Alzheimer's disease: Its origin at the membrane, evidence and questions

被引：16

作者：

Buchet, R ^{[1
]}

Pikula, S

机构：

[1] Univ Lyon 1, UFR Chim Biochim, Lab Physicochim Biol, CNRS,UMR 5013, F-69622 Villeurbanne, France

[2] M Nencki Inst Expt Biol, Dept Cellular Biochem, PL-02093 Warsaw, Poland

来源：

ACTA BIOCHIMICA POLONICA | 2000年 / 47卷 / 03期

关键词：

beta-amyloid precursor protein; membrane proteases; lipid composition; membrane microdomains; Alzheimer's disease;

D O I：

10.18388/abp.2000_3991

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：

Numerous results on membrane lipid composition from different regions of autopsied Alzheimer's disease brains in comparison with corresponding fractions isolated from control brains revealed significant differences in serine- and ethanolamine-containing glycerophospholipid as well as in glycosphingolipid content. Changes in membrane lipid composition are frequently accompanied by alterations in membrane fluidity, hydrophobic mismatch, lipid signaling pathways, transient formation and disappearance of lipid microdomains, changes in membrane permeability to cations and variations of other membrane properties. In this review we focus on possible implications of altered membrane composition on beta-amyloid precursor protein (APP) and on proteolysis of APP leading eventually to the formation of neurotoxic beta-amyloid (A beta) peptides, the major proteinaceous component of extracellular senile plaques, directly involved in Alzheimer's disease pathogenesis.

引用

页码：725 / 733

页数：9

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