Presenilin structure, function and role in Alzheimer disease

Fraser, Paul E, Yang, Dun-Sheng, Yu, Gang, Lévesque, Lyne, Nishimura, Masaki, Arawaka, Shigeki, Serpell, Louise, Rogaeva, Ekaterina and St George-Hyslop, Peter (2000) Presenilin structure, function and role in Alzheimer disease. BBA - Molecular Basis of Disease, 1502 (1). ISSN 0925-4439

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Abstract

Numerous missense mutations in the presenilins are associated with the autosomal dominant form of familial Alzheimer disease. Presenilin genes encode polytopic transmembrane proteins, which are processed by proteolytic cleavage and form high-molecular-weight complexes under physiological conditions. The presenilins have been suggested to be functionally involved in developmental morphogenesis, unfolded protein responses and processing of selected proteins including the ß-amyloid precursor protein. Although the underlying mechanism by which presenilin mutations lead to development of Alzheimer disease remains elusive, one consistent mutational effect is an overproduction of long-tailed amyloid ß-peptides. Furthermore, presenilins interact with ß-catenin to form presenilin complexes, and the physiological and mutational effects are also observed in the catenin signal transduction pathway.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Louise Serpell
Date Deposited: 06 Feb 2012 21:11
Last Modified: 11 Jun 2012 10:03
URI: http://sro.sussex.ac.uk/id/eprint/30071
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