'Shadoo' prion sheds light on BSE, page 1
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Topic started on 27-8-2007 @ 07:15 AM by astmonster

'Shadoo' prion sheds light on BSE


www.newscientist.com
PRION diseases such as BSE and variant Creutzfeldt-Jakob disease (vCJD) just got more complicated.

These diseases destroy the brain when a wrongly folded version of a prion protein called PrP begins converting normal PrP - which usually protects the brain - into the misfolded variety. Researchers had suspected that other types of prion might exist in the brain, but none had ever been identified - until now.

(visit the link for the full news article)


reply posted on 27-8-2007 @ 07:27 AM by flice
reply to post by astmonster



So basicly the hype that was on about it being cause by fx. bad meat from cows is now out of the loop? Meaning that the disease in fact already is in us and bad meat is merely in some cases a triggereffect?

This would mean that there could be other triggereffects or could it happen randomly too?

[edit on 27/8/07 by flice]



reply posted on 27-8-2007 @ 08:38 PM by astmonster
reply to post by flice



Prion have no known "enemies" they "accumulate" they never "DIE", they clump together in fish, vegetables, heck............everywhere.

They are just "protein"....how they infect others is unknown.

Search the ATS archives........


reply posted on 27-8-2007 @ 08:59 PM by Tom Bedlam
reply to post by flice



No, that's not what the article is saying. They're saying there are multiple types of "good" prions, and that they'd found a second one they named "shadoo", and that it complements the normal PrP prion.

You produce these normally. The issue is when they misfold. When proteins are made, they're intended to fold a certain way. The usefulness of most proteins depends on their shapes, and on the pattern of electrical charges on them.

The structure of the proteins normally determines how they fold, but it's not always the only way they can fold, and the other shape(s) they can assume may be useless or harmful. There are other enzymes and what are called "chaperone" molecules which either re-fold, denature or destroy the errant proteins.

You produce some misfolded proteins as a matter of statistics, but you destroy them, normally. Other proteins may be misfolded in a way which you have no enzymes or chaperones to deal with, and they accumulate. Worse, they may come in contact with normally folded proteins and cause them to misfold as well.

That's the case with errant prions, at least the vCJD and Kuru types, I'm sure there are others.

It really hasn't got beans to do with "electromagnetic contamination", whatever that might be. Protein folding is a really complex issue, and it's really easy for it to "go wrong". Kuru is a prion disease, and was known to infect the Fore before 1900, scrapie is a prion disease of sheep and has been recorded back as far as the mid 1700's. That sort of rules out "electromagnetic contamination" as a possibility, if you consider you have defensive systems against this sort of thing in your cells that also tells you the general problem exists all the time. It's just that the vCJD and Kuru prions (and now possibly a misfolded shadoo) are things you have no defensive systems tailored for specifically.


reply posted on 30-8-2007 @ 08:08 PM by astmonster
reply to post by Tom Bedlam



Actually prion related disease tend to group around or near bio-research facilities that used high speed centrifuge. The prions ended up as clumps of "contamination" at the bottom of the test tubes and were simply flushed down drains. There they accumulated in the surrounding environment. Example is the "ground zero" location of the western deer and elk CWD near the rocky mountian bio-research facility in upstate colorado.

The source of prion related diease dates farther back than even 1700's, however, since the "electric" revolution the prion has exploded. Several leading theories include electromagnetic contamination on the atomic level that alter the folding of the prion. Others include chemicals and still other the filtering and accumulation around research facilities.
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