Title

The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer's Beta Amyloid

Document Type

Journal Article

Publisher

Springer

Faculty

Computing, Health and Science

School

Exercise, Biomedical and Health Science

RAS ID

5103

Comments

This article was originally published as: Verdile, G. , Gandy, S. , & Martins, R. N. (2007). The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer's Beta Amyloid. Neurochemical Research, 32(4-5), 609-623. Original article available here. The original publication is available at www.springerlink.com

Abstract

The biogenesis and accumulation of the beta amyloid protein (Ab) is a key event in the cascade of oxidative and inflammatory processes that characterises Alzheimer’s disease. The presenilins and its interacting proteins play a pivotal role in the generation of Ab from the amyloid precursor protein (APP). In particular, three proteins (nicastrin, aph-1 and pen-2) interact with presenilins to form a large multi-subunit enzymatic complex (c-secretase) that cleaves APP to generate Ab. Reconstitution studies in yeast and insect cells have provided strong evidence that these four proteins are the major components of the c-secretase enzyme. Current research is directed at elucidating the roles that each of these protein play in the function of this enzyme. In addition, a number of presenilin interacting proteins that are not components of c-secretase play important roles in modulating Ab production. This review will discuss the components of the c-secretase complex and the role of presenilin interacting proteins on c-secretase activity.

DOI

10.1007/s11064-006-9131-x

 

Link to publisher version (DOI)

10.1007/s11064-006-9131-x