enough
    > >of a "proof" that prion proteins are nonessential.
    >
    > See above. Key points are that... that does not mean it
    > does not have an important function, and that it really
    > doesn’t matter anyway.
    >
    > [ As noted in previous msg, not sure the Kirin cow
    > actually exists yet (??). ]
    >
    > >The logical next step is that Prion disease exists
    > >when one single prion protein is manufactured in a
    > >animal body.
    >
    > Why? It is a normal protein, found in neuron cells of all
    > higher animals.
    >

    If the Kirin cow is normal is evidence that PrC is a disease
    molecule. If the prion free mouse is normal is evidence that
    any prion is a disease molecule. It makes no difference if
    it is PrC or PrP. A normal healthy animal is one that has 0
    amount of these proteins.

    >
    > >
    > >>
    > >> >for Alzheimers and Parkinsons is near at hand rather
    > >> >than focus on details of Prion disease.
    > >>
    > >> ?? By the same approach? I doubt that all the
    > >> underlying proteins are non-essential. (That means I do
    > >> not know, but I suspect it is known.)
    > >>
    > >
    > >This is the Methodology in action. We have a question as
    > >to Prion disease and we immediately transpose that
    > >question onto Alzheimers and Parkinsons and then try to
    > >glean a meaningful answer. It all prion molecules are
    > >useless and nonessential
    >
    > which is questionable at best
    >
    > >would imply that tau and betaamyloid in Alzheimers and
    > >alphasynuclein in Parkinsons are also nonessential.
    >
    > which is, I am fairly sure, known to be not true.

    Well no-one has bioteched a mouse that was APP free or
    amyloid/tau free. No-one has bioteched a mouse that was
    alphasynuclein free, nor a cow.

    The Methodology of crosslinking Alzheimers to Parkinsons to
    Prion has never been adopted by the science community. There
    is not a team of researchers devoted to putting these 3
    diseases together as one family and where answers from one
    help spur answers in the other 2. If you research Alzheimers
    then you only glance at work done in Parkinsons and Prion.
    So if a group of scientists were to get together and put all
    3 diseases lumped as one and did research that links and
    connects all three then we would see real big progress.

    >
    >
    > Anyway, so what? Whether the normal protein is good, bad
    > or indifferent has nothing to do with the disease.
    >
    > (Sickle cell is a nice example of a single protein being
    > both good and bad.)
    >
    > >Apparently Bob knows of no case where tau or betaamyloid
    > >or alphasynuclein exists in a normal healthy body doing
    > >some useful and purposeful work. These molecules exist
    > >only in a diseased body.
    >
    > That I do not know is not very relevant. (I have not made
    > any particular effort to find out -- and/or do not
    > remember if I have come across anything.) There are lots
    > of protein whose function is not known. Most proteins. As
    > noted earlier, there was a recent report on the normal
    > function of AB.
    >
    > I assume that they exist for a reason -- though of course
    > that may not be true in any specific case. And even if
    > there was a test for essentiality (I do not know that for
    > these), that does not say they do not have a role.

    I suppose terminally ill CJD patients would be willing to
    run the test of gene removal of the prion-gene. If they come
    out cured and normal, then we will have solved CJD. I
    suppose terminally ill Alzheimers and Parkinsons would be
    willing to a gene-deletion for those proteins. I do not know
    how the Kirin cow was engineered and whether a similar gene-
    deletion can be applied to a human adult.

    >
    >
    > >> >
    > >> >Bob, I feel if any of the above comments are correct
    > >> >in part or in whole, then all three of these diseases
    > >> >of Alzheimers, Parkinsons and Prion are brain diseases
    > >> >created by malfunctioning manufacturing sites that
    > >> >spew out a protein that the body does not need or want
    > >> >and thus the disease is borne. All three are
    > >> >hereditary diseases indicating that manufacturing
    > >> >sites gone awry are genetically based. Prion is
    > >> >contagious by eating, but is it a protein molecule
    > >> >that alters the shape of other protein molecules? The
    > >> >Kirin report suggests otherwise.
    > >>
    > >> How so? It is exactly the result predicted by the prion
    > >> model. (which does not mean that it could not also be
    > >> predicted by some other model.)
    > >
    > >Well, no.
    >
    > Well, yes. The prion model has the host gene for the
    > protein is essential to have disease. Delete the host
    > gene, and you cannot have the disease. That is exactly
    > what the data says. There may be some other model that
    > also makes that prediction, but the deletion test is
    > exactly in agreement with the prion model.
    >

    If the cure for Alzheimers is delete the gene that makes APP
    and if the cure for Parkinsons is delete the gene that makes
    alphasynuclein and if the cure for CJD is delete the prion
    gene, then, the Prusiner Model is irrelevant.

    >
    > >The Prusiner Model predicts bad proteins altering good
    > >proteins.
    >
    > good proteins made by the host -- thus predicting that the
    > host gene for that protein is required in order to have
    > disease.
    >
    > bob

    We should be clear about the term "nonessential" in saying
    that if the body produces anything that has no function or
    use, then it is a disease-molecule.

    There is one link between Alzheimers, Parkinsons and Prion
    that is obvious and that is a disease of the old. Generally
    the old, not always. Thus, the disease is a accumulation of
    waste. In that light, it is irrelevant whether there is a
    PrC or PrP or 13 variants for all of them are disease
    molecules. It is irrelevant whether PrP converts PrC. The
    disease begins when the body produces any of these
    molecules.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  13. Bob

    Bob Guest

    On Thu, 10 Jun 2004 03:22:56 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >
    >It would be interesting to me to go back and try to follow
    >what the German, Mr. Alzheimer ever conjectured about his
    >disease when he first discovered it.

    From a little reading... nothing, and he had no basis for
    doing so. There is no historical parallel between the roles
    of alz and prus. One discovered (first reported) a disease,
    the other offered a model to explain (and resolve a
    controversy about) a long-known disease.

    >>
    >> So, everything Prusiner said has been shown to be true --
    >> but we are still not sure exactly what is happening with
    >> the mammalian prions.
    >
    >No, I would say the only thing Prusiner has said that has
    >been shown true is that the protein has the ability to
    >infect, or infectious agent.

    All steps of the prion model are now known to be reasonable
    -- something not true 20 yr ago. What is not known is
    exactly how they apply to mammalian prions. But we are no
    longer dealing with "it can't be", rather trying to sort out
    what is, in a difficult system.

    >The entire Conversion aspect is doubtful. It may happen
    >that once a prion enters the brain, a PrP forms a scissors.

    The data does not support that. You can’t make up facts --
    esp. when they contradict what is known :)

    >>
    >> With some reservation (BSE, CWD), prion diseases are the
    >> least common/important of these various neurodegenerative
    >> diseases.
    >>
    >
    >Least important in terms of death rates and affliction
    >numbers, but Prion disease maybe as important as Alzheimers
    >or Parkinsons in answering the questions about all 3
    >diseases. Because prion is rare, we do not want to put it
    >on the backshelf because its theory may solve Alzheimers or
    >Parkinsons faster than without.

    agreed, but it rates lower in funding priorities because it
    affects fewer people.

    >>
    >> He was faced with a novel feature -- "transmission" by a
    >> protein.
    >
    >I lived through that history as well as you did Bob and I
    >suspect he was not faced with a novel feature but rather
    >instead his personality to be a "maverick".
    >

    He was faced with a novel feature, the apparent self-
    replication of a protein. It was at the root of a great
    debate, virus or not. I included "prions" (the word had not
    yet been invented; we just talked about scrapie) in a
    virology course I taught, about 1970.

    >Because Prusiner could have just said it was a "virus" too
    >small to measure

    which it is not

    > I suspect in 50 years from now when these diseases are
    > resolved that the years spent from 1990-2004 with oceans
    > of reports on yeast prions will all have been seen as a
    > gigantic waste of time and irrelevant.

    well, we learned something about yeast -- and about
    proteins. Actually, the prion model stimulated the yeast
    folks to invoke the prion explanation of a long known
    mysterious phenomenon in yeast. So in that sense, the prion
    model fed the yeast work.

    >
    >Suppose in 50 years from now we cure Alzheimers and
    >Parkinsons and Prion. And the cure is that we snip or
    >delete or alter a few genes in the body at birth. Just like
    >the Kirin cow. We delete the gene that makes amyloid/tau
    >and thus the person will never contract Alzheimers. We
    >delete the gene that makes alphasynuclein and thus the
    >person never gets Parkinsons. We delete the gene that makes
    >prion molecules and thus never worry about getting CJD. So,
    >every person is like a Kirin cow by 2050 where we know
    >which genes will cause Alzheimers Parkinsons and Prion and
    >we delete them.
    >
    >If that comes true, that the cure is a Kirin cow procedure,
    >then all facets of the Prusiner Model were wrong except for
    >possible transmission.

    That is just plain wrong. You did not read or understand
    what was written earlier.

    The prion model precisely predicts that result -- that
    deletion of the PrP gene would prevent the disease. If you
    don't understand that, then you don't understand what the
    model says. This is really a key point about your
    understanding. You may be objecting to something which is
    not what is being proposed.

    >
    >If the Kirin cow is normal is evidence that PrC is a
    >disease molecule.

    since that cow does not yet exist, that is for the future.

    >If the prion free mouse is normal is evidence that any
    >prion is a disease molecule.

    And some argue that it is not normal -- that it has
    neurological damage. (Not so easy to tell with a mouse.) And
    there is circumstantial evidence to argue for its
    importance. I've written that, and you ignore it. You need
    to understand what is known. (Later you will come back and
    say you didn’t know.)

    The role of PrP must remain open, for now.

    >It makes no difference if it is PrC or PrP. A normal
    >healthy animal is one that has 0 amount of these proteins.

    then there is no such thing as normal healthy human (or any
    other mammal?) on earth, since we all have it. (presumably)

    >
    >Well no-one has bioteched a mouse that was APP free or
    >amyloid/tau free. No-one has bioteched a mouse that was
    >alphasynuclein free,

    ??? are you sure?

    >nor a cow.
    >
    >The Methodology of crosslinking Alzheimers to Parkinsons to
    >Prion has never been adopted by the science community.
    >There is not a team of researchers devoted to putting these
    >3 diseases together as one family and where answers from
    >one help spur answers in the other 2.

    many are doing so.

    >I do not know how the Kirin cow was engineered and whether
    >a similar gene-deletion can be applied to a human adult.

    can't be applied to adults at all. It is done thru stem cell
    work, and the formation of a embryo. Such work is not
    allowed with humans. And work to delete genes from adults
    would never be likely anyway.

    However, drugs to turn off/down a gene may be possible and
    helpful. And such drugs may also serve as probes of
    mechanism. Development of drugs per se does not entirely
    depend on understanding the mechanism. A drug that
    "interacts with" PrP, for example, may prevent it from doing
    whatever it is doing. And once you have the drug, it may be
    a useful probe of mechanism.

    Note that a _reduction_ in a key protein may be useful,
    rather than a complete elimination. Further, esp since these
    are old people, some side effects may be tolerable, if the
    drugs in fact provide real benefit.

    So there is reason for optimism.

    BTW, have a look at a perspective item in Science
    304:1259 (May 28), by Dobson. Discusses therapeutic
    approaches for amyloid diseases. Not much meat in it, but
    a useful overview.

    bob
     
  14. Sun, 13 Jun 2004 19:36:28 -0700 Bob wrote:

    > On Thu, 10 Jun 2004 03:22:56 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >
    > >It would be interesting to me to go back and try to
    > >follow what the German, Mr. Alzheimer ever conjectured
    > >about his disease when he first discovered it.
    >
    > From a little reading... nothing, and he had no basis for
    > doing so. There is no historical parallel between the
    > roles of alz and prus. One discovered (first reported) a
    > disease, the other offered a model to explain (and resolve
    > a controversy about) a long-known disease.
    >
    > >>
    > >> So, everything Prusiner said has been shown to be true
    > >> -- but we are still not sure exactly what is happening
    > >> with the mammalian prions.
    > >
    > >No, I would say the only thing Prusiner has said that has
    > >been shown true is that the protein has the ability to
    > >infect, or infectious agent.
    >
    > All steps of the prion model are now known to be
    > reasonable -- something not true 20 yr ago. What is not
    > known is exactly how they apply to mammalian prions. But
    > we are no longer dealing with "it can't be", rather trying
    > to sort out what is, in a difficult system.
    >
    > >The entire Conversion aspect is doubtful. It may happen
    > >that once a prion enters the brain, a PrP forms a
    > >scissors.
    >
    > The data does not support that. You can’t make up facts --
    > esp. when they contradict what is known :)
    >
    > >>
    > >> With some reservation (BSE, CWD), prion diseases are
    > >> the least common/important of these various
    > >> neurodegenerative diseases.
    > >>
    > >
    > >Least important in terms of death rates and affliction
    > >numbers, but Prion disease maybe as important as
    > >Alzheimers or Parkinsons in answering the questions about
    > >all 3 diseases. Because prion is rare, we do not want to
    > >put it on the backshelf because its theory may solve
    > >Alzheimers or Parkinsons faster than without.
    >
    > agreed, but it rates lower in funding priorities because
    > it affects fewer people.
    >
    > >>
    > >> He was faced with a novel feature -- "transmission" by
    > >> a protein.
    > >
    > >I lived through that history as well as you did Bob and I
    > >suspect he was not faced with a novel feature but rather
    > >instead his personality to be a "maverick".
    > >
    >
    > He was faced with a novel feature, the apparent self-
    > replication of a protein. It was at the root of a great
    > debate, virus or not. I included "prions" (the word had
    > not yet been invented; we just talked about scrapie) in a
    > virology course I taught, about 1970.
    >

    You may have given away your age Bob-- guess-- 64. Did you
    teach at Berkeley?

    Perhaps you can tell me how many protons exist in a
    hepatitus virus and then how many protons exist in a prion
    molecule. Example: dopamine C8 H11 N O2 has 8x6 + 11x1 + 1x7
    + 2x8 for a grand total of 82 protons.

    Question: the purported indestructibility of prion proteins
    is rather unbelievable. So do they actually incinerate
    prions and turn them to dust and find they are not
    destroyed. No acid destroys prions and UV does not destroy
    prions. This indestructibility is not believable because
    then, well much of the deposits of fossils should be exuding
    with prion proteins. In fact every skull fossil, due to
    prion indestructibility should be coated with ancient
    prions. Yet there has never been prion fossils found. Prion
    indestructibility suggests a layer of slime of prion
    proteins in the Earth's crust yet there is none.

    >
    > >Because Prusiner could have just said it was a "virus"
    > >too small to measure
    >
    > which it is not
    >

    It is easy to say. But your statement does not cover viral
    debri such as the injection that is discarded when the virus
    enters a cell. Who know if the injection needle is the
    "flack" that when in contact with DNA sequencing causes
    abnormal protein manufacture. Can someone tell me how many
    protons is in a viral injection system? Can someone tell me
    if the viral injection system is a protein molecule? Perhaps
    it is similar to a prion protein itself?

    Viral Debri Remains is a better solution for what causes CJD
    or MadCow or sheep scrapie. Not a virus itself but the
    debris a virus leaves behind. I forgotten the name of a
    disease that a viral debris particle causes but some are
    known to exist. And such an explanation easily explains the
    prion variants.

    >
    > > I suspect in 50 years from now when these diseases are
    > > resolved that the years spent from 1990-2004 with oceans
    > > of reports on yeast prions will all have been seen as a
    > > gigantic waste of time and irrelevant.
    >
    > well, we learned something about yeast -- and about
    > proteins. Actually, the prion model stimulated the yeast
    > folks to invoke the prion explanation of a long known
    > mysterious phenomenon in yeast. So in that sense, the
    > prion model fed the yeast work.
    >

    I would counter by saying that Alzheimers disease has
    significantly progressed in the last 5 years but that Prion
    disease has languished. And a faulty model will hinder and
    tripp-up understanding.

    >
    > >
    > >Suppose in 50 years from now we cure Alzheimers and
    > >Parkinsons and Prion. And the cure is that we snip or
    > >delete or alter a few genes in the body at birth. Just
    > >like the Kirin cow. We delete the gene that makes
    > >amyloid/tau and thus the person will never contract
    > >Alzheimers. We delete the gene that makes alphasynuclein
    > >and thus the person never gets Parkinsons. We delete the
    > >gene that makes prion molecules and thus never worry
    > >about getting CJD. So, every person is like a Kirin cow
    > >by 2050 where we know which genes will cause Alzheimers
    > >Parkinsons and Prion and we delete them.
    > >
    > >If that comes true, that the cure is a Kirin cow
    > >procedure, then all facets of the Prusiner Model were
    > >wrong except for possible transmission.
    >
    > That is just plain wrong. You did not read or understand
    > what was written earlier.
    >
    > The prion model precisely predicts that result -- that
    > deletion of the PrP gene would prevent the disease. If you
    > don't understand that, then you don't understand what the
    > model says. This is really a key point about your
    > understanding. You may be objecting to something which is
    > not what is being proposed.
    >

    Suppose it is a viral-debris-particle which when eaten in
    the food supply makes its way into the brain and then alters
    the PrP gene. But if there is no PrP gene then there is
    nothing to alter.

    >
    > >
    > >If the Kirin cow is normal is evidence that PrC is a
    > >disease molecule.
    >
    > since that cow does not yet exist, that is for the future.
    >
    > >If the prion free mouse is normal is evidence that any
    > >prion is a disease molecule.
    >
    > And some argue that it is not normal -- that it has
    > neurological damage. (Not so easy to tell with a mouse.)
    > And there is circumstantial evidence to argue for its
    > importance. I've written that, and you ignore it. You need
    > to understand what is known. (Later you will come back and
    > say you didn’t know.)
    >

    I am not going to do that. The bit about prion function in
    cell wall was genuine and I had been under a false
    assumption for 7 years.

    >
    > The role of PrP must remain open, for now.

    This is what is really nice about my methodology compared to
    the Prusiner Model. The Prusiner Model is fixed with little
    to no guidance or direction. But the methodology of
    crosslinking of 3 diseases asks questions everywhere you
    turn. You say the role of PrP must remain open.

    So let us ask whether the protein in Parkinsons of
    alphasynuclein has any real role or function of a normal
    healthy individual. So far as I can see, there is none for
    alphasynuclein. Young people do not have alphasynuclein,
    only people old age with Parkinsons have alphasynuclein.
    Then there is Alzheimers with betaamyloid. There is no use
    or function or purpose for betaamyloid except that of
    driving the disease of Alzheimers. Young people do not have
    betaamyloid, only old people with the Alzheimers disease in
    progress have betaamyloid.

    >
    >
    > >It makes no difference if it is PrC or PrP. A normal
    > >healthy animal is one that has 0 amount of these
    > >proteins.
    >
    > then there is no such thing as normal healthy human (or
    > any other mammal?) on earth, since we all have it.
    > (presumably)

    Tell me Bob, do insects have serotonin and dopamine? If they
    do, then they should be able to get Parkinsons. Do they have
    the APP sensory molecule? If they do, then they should be
    able to catch Alzheimers. If true would be a boom for
    research since insects under study are so quick to provide
    data and information, even faster than mice.

    >
    >
    > >
    > >Well no-one has bioteched a mouse that was APP free or
    > >amyloid/tau free. No-one has bioteched a mouse that was
    > >alphasynuclein free,
    >
    > ??? are you sure?

    Not sure.

    >
    >
    > >nor a cow.
    > >
    > >The Methodology of crosslinking Alzheimers to Parkinsons
    > >to Prion has never been adopted by the science community.
    > >There is not a team of researchers devoted to putting
    > >these 3 diseases together as one family and where answers
    > >from one help spur answers in the other 2.
    >
    > many are doing so.

    You yourself admit that our understanding of mammalian
    prions is sketchy and has gaps. The Prusiner Model has two
    unbelievables (1) means of replicating (2)
    indestructibility. If we ask for one item of viral debris,
    then this one item alone can solve the pathology, an Occam
    Razor to prion disease.

    All 3 diseases of Alzheimers , Parkinsons and Prion are
    hereditary diseases. Because they are hereditary means
    that a virus can start the disease because a virus can
    mimic the DNA sequencing of a disease. But not only the
    virus but the virus debris particles it discards when it
    enters a host cell.

    A virus has never been found for prion disease. But no-one
    ever bothered to look at the viral debris. Nor looked at
    fungus or bacteria debris. Example is Chlamydia. Does it
    leave behind debris particles. The common cold viruses of
    rhino viruses leaves behind particles. And no-one has
    studied those in detail

    Perhaps the tau protein in Alzheimers which seems to be
    connected to the disease but not directly, perhaps tau is a
    result of some virus debris particle that started the
    Alzheimers but also the tau.

    Perhaps Alzheimers and Parkinsons are just as transmissible
    as Prion because if a viral debris particle is responsible
    then the eating of the brains of a infected Alzheimers or
    Parkinsons would procure the disease.

    >
    >
    > >I do not know how the Kirin cow was engineered and
    > >whether a similar gene-deletion can be applied to a
    > >human adult.
    >
    > can't be applied to adults at all. It is done thru stem
    > cell work, and the formation of a embryo. Such work is not
    > allowed with humans. And work to delete genes from adults
    > would never be likely anyway.
    >
    > However, drugs to turn off/down a gene may be possible and
    > helpful. And such drugs may also serve as probes of
    > mechanism. Development of drugs per se does not entirely
    > depend on understanding the mechanism. A drug that
    > "interacts with" PrP, for example, may prevent it from
    > doing whatever it is doing. And once you have the drug, it
    > may be a useful probe of mechanism.
    >
    > Note that a _reduction_ in a key protein may be useful,
    > rather than a complete elimination. Further, esp since
    > these are old people, some side effects may be tolerable,
    > if the drugs in fact provide real benefit.
    >
    > So there is reason for optimism.
    >
    > BTW, have a look at a perspective item in Science 304:1259
    > (May 28), by Dobson. Discusses therapeutic approaches for
    > amyloid diseases. Not much meat in it, but a useful
    > overview.
    >
    > bob

    I like more to have the formulas of prion, tau, betaamyloid
    and alphasynuclein molecules.

    PS, one experimental test that would favor the Prusiner
    Model and disfavor my methodology of Family-Related 3
    diseases would be if a individual were found to have any
    two of the 3 diseases simultaneously. If there exists a
    person with say both Parkinsons and CJD would bolster the
    Prusiner Model and would disfavor my methodology. But
    since there does not exist such a animal that has two of
    the three diseases of Alzheimers, Parkinsons or Prion
    suggests that the Prusiner Model is false. Even with the
    viral-debris as the inceptor of the diseases.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  15. Mark Tarka

    Mark Tarka Guest

    Archimedes Plutonium <[email protected]> wrote in message news:<[email protected]>...
    > Sun, 13 Jun 2004 19:36:28 -0700 Bob wrote:
    [snip stuff, a fair amount I could understand at
    skimming speed]
    > > So there is reason for optimism.
    > >
    > > BTW, have a look at a perspective item in Science
    > > 304:1259 (May 28), by Dobson. Discusses therapeutic
    > > approaches for amyloid diseases. Not much meat in it,
    > > but a useful overview.
    > >
    > > bob
    >
    > I like more to have the formulas of prion, tau,
    > betaamyloid and alphasynuclein molecules.
    >
    > PS, one experimental test that would favor the Prusiner
    > Model and disfavor my methodology of Family-Related 3
    > diseases would be if a individual were found to have any
    > two of the 3 diseases simultaneously. If there exists a
    > person with say both Parkinsons and CJD would bolster
    > the Prusiner Model and would disfavor my methodology.
    > But since there does not exist such a animal that has
    > two of the three diseases of Alzheimers, Parkinsons or
    > Prion suggests that the Prusiner Model is false. Even
    > with the viral-debris as the inceptor of the diseases.

    Apparently the medical people available to the middle
    classes and below in NYC have difficulty distinguishing
    between Alzheimer's and Parkinsons. Problems in
    differentiating other more usual conditions as well, but
    that's another story (I've got a thread sitting in fifth
    place or so on the first page for sci.med.radiology if you
    want to look).

    You look for novel causes of the disease. Why not a simple
    build-up of toxins over the years of eating processed foods
    (the range from fruits and vegies exposed to various 'cides,
    whatever other foods legally contain, etc.)? Old bodies got
    'em, youngies aint.

    And could Alzheimer's simply be the loss of a will to live.
    Hopeless dispair born of frustration, loss of contact with
    family, church? Beaten-down, ground-down, by a vengeful
    sibling or offspring?

    But my main question, for personal reasons, relates to a
    medication used for Alzheimer's: Cognex (Floxitine HCl I
    think). It's still on the market. There's no negative
    reports about it that I have found, other than, I think,
    that it and Prozac interact with the same _______ (sorry,
    not near my notes, even if I could find them in the truck).
    At the time my mother started taking the drug, it was called
    experimental. The PDR doesn't say much about long term
    effects. Have either of you any knowledge of adverse
    affects, even simple tables of sales figures compared to
    alternatives over the years since 1992?

    Mark
     
  16. Bob

    Bob Guest

    On Mon, 14 Jun 2004 02:47:37 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >>
    >> He was faced with a novel feature, the apparent self-
    >> replication of a protein. It was at the root of a great
    >> debate, virus or not. I included "prions" (the word had
    >> not yet been invented; we just talked about scrapie) in a
    >> virology course I taught, about 1970.
    >>
    >
    >You may have given away your age Bob-- guess-- 64. Did you
    >teach at Berkeley?

    I was on the bio faculty at Rice at that time.

    >
    >Perhaps you can tell me how many protons exist in a
    >hepatitus virus and then how many protons exist in a prion
    >molecule. Example: dopamine C8 H11 N O2 has 8x6 + 11x1 +
    >1x7 + 2x8 for a grand total of 82 protons.

    zillions. who cares.

    >
    >Question: the purported indestructibility of prion proteins
    >is rather unbelievable. So do they actually incinerate
    >prions and turn them to dust and find they are not
    >destroyed. No acid destroys prions and UV does not destroy
    >prions. This indestructibility is not believable

    nor is it true. They are "relatively" resistant to common
    inactivating agents (compared to typical bio agents). No one
    said they are completely resistant.

    >
    >>
    >> >Because Prusiner could have just said it was a "virus"
    >> >too small to measure
    >>
    >> which it is not
    >>
    >
    >It is easy to say.

    The gene for the infectious agent is a host gene. That
    is a known.

    >> >
    >> >If that comes true, that the cure is a Kirin cow
    >> >procedure, then all facets of the Prusiner Model were
    >> >wrong except for possible transmission.
    >>
    >> That is just plain wrong. You did not read or understand
    >> what was written earlier.
    >>
    >> The prion model precisely predicts that result -- that
    >> deletion of the PrP gene would prevent the disease. If
    >> you don't understand that, then you don't understand what
    >> the model says. This is really a key point about your
    >> understanding. You may be objecting to something which is
    >> not what is being proposed.
    >>
    >
    >Suppose it is a viral-debris-particle which when eaten in
    >the food supply makes its way into the brain and then
    >alters the PrP gene. But if there is no PrP gene then there
    >is nothing to alter.
    >

    Please read carefully. What I said was that the prion model
    predicts that deletion of the PrP gene would prevent
    disease. I did not say that no other model could make that
    prediction. But the other key part of the story is that we
    know the infectious agent is in fact the product of that
    gene. Put the two together, and you more or less prove the
    prion model -- with the mechanism being a black box, but one
    that is proven to be reasonable.

    Somewhere you asked about why prion diseases are
    infectious. I started to answer but seem to have lost it, I
    think. To some extent, it may be a side issue, but still of
    some interest.

    First, must distinguish an agent that is infectious form one
    that is merely toxic. Both cause an effect, but when we say
    that something is infectious, we mean that it "replicates"
    -- makes more of itself. This is part of the background for
    prions (though we now realize it is not the only source of
    prion disease). It would be unreasonable that any single
    protein in Alz, as we currently understand the mech, would
    "replicate"; thus infectiousness is unlikely.

    But then, for an agent to have an effect requires that it
    get in and get to the right place. This is much a matter of
    luck. Some do, some don't. No real basis for predicting it.
    Prions are effective when injected in the brain, and
    somewhat effective orally. They also replicate = make more
    of themselves. Whether AB42 (the active fragment of APP) has
    any effect when administered by any route, I don't really
    know. No real significance (to the models of how it works)
    one way or the other.

    >
    >So let us ask whether the protein in Parkinsons of
    >alphasynuclein has any real role or function of a normal
    >healthy individual. So far as I can see, there is none for
    >alphasynuclein. Young people do not have alphasynuclein,
    >only people old age with Parkinsons have alphasynuclein.
    >Then there is Alzheimers with betaamyloid. There is no use
    >or function or purpose for betaamyloid except that of
    >driving the disease of Alzheimers. Young people do not have
    >betaamyloid, only old people with the Alzheimers disease in
    >progress have betaamyloid.

    You are making up facts again. Those things are not known,
    and you admit to that below. I told you earlier that recent
    work reported on a function for the alz peptide.

    >
    >>
    >>
    >> >It makes no difference if it is PrC or PrP. A normal
    >> >healthy animal is one that has 0 amount of these
    >> >proteins.
    >>
    >> then there is no such thing as normal healthy human (or
    >> any other mammal?) on earth, since we all have it.
    >> (presumably)
    >
    >Tell me Bob, do insects have serotonin and dopamine?

    no idea

    >If they do, then they should be able to get Parkinsons.

    maybe, maybe not. There is no particular logic in that.

    >Do they have the APP sensory molecule? If they do, then
    >they should be able to catch Alzheimers. If true would be a
    >boom for research since insects under study are so quick to
    >provide data and information, even faster than mice.

    yes, and they are used as model system for many things. I
    know they are used for huntingtin. Don't know about these
    others. Why not search Medline and see. The common insect
    for such work is Drosophila (because it has a well developed
    genetic system). Try a search on something like Drosophila
    AND parkinson.

    >
    >>
    >>
    >> >
    >> >Well no-one has bioteched a mouse that was APP free or
    >> >amyloid/tau free. No-one has bioteched a mouse that was
    >> >alphasynuclein free,
    >>
    >> ??? are you sure?
    >
    >Not sure.

    Then don't keep repeating it as if it were true.

    >> >The Methodology of crosslinking Alzheimers to Parkinsons
    >> >to Prion has never been adopted by the science
    >> >community. There is not a team of researchers devoted to
    >> >putting these 3 diseases together as one family and
    >> >where answers from one help spur answers in the other 2.
    >>
    >> many are doing so.
    >
    >You yourself admit that our understanding of mammalian
    >prions is sketchy and has gaps. The Prusiner Model has two
    >unbelievables (1) means of replicating (2)
    >indestructibility.

    No, no, no.

    #2 is simply false (see above), and #1 is known to be
    #reasonable, even
    if we are not sure of details in this case. The inability to
    show in vitro replication of mammalian prions is not a
    problem, given all else that we do know. There are many
    reasons why it may be hard to do in the lab. There are many
    infectious agents which can not be grown in the lab

    >
    >PS, one experimental test that would favor the Prusiner
    > Model and disfavor my methodology of Family-Related 3
    > diseases would be if a individual were found to have any
    > two of the 3 diseases simultaneously.

    I'd be quite surprised if that wasn't well known -- that
    one can get
    >1 of them. As someone else noted, diagnosis is not easy,
    >esp early,
    but both Alz and park are common enough that surely dual-
    disease patients are known. Try Medline. But I don't think
    I'd make much of the answer one way or the other.

    bob
     
  17. Bob

    Bob Guest

    On 14 Jun 2004 12:56:53 -0700, [email protected] (Mark Tarka)
    wrote:

    >
    >But my main question, for personal reasons, relates to
    >a medication used for Alzheimer's: Cognex (Floxitine
    >HCl I think).
    >

    Mark,

    Suggest...

    1. Medline, where you can get whatever is being published
    on a particular drug -- with at least the abstracts
    being free.

    2. You might also check the NIH web site for general info on
    clinical trials, for the latest developments. If you/she
    are so inclined, you might try to make contact with a
    place that is on the frontline of this, and even consider
    taking part in a clinical trial. (That is a complex
    personal issue; my comment is not advice to do the trial.
    But I know you have a science background, and thus some
    basis for analyzing the merits of this -- at least the
    objective parts.)

    bob
     
  18. Tue, 15 Jun 2004 19:34:54 -0700 Bob wrote:

    > On Mon, 14 Jun 2004 02:47:37 -0500, Archimedes Plutonium
    > <[email protected]> wrote:
    >
    > >>
    > >> He was faced with a novel feature, the apparent self-
    > >> replication of a protein. It was at the root of a great
    > >> debate, virus or not. I included "prions" (the word had
    > >> not yet been invented; we just talked about scrapie) in
    > >> a virology course I taught, about 1970.
    > >>
    > >
    > >You may have given away your age Bob-- guess-- 64. Did
    > >you teach at Berkeley?
    >
    > I was on the bio faculty at Rice at that time.
    >
    > >
    > >Perhaps you can tell me how many protons exist in a
    > >hepatitus virus and then how many protons exist in a
    > >prion molecule. Example: dopamine C8 H11 N O2 has 8x6 +
    > >11x1 + 1x7 + 2x8 for a grand total of 82 protons.
    >
    > zillions. who cares.

    I care. Someone ought to find a poetical phrase out of the
    Bible that says something like this-- Covet those facts
    which are least in dispute.

    Dopamine is C8 H11 N O2 and has 82 protons whereas serotonin
    is C10 H12 N2 O and has 10x6 + 12x1 + 2x7 + 1x8 = 94
    protons. The more protons the more likelihood of unstable
    compared to lesser protons. Thus a disease borne around
    dopamine would be more widespread and common than a disease
    borne around serotonin. We are certain that Parkinsons
    involves dopamine. We are unsure as to whether Prion or even
    Alzheimers involves serotonin. Because dopamine is a more
    stable molecule with 82 protons than is serotonin of 94
    protons then the disease involving dopamine of Parkinsons
    would be a more well defined disease than any disease
    involving serotonin.

    This concept of less complex and more stable reaches into
    the proteins involved. Alzheimers is the most common of the
    3 diseases and the betaamyloid is the most simple and stable
    of the proteins and so Alzheimers, in likelihood is the most
    common and most well defined of Alz, Parkinsons or Prion.

    Is it a fact that PrP protein is the most complex protein of
    these 3 diseases would suggest Prion disease is the most
    rare of them and the least clearcut.

    So, yes, facts that are least able to be disputed are
    probably the best facts of all.

    >
    >
    > >
    > >Question: the purported indestructibility of prion
    > >proteins is rather unbelievable. So do they actually
    > >incinerate prions and turn them to dust and find they are
    > >not destroyed. No acid destroys prions and UV does not
    > >destroy prions. This indestructibility is not believable
    >
    > nor is it true. They are "relatively" resistant to common
    > inactivating agents (compared to typical bio agents). No
    > one said they are completely resistant.
    >

    This is an area where science has been abandoned and social
    hysteria has entered and taken place of science. When we see
    pictures in England of burn squad units and crematoria of
    herds of cattle. Do we really believe that burning prions
    into dust is a demand of science or a demand of the social
    hysteria of the times. And then that hysteria gets
    translated on paper as that prion proteins are tough
    proteins when in reality they probably are no even
    noteworthy. Because probably the prion proteins did not
    cause the Mad Cow disease of England as what the hysteria
    people believe it caused.

    It is nice to see that in the USA with the recent Canadian
    cow with prion disease that there was no hysterical
    cremation of cattle.

    >
    > >
    > >>
    > >> >Because Prusiner could have just said it was a "virus"
    > >> >too small to measure
    > >>
    > >> which it is not
    > >>
    > >
    > >It is easy to say.
    >
    > The gene for the infectious agent is a host gene. That is
    > a known.
    >
    > >> >
    > >> >If that comes true, that the cure is a Kirin cow
    > >> >procedure, then all facets of the Prusiner Model were
    > >> >wrong except for possible transmission.
    > >>
    > >> That is just plain wrong. You did not read or
    > >> understand what was written earlier.
    > >>
    > >> The prion model precisely predicts that result -- that
    > >> deletion of the PrP gene would prevent the disease. If
    > >> you don't understand that, then you don't understand
    > >> what the model says. This is really a key point about
    > >> your understanding. You may be objecting to something
    > >> which is not what is being proposed.
    > >>
    > >
    > >Suppose it is a viral-debris-particle which when eaten in
    > >the food supply makes its way into the brain and then
    > >alters the PrP gene. But if there is no PrP gene then
    > >there is nothing to alter.
    > >
    >
    > Please read carefully. What I said was that the prion
    > model predicts that deletion of the PrP gene would prevent
    > disease. I did not say that no other model could make that
    > prediction. But the other key part of the story is that we
    > know the infectious agent is in fact the product of that
    > gene. Put the two together, and you more or less prove the
    > prion model -- with the mechanism being a black box, but
    > one that is proven to be reasonable.

    Thanks for making that statement and I must compliment
    you Bob, even though I know you do not like being
    complimented on. For I could never make a clear paragraph
    such as your above.

    I read it carefully. The PrP gene is a manufacturing site
    within the body. So the body never really needs to come in
    contact with a diseased prion. So the body itself can
    produce the infectious agent.

    So then the flaw of the Prusiner Model is that the foreign
    prion that enters the body is shape changing or conform
    changing the PrP gene to spew out more invading prions.

    Bob, Occams Razor suggests that the PrP prion is not shape
    changing other prions but is aggregating. It is plaqueing or
    accumulating or forming aggregates with other prion
    proteins. Much like betaamyloid or alphasynuclein in Alzh
    and Parkinsons respectively. So that Bob, what you and Mr.
    Prusiner thought was a prion proteins coming together and
    shape change one another was rather instead a coming
    together because the bonds are for Plaqueing or fibril
    aggregation.

    Occams Razor further suggests that if the PrP gene is the
    site of creation of these disease proteins then it does not
    need a foreign prion to enter the body to start that gene to
    mass produce. It could be some other particle that when
    eaten such as a viroid that turns the PrP gene on.

    The difference between the Prusiner Model and my stance on
    Prion disease is that of Manufacturing Site. The body itself
    creates the disease because the genes are all set up to mass
    produce. The Prusiner Model wants you to believe that a
    foreign protein that is eaten will shape change either the
    PrP gene or shape change other prion molecules. Most Prion
    disease that occurs is borne not of eating infectious food
    but is created spontaneously inside the body. Most prion
    disease is hereditary. I do not have the percentage but I
    would guess that 90% of every prion disease case was borne
    of hereditary and not of infection agent.

    Occams Razor would then say that if 90% of a disease is
    caused by the internal body of a animal and not some foreign
    eaten protein, then it stands to reason that the PrP gene
    which is a Manufacturing Site is the origin of this disease.
    And that catching Prion disease from eating is probably due
    to some viroid particle that switches the PrP gene on.

    This thing about PrP proteins shape changing other PrP
    proteins is doubtful because like in Alzheimers or
    Parkinsons Lewy bodies, these proteins tend to clump
    together. And it is this clumping together tendency that has
    clouded the mind and model of Mr. Prusiner into thinking
    that the prion proteins are creating more prion proteins by
    shape changing existing ones. Mr. Prusiner mistakes clumping
    for shape changing.

    Can the so called infectious prion switch on the PrP gene.
    That is the question that needs to be answered. That is the
    important question for Bob and Mr. Prusiner. Can the eaten
    prion molecule get to the PrP gene and cause that gene to
    spew out in mass production more infectious proteins.

    Or is there something else such as a viroid or viral debris
    that is easier to eat and finds its way into the brain and
    switches the PrP gene to spew bad prions.

    Looking at how big a molecule and complex a molecule with
    its metal ions in the molecule, that there exists thousands
    and millions of viral particles that would more easily
    transport themselves from feedlot into the brains and turn
    the PrP switch.

    You see, Bob can so easily describe the Prusiner Model in a
    nice clear paragraph whereas I have to rumble on.

    >
    >
    > Somewhere you asked about why prion diseases are
    > infectious. I started to answer but seem to have lost it,
    > I think. To some extent, it may be a side issue, but still
    > of some interest.

    I do not think Prion diseases are infectious. Since most of
    them are hereditary, guessing that 90% of reported cases are
    hereditary. That those cases due to eating of contaminated
    food is because of some virus particle that exists within
    that food that turns the PrP gene to initiate the disease.

    I think this conformal shape change ascribed to prion
    proteins for the last decade has more to do with the fact
    that all 3 of these protein diseases fibril congregate in
    clumps. What prion researchers were thinking of shape
    changing was merely the tendency of these proteins to clump
    together whether in betaamyloid plaques or alphasynuclein
    Lewy bodies or in Prion proteins of plaques. They were not
    shape changing but Clumping.

    It is far easier to hypothesize some viroid particle that
    sneeks into the food supply gets up into the brain and turns
    the PrP gene into mass production site rather than think
    that this large cumbersome prion protein is going to travel
    eventually into the brain and end up at the PrP gene and
    then change that gene.

    >
    >
    > First, must distinguish an agent that is infectious form
    > one that is merely toxic. Both cause an effect, but when
    > we say that something is infectious, we mean that it
    > "replicates" -- makes more of itself. This is part of the
    > background for prions (though we now realize it is not the
    > only source of prion disease). It would be unreasonable
    > that any single protein in Alz, as we currently understand
    > the mech, would "replicate"; thus infectiousness is
    > unlikely.

    Agreed. We do not say a asbestos fiber is a cancer
    infectious agent. Although it can cause cancer once it gets
    inside the body.

    The Prusiner Model relies on the PrP gene. The Prusiner
    Model wants to say that the foreign prion will shape change
    either the PrP gene or proteins created from the PrP gene.
    What I want to say is that a virus particle has an easier
    time of getting into the brain and to the PrP gene and then
    starting the disease by altering the PrP gene.

    I do not deny the possibility that Prion proteins can cause
    shape changes of other prion proteins and as Bob continually
    reminds me of evidence that this goes on. But I wonder
    whether the tendency for these proteins in these 3 diseases
    to clump is what is seen and misreported as shape changing.

    >
    >
    > But then, for an agent to have an effect requires that it
    > get in and get to the right place. This is much a matter
    > of luck. Some do, some

    And this is where the Prusiner Model and Manufacturing Site
    Model differ. In that it would be far easier for a virus
    particle to get into the brain and to alter the PrP gene.
    Easier and better because viruses reason for existence is to
    alter genetics whereas proteins are a byproduct of genetics.
    How much easier it would be for a viroid to alter PrP gene
    than for this huge lumbering cumbersone protein.

    >
    > don't. No real basis for predicting it. Prions are
    > effective when injected in the brain, and somewhat
    > effective orally. They also replicate = make more of
    > themselves. Whether AB42 (the active fragment of APP) has
    > any effect when administered by any route, I don't really
    > know. No real significance (to the models of how it works)
    > one way or the other.
    >

    Do they really make more of themselves or are they just
    clumping together because clumping is natural in these
    3 diseases.

    Alzheimers is hereditary. That means virus particles have
    the greatest chance of turning normal APP into rogue APP. So
    if a rogue APP is inserted into a normal brain, it probably
    will not go diseased. But if a virus were inserted that has
    a proclivity to APP chemistry could start the disease.

    >
    > >
    > >So let us ask whether the protein in Parkinsons of
    > >alphasynuclein has any real role or function of a normal
    > >healthy individual. So far as I can see, there is none
    > >for alphasynuclein. Young people do not have
    > >alphasynuclein, only people old age with Parkinsons have
    > >alphasynuclein. Then there is Alzheimers with
    > >betaamyloid. There is no use or function or purpose for
    > >betaamyloid except that of driving the disease of
    > >Alzheimers. Young people do not have betaamyloid, only
    > >old people with the Alzheimers disease in progress have
    > >betaamyloid.
    >
    > You are making up facts again. Those things are not known,
    > and you admit to that below. I told you earlier that
    > recent work reported on a function for the alz peptide.
    >
    > >
    > >>
    > >>
    > >> >It makes no difference if it is PrC or PrP. A normal
    > >> >healthy animal is one that has 0 amount of these
    > >> >proteins.
    > >>
    > >> then there is no such thing as normal healthy human (or
    > >> any other mammal?) on earth, since we all have it.
    > >> (presumably)
    > >
    > >Tell me Bob, do insects have serotonin and dopamine?
    >
    > no idea
    >
    > >If they do, then they should be able to get Parkinsons.
    >
    > maybe, maybe not. There is no particular logic in that.
    >
    > >Do they have the APP sensory molecule? If they do,
    > >then they should be able to catch Alzheimers. If true
    > >would be a boom for research since insects under study
    > >are so quick to provide data and information, even
    > >faster than mice.
    >
    > yes, and they are used as model system for many things. I
    > know they are used for huntingtin. Don't know about these
    > others. Why not search Medline and see. The common insect
    > for such work is Drosophila (because it has a well
    > developed genetic system). Try a search on something like
    > Drosophila AND parkinson.
    >
    > >
    > >>
    > >>
    > >> >
    > >> >Well no-one has bioteched a mouse that was APP free or
    > >> >amyloid/tau free. No-one has bioteched a mouse that
    > >> >was alphasynuclein free,
    > >>
    > >> ??? are you sure?
    > >
    > >Not sure.
    >
    > Then don't keep repeating it as if it were true.
    >
    > >> >The Methodology of crosslinking Alzheimers to
    > >> >Parkinsons to Prion has never been adopted by the
    > >> >science community. There is not a team of researchers
    > >> >devoted to putting these 3 diseases together as one
    > >> >family and where answers from one help spur answers in
    > >> >the other 2.
    > >>
    > >> many are doing so.
    > >
    > >You yourself admit that our understanding of mammalian
    > >prions is sketchy and has gaps. The Prusiner Model has
    > >two unbelievables (1) means of replicating (2)
    > >indestructibility.
    >
    > No, no, no.
    >
    > #2 is simply false (see above), and #1 is known to be
    > #reasonable, even
    > if we are not sure of details in this case. The inability
    > to show in vitro replication of mammalian prions is not a
    > problem, given all else that we do know. There are many
    > reasons why it may be hard to do in the lab. There are
    > many infectious agents which can not be grown in the lab

    Granted #1 is reasonable. But is it likely? According to
    Occams Razor and the fact that 99% of all Alzh, Parkinsons
    and Prion are initiated by heredity combined with the fact
    that viruses or viroids or virus debris particles are the
    worlds easiest means of altering genetics in animals.
    Probability would then rest on a viral type trigger that
    turns on the PrP gene. People when presented with facts of
    how large and cumbersome a prion molecule is and how small
    and transportable a viroid or virus debris particle is and
    how easy a virus particle can change a gene site then the
    probabilities disfavor the Prusiner Model.

    >
    >
    > >
    > >PS, one experimental test that would favor the Prusiner
    > > Model and disfavor my methodology of Family-Related 3
    > > diseases would be if a individual were found to have
    > > any two of the 3 diseases simultaneously.
    >
    > I'd be quite surprised if that wasn't well known -- that
    > one can get
    > >1 of them. As someone else noted, diagnosis is not easy,
    > >esp early,
    > but both Alz and park are common enough that surely dual-
    > disease patients are known. Try Medline. But I don't think
    > I'd make much of the answer one way or the other.
    >
    > bob

    Here I would have to ask whether a person can have several
    viral attacks in conjunction with one another. I suppose
    this happens commonly with HIV and pneumonia viruses. So I
    rescind my above test of 2 Family of Protein diseases.

    It is likely that a person with Alzheimers could get a Prion
    viroid and thus have both Alzheimers and CJD all at once.

    Archimedes Plutonium www.archimedesplutonium.com
    www.iw.net/~a_plutonium whole entire Universe is just one
    big atom where dots of the electron-dot-cloud are galaxies
     
  19. Steve Turner

    Steve Turner Guest

    On Wed, 16 Jun 2004 13:16:03 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >Dopamine is C8 H11 N O2 and has 82 protons whereas
    >serotonin is C10 H12 N2 O and has 10x6 + 12x1 + 2x7 + 1x8 =
    >94 protons. The more protons the more likelihood of
    >unstable compared to lesser protons. Thus a disease borne
    >around dopamine would be more widespread and common than a
    >disease borne around serotonin. We are certain that
    >Parkinsons involves dopamine. We are unsure as to whether
    >Prion or even Alzheimers involves serotonin. Because
    >dopamine is a more stable molecule with 82 protons than is
    >serotonin of 94 protons then the disease involving dopamine
    >of Parkinsons would be a more well defined disease than any
    >disease involving serotonin.

    This has got to be about the most creative crackpottery that
    I've seen. I wish I had time to read AP's posts more
    thoroughly because they make for some really unique
    entertainment.

    Steve Turner
     
  20. Bob

    Bob Guest

    On Wed, 16 Jun 2004 13:16:03 -0500, Archimedes Plutonium
    <[email protected]> wrote:

    >
    >Dopamine is C8 H11 N O2 and has 82 protons whereas
    >serotonin is C10 H12 N2 O and has 10x6 + 12x1 + 2x7 + 1x8 =
    >94 protons. The more protons the more likelihood of
    >unstable compared to lesser protons.

    That is ludicrous.

    bob
     
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