Processing of the beta-amyloid precursor protein in ex vivo human brain cells

被引：7

作者：

Jung, SS ^{[1
]}

Cashman, NR ^{[1
]}

机构：

[1] McGill Univ, Montreal Neurol Inst, Dept Microbiol & Immunol, Montreal, PQ, Canada

来源：

NEUROREPORT | 1999年 / 10卷 / 18期

关键词：

Alzheimer's Disease; amyloid beta; amyloid precursor protein; brain cells; human; oligomer; processing;

D O I：

10.1097/00001756-199912160-00028

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

WE studied distribution and processing of the Alzheimer's beta-amyloid precursor protein (beta APP) in immediately ex vivo human brain cells obtained during neurosurgical procedures. Immunoblotting and flow cytometry studies revealed that brain cells supported beta APP as a transmembrane holoprotein. Brain cells in short-term suspension culture were competent to process beta APP into A beta as shown by [S-35]methionine pulse-chase studies. Brain cell AP was immunoprecipitated as SDS-stable dimers and higher-order multimers. Cleavage of cell surface beta APP with trypsin prior to metabolic labeling reduced cellular A beta by similar to 50%. We conclude that plasmalemmal beta APP in human brain cells is a source of cellular A beta, presumably via endosomal-lysosomal processing. (C) 1999 Lippincott Williams & Wilkins.

引用

页码：3875 / 3879

页数：5

共 25 条

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