(APP is processed differently in AD patients over time in a way that generates Aβ fragments more likely to oligomerize.Īβ/amyloid is not recycled properly - and the excess creates conditions necessary for oligomerization. (your idea): Aβ is not 'used up', creating excess that allows for oligomerization. Other factors accumulate that make it more likely for Aβ to oligomerize. (I realize that you wrote that comment later, I'm just attaching it here to make one I think is a logical continuation of your above exchange) I don't think any of these ideas are mutually exclusive with others, and it is quite possible more than one - or other possibilities - may be modulating plaque formation.Īβ not being used up is not the prevailing theory (I think the prevailing theory is usually APP gets cleaved in ways that favor Aβ forming plaques). The reason many people believe abeta to play a role in the development of alzheimers, stems from it being found in plaques of diseased patients. But the best clue is that familial alzheimers / early onset alzheimers has been linked to mutations in genes coding for either APP or proteins that interact with abeta. As to why removing/preventing plaques does not cure or stop disease progression, might relate to the fact that oligomeric species forming on/off-pathway towards amyloid plaques can also be extremely toxic to cells.
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