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P3‐027: ROLES OF P75 IN AMYLOIDOGENIC PROCESSING OF APP
Author(s) -
Zhou XinFu,
Saadipour Khalil,
Wang YanJiang
Publication year - 2014
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2014.05.1114
Subject(s) - hek 293 cells , pathogenesis , amyloid precursor protein secretase , transfection , immunoprecipitation , amyloid precursor protein , chemistry , microbiology and biotechnology , biology , alzheimer's disease , disease , medicine , receptor , immunology , biochemistry , gene
changes of TMDs by SCAM. Results: We found that both TMD4 and 5 directly face the hydrophilic catalytic pore in the membrane. Especially, cytosolic sides of these TMDs locate in proximity to the catalytic aspartate in TMD7, suggesting that TMD4 and 5 participate in the catalytic site structure. Notably, the distance between I213 in TMD4 and L383 in TMD7 was altered by FAD-linked mutation and GSM-1 in an opposite manner. Conclusions: Proximity between cytoplasmic sides of TMD4 and 7 of PS1 is correlated with Abeta42 production.