Structural aspects and physiological consequences of APP/APLP trans-dimerization

被引：35
作者：
Baumkoetter, Frederik [1 ]
Wagner, Katja [1 ]
Eggert, Simone [1 ]
Wild, Klemens [1 ]
Kins, Stefan [1 ]
机构：
[1] Tech Univ Kaiserslautern, Dept Human Biol & Human Genet, D-67663 Kaiserslautern, Germany
来源：
EXPERIMENTAL BRAIN RESEARCH | 2012年 / 217卷 / 3-4期
关键词：
Alzheimer disease; APLP-1; APLP-2; Dimerization; Cell adhesion; Synaptogenesis; AMYLOID PRECURSOR PROTEIN; ALPHA-SECRETASE CLEAVAGE; CELL-ADHESION; GENE FAMILY; APP FAMILY; FE65; BINDING; EXPRESSION; MEMBERS; DOMAIN;
D O I：
10.1007/s00221-011-2878-6
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
The amyloid precursor protein (APP) is one of the key proteins in Alzheimer's disease (AD), as it is the precursor of amyloid beta (A beta) peptides accumulating in amyloid plaques. The processing of APP and the pathogenic features of especially A beta oligomers have been analyzed in detail. Remarkably, there is accumulating evidence from cell biological and structural studies suggesting that APP and its mammalian homologs, the amyloid precursor-like proteins (APLP1 and APLP2), participate under physiological conditions via trans-cellular dimerization in synaptogenesis. This offers the possibility that loss of synapses in AD might be partially explained by dysfunction of APP/APLPs cell adhesion properties. In this review, structural characteristics of APP trans-cellular interaction will be placed critically in context with its putative physiological functions focusing on cell adhesion and synaptogenesis.
引用
收藏
页码：389 / 395
页数：7
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