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Proteins central to the pathology of Alzheimer’s disease act as prions – study

ucsf.edu

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Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#31

Post by jrumbut »

jeffdavis wrote: post #16

How does a protein come to be misfolded? Is it a random mutation that happens to be self-propagating? Is it different between alzheimers and other ones like mad cow?

I have no idea what the mechanisms affecting protein folding are in this context, but if you are interested in learning more about how proteins fold and perhaps helping researchers fold interesting new ones, check out FoldIt (a protein folding citizen science project): https://fold.it/portal/

It was featured in Werner Herzog's Lo and Behold and I had the privilege of taking a class taught by a professor involved in its development. The community there can do a little bit to restore your faith in humanity and technology.

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#33

Post by labster »

thanatropism wrote: post #18
dreamcompiler wrote: post #3

This is an absolutely astonishing game-changer for Alzheimer's research. The scientist who discovered prions (and got a Nobel prize for it) now has convincing evidence that the proteins that cause Alzheimer's are themselves prions. Amazing, scary, and hopeful all at the same time.

Well, when you’re an authority on prions everything looks like a prion disease.

As a web developer, I'm curious if Alzheimer's is really a cross-site scripting attack. If so, we could prevent it by encoding the amino entities, and that would be a game changer.

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#35

Post by autokad »

outlace wrote: post #28

Taken out of context, the press release makes this finding look a lot more ground-breaking than it is after I quickly read through the actual study. Still a good piece of work though. It was already known, as pointed out in the actual paper, that Amyloid-beta (AB) and Tau, the proteins that have long been implicated in Alzheimer's disease (AD), have prion-like properties which means they exist in an abnormal 3D confi…

could that be interpreted as the ones with trash balls (NFTs) might actually be the ones handling it 'better'?

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#36

Post by wahern »

thaumasiotes wrote: post #20
josephagoss wrote: post #7

Does this mean that inflammation of the brain is to be ruled out as a cause?

cheesymuffin's comment is downvoted, but I think he's on to something. It would be very odd to consider inflammation of the brain to be a cause of any problem, because inflammation is a symptom of something else.

Inflammation often is directly causative, for example atherosclerosis where the inflammatory response directly results in the buildup of plaques. Inflammation is not typically the root cause, however; something else instigates the inflammation.

The distinction matters because the best treatment (greatest efficacy, most cost efficient) may target one or more of the links in the causative chain, but not necessarily the root cause.

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#37

Post by robbiep »

jmpman wrote: post #12

How does this mesh with the gingivitis correlation?

There is an inflammatory correlation as well, it may be simply that.

I have been out of the AD literature for about 6 years but back in Med school read every major paper from the 80s onwards. The flip flop between tau and AB as the causative agent was very interesting

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#38

Post by bboygravity »

amyloid_tau wrote: post #2

Pretty awesome work. Looks like we don’t have obvious ways to avoid these classes of proteins in the same way we can just avoid tainted meat and abstain from cannibalism... https://en.wikipedia.org/wiki/Amyloid https://en.wikipedia.org/wiki/Tau_protein

Or do we?

People taking acyclovir regularly (to suppress HSV1 and 2 symptoms) have been found to have a 10 fold decrease in risk of getting Alzheimer's (Taiwanese study).

https://www.medicalnewstoday.com/articles/322463.php

Additional studies are currently ongoing to confirm this in the US.

The scientific "journalists" seem to jump to the conclusion that therefor HSV1,2 must be cuasal for Alzheimer's. But it could be that Acyclovir somehow prevents or slows the formation of AB tau prion-like forms (and has nothing to do with the herpes - Alzheimer's causality).

Or. Some Acyclovir prevents Alzheimer's through a completely different mechanism we don't know about yet.

My point: effective medication may already be there. We just don't know how it works yet.

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#39

Post by autokad »

cjbprime wrote: post #14

Y'all, please never post university press releases about single scientific studies . They are the worst thing. Every major human problem has been declared solved by one of them. They are even worse than posting single scientific study papers themselves at the time of publication, and that's still pretty bad, because of the overwhelming incentive to create exciting studies that are wrong, and our current inability to…

one of the authors discovered prions, so I am not so quick to discount their work.

Re: Proteins central to the pathology of Alzheimer’s disease act as prions – study

#40

Post by robbiep »

jeffdavis wrote: post #16

How does a protein come to be misfolded? Is it a random mutation that happens to be self-propagating? Is it different between alzheimers and other ones like mad cow?

Thermodynamics.

Certain proteins have a propensity to Misfold, this is driven by the folding conformations as well as by Heat Shock Proteins. The underlying genetics that drive amino acid sequence are the basis for this. In the best known prion disease, Mad Cow, one misfolded protein drives other similar proteins it runs into to induce the same conformation. Due to the thermodynamics of folding, it is now in a very stable structure and won’t revert to its original or desired biological structure, is difficult or impossible to clear, and will cause other proteins to fold in the same way.

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