Board index » medical » Prion disease; viroid Model versus Family-Related-Model versus Prusiner Model

Prion disease; viroid Model versus Family-Related-Model versus Prusiner Model

2004-06-23 12:30:15 PM
On Tue, 22 Jun 2004 01:40:55 -0500, Archimedes Plutonium
<a_plutonium@iw.net>wrote:
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Call them Retroviruses. There is evidence of the latter but immense
suppression in the science literature thereof. In the Finkel report, she
says evidence of shreds of DNA and RNA are found in prion proteins.
AFAIK (and not very sure)... there is no definable, reproducible
nucleic acid in good prion preps. What little there is is presumably
random cellular debris. Those who have looked hard for viruses in
"prions" have presumably analyzed this hard.
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Just today in the news is report that a woman in Florida died of the Mad Cow
variant CJD which she contracted in England some 10 years ago. The rate of
incubation does not match the Prusiner Model.

nonsense. Read what I wrote earlier on this. The model makes no such
prediction at all. It is rare that any disease model does.
Somewhere... I read that known mutations in the Pr gene cause
variations of 10^4 fold in conversion rate. That should make it clear
that the basic, core model cannot possibly predict any rates.
bob
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Re:Prion disease; viroid Model versus Family-Related-Model versus Prusiner Model

On Tue, 22 Jun 2004 02:20:07 -0500, Archimedes Plutonium
<a_plutonium@iw.net>wrote:
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I have proposed that we toss out the Prusiner Model and start anew with the
methodology that advances in the understanding of Alzheimers and Parkinsons
will advance prion disease. So that approach will guide research.

There is nothing inconsistent about using both approaches; they are
quite complementary. I suspect they address different parts of the
problem.
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>>
>>Why invoke a protein molecule that has a hard time of traveling and of
>>circulating
>
>Huh? Blood proteins do that routinely.

Bob, you have never addressed the issue of whether PrP can pass the blood
brain barrier and if so, whether easily or with difficulty. I suppose with
its metal ions in the prion molecule that it is difficult.
My recollection is...
1. It isn't well understood.
2. It is thought that the PrP enters thru nervous system, not thru
blood, so the bbb is not really an issue.
3. Oral infection is inefficient, compared to inoculation into the
brain.
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>>and of infecting when a virus can easily do that. And why
>>invoke a protein to initiate the disease when a virus can more easily
>>initiate the disease by altering the gene code of its victim.
>
>No reason to believe that it involves altering the gene code (gene
>function?) at all. But if it does, then it is likely that a protein
>would do that; that is a common major role for proteins.
>

I thought the major role was to build the body and not rewire the genetics.
Read about Jacob/Monod, 1960. Nobel prize a few years later. One of
the largest class of proteins is those that bind and control DNA.
Why don’t you go read about this stuff. Biology is neat! Then you will
even have some basis for talking about it.
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>
>Given the poor infectivity of prions, not even sure that it helps with
>that point. And disease action is ultimately due to proteins in any
>case, so it is simpler to just use the protein. (I'm not trying to
>suggest that my argument here is "right", merely that one can argue
>most anything here. We need data.)

The more persuasive argument is that viruses purpose in life is to cause and
create diseases
Uh, no. Viruses do not have purpose. Or, if you prefer, their purpose
is to replicate. Viruses need not cause disease -- any more than
prions need to. (Of course, we are more likely to recognize those that
have an effect, and that effect is most often negative. But that is a
problem with our perspective, not with the viruses.)
But my point was that we do not solve these matters with arguments,
but with data.
bob
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