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P3‐326: Neprilysin regulates the anatomical distribution of amyloid pathology in an age‐dependent manner
Author(s) -
Farris Wesley,
Peng Ying,
Lemere Cindy A.,
Selkoe Dennis J.,
Kovács Krisztina
Publication year - 2008
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.2008.05.1895
Subject(s) - neprilysin , cerebral amyloid angiopathy , hippocampal formation , amyloid precursor protein , amyloid (mycology) , subiculum , genetically modified mouse , pathology , human brain , alzheimer's disease , biology , endocrinology , medicine , neuroscience , dementia , dentate gyrus , transgene , disease , gene , biochemistry , enzyme
ation has no effect on gamma-secretase complex assembly. We are presently characterizing the roles of S -palmitoylation in gamma-secretase neuronal trafficking and activity towards intramembranous cleavage of APP and other substrates. Conclusions: In summary, we have observed that nicastrin and APH-1 undergo S-palmitoylation. We also showed that this posttranslational modification increases the stability of nicastrin and APH-1 and targets nicastrin and APH-1 to lipid rafts.