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

共 49 条

[21] Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes [J].

Matsuzaki, K ;

Horikiri, C .

BIOCHEMISTRY, 1999, 38 (13) :4137-4142

[22] Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest [J].

McLaurin, J ;

Franklin, T ;

Chakrabartty, A ;

Fraser, PE .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 278 (01) :183-194

[23] The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells [J].

Morishima-Kawashima, M ;

Ihara, Y .

BIOCHEMISTRY, 1998, 37 (44) :15247-15253

[24] Alzheimer's disease: a re-examination of the amyloid hypothesis [J].

Neve, RL ;

Robakis, NK .

TRENDS IN NEUROSCIENCES, 1998, 21 (01) :15-19

[25] Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein [J].

Parkin, ET ;

Turner, AJ ;

Hooper, NM .

BIOCHEMICAL JOURNAL, 1999, 344 :23-30

[26] Characterization of detergent-insoluble complexes containing the familial Alzheimer's disease-associated presenilins [J].

Parkin, ET ;

Hussain, I ;

Karran, EH ;

Turner, AJ ;

Hooper, NM .

JOURNAL OF NEUROCHEMISTRY, 1999, 72 (04) :1534-1543

[27]

Parkin ET, 1997, J NEUROCHEM, V69, P2179

[28] Cleavage of Alzheimer's amyloid precursor protein by α-secretase occurs at the surface of neuronal cells [J].

Parvathy, S ;

Hussain, I ;

Karran, EH ;

Turner, AJ ;

Hooper, NM .

BIOCHEMISTRY, 1999, 38 (30) :9728-9734

[29] Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors:: Similarities to the angiotensin converting enzyme secretase [J].

Parvathy, S ;

Hussain, I ;

Karran, EH ;

Turner, AJ ;

Hooper, NM .

BIOCHEMISTRY, 1998, 37 (06) :1680-1685

[30]

PIKE CJ, 1993, J NEUROSCI, V13, P1676

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