Biogenesis and metabolism of Alzheimer's disease Aβ amyloid peptides

被引：150

作者：

Evin, G ^{[1
]}

Weidemann, A

机构：

[1] Univ Melbourne, Dept Pathol, Parkville, Vic 3010, Australia

[2] Mental Hlth Res Inst, Parkville, Vic 3010, Australia

[3] Heidelberg Univ, ZMBH, Ctr Mol Biol, D-69120 Heidelberg, Germany

来源：

PEPTIDES | 2002年 / 23卷 / 07期

基金：

英国医学研究理事会;

关键词：

secretase; protease; protease inhibitors; amyloid; peptide vaccine; presenilin; Alzheimer's disease;

D O I：

10.1016/S0196-9781(02)00063-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Biochemical and genetic evidence indicates the balance of biogenesis/clearance of Abeta amyloid peptides is altered in Alzheimer's disease. Abeta is derived, by two sequential cleavages, from the receptor-like amyloid precursor protein (APP). The proteases involved are beta-secretase, identified as the novel aspartyl protease BACE, and gamma-secretase, a multimeric complex containing the presenilins (PS). gamma-Secretase can release either Abeta40 or the more aggregating and cytotoxic Abeta42. Secreted Abeta peptides become either degraded by the metalloproteases insulin-degrading enzyme (IDE) and neprilysin or metabolized through receptor uptake mediated by apolipoprotein E. Therapeutic approaches based on secretase inhibition or amyloid clearance are currently under development. (C) 2002 Published by Elsevier Science Inc.

引用

页码：1285 / 1297

页数：13

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