Structural aspects and physiological consequences of APP/APLP trans-dimerization.
Exp Brain Res
; 217(3-4): 389-95, 2012 Apr.
Article
en En
| MEDLINE
| ID: mdl-21952790
The amyloid precursor protein (APP) is one of the key proteins in Alzheimer's disease (AD), as it is the precursor of amyloid ß (Aß) peptides accumulating in amyloid plaques. The processing of APP and the pathogenic features of especially Aß 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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Precursor de Proteína beta-Amiloide
/
Multimerización de Proteína
/
Proteínas del Tejido Nervioso
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Exp Brain Res
Año:
2012
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Alemania