Amyloid peptide precursor' metabolism and presenilins

被引：5

作者：

Checler, F ^{[1
]}

do Costa, CA ^{[1
]}

Dumanchin-Njock, C ^{[1
]}

Lopez-Perez, E ^{[1
]}

Marambaud, P ^{[1
]}

Paitel, E ^{[1
]}

Petit, A ^{[1
]}

Vincent, B ^{[1
]}

机构：

[1] CNRS, Inst Pharmacol Mol & Cellulaire, UMR 6097, F-06560 Valbonne, France

来源：

M S-MEDECINE SCIENCES | 2002年 / 18卷 / 6-7期

关键词：

D O I：

10.1051/medsci/20021867717

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Alzheimers' disease is characterized by extracellular deposits called senile plaques, that are mainly composed by the amyloid-beta peptide (Abeta). This peptide derives from the sequential proteolysis of a precursor protein (betaAPP) by beta- and gamma-secretases. Familial forms of Alzheimer's disease are due to autosomal dominant mutations on the genes encoding betaAPP and two homologous proteins called presenilins. This paper reviews the physiopathological processing of the betaAPP, the mechanisms by which presenilins influence such pathways and their control by the proteasome, and recent advances concerning the potential nature of the secretases.

引用

页码：717 / 724

页数：8

共 44 条

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