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Re: falconer66a post# 102946

Tuesday, 04/25/2017 8:24:12 PM

Tuesday, April 25, 2017 8:24:12 PM

Post# of 461441
Misfolded proteins have a tendency to aggregate. Is an example of this phenomenon a-beta protein aggregating into amyloid plagues? If we assume that a-beta is a misfolded protein, where does it get misfolded? I watched the linked 2' video and it doesn't show a-beta becoming misfolded. It shows APP, residing across the cell membrane, being clipped by enzymes to form a-beta, which is promptly expelled from the cell via exocytosis. This is happening at the cell membrane, not at the MAM.

The video leads one to believe all a-beta that is produced is immediately expelled from the cell; however, I have read or heard that a-beta can be found inside the cell too. I haven't verified to my satisfaction that a-beta can also be found inside cells. If it in fact does occur, I don't know how that happens.

To my knowledge, all amyloid plague is extracellular, whereas Tau is intracellular.

Considering the aforementioned, what does the MAM have to do with formation of a-beta?

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