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Biology of presenilins as causative molecules for Alzheimer disease
Author(s) -
Nishimura Masaki,
Yu Gang,
St GeorgeHyslop Peter H
Publication year - 1999
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1034/j.1399-0004.1999.550401.x
Subject(s) - presenilin , biology , amyloid precursor protein , missense mutation , transmembrane protein , genetics , microbiology and biotechnology , alzheimer's disease , mutation , gene , disease , receptor , medicine , pathology
Many missense mutations in the presenilins are associated with autosomal dominant forms of familial Alzheimer disease (AD). 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, apoptosis signal pathways, and processing of selected proteins including β‐amyloid precursor protein. Although the underlying mechanism in which presenilin mutations lead to development of AD remains elusive, one consistent mutational effect is an overproduction of long‐tailed amyloid β‐peptides. Furthermore, presenilins interact with β‐catenin to form presenilin complexes and presenilin mutations effect β‐catenin signalling pathways.