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

The biogenesis and accumulation of the beta amyloid protein (Aß) 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 Aß from the amyloid precursor protein (...

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Main Authors: Verdile, Giuseppe, Gandy, S., Martins, R.
Format: Journal Article
Published: Kluwer Academic Publishers-Plenum Publishers 2007
Online Access:http://hdl.handle.net/20.500.11937/14145
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author Verdile, Giuseppe
Gandy, S.
Martins, R.
author_facet Verdile, Giuseppe
Gandy, S.
Martins, R.
author_sort Verdile, Giuseppe
building Curtin Institutional Repository
collection Online Access
description The biogenesis and accumulation of the beta amyloid protein (Aß) 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 Aß 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 (?-secretase) that cleaves APP to generate Aß. Reconstitution studies in yeast and insect cells have provided strong evidence that these four proteins are the major components of the ?-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 ?-secretase play important roles in modulating Aß production. This review will discuss the components of the ?-secretase complex and the role of presenilin interacting proteins on ?-secretase activity.
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spelling curtin-20.500.11937-141452017-09-13T15:02:44Z The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid Verdile, Giuseppe Gandy, S. Martins, R. The biogenesis and accumulation of the beta amyloid protein (Aß) 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 Aß 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 (?-secretase) that cleaves APP to generate Aß. Reconstitution studies in yeast and insect cells have provided strong evidence that these four proteins are the major components of the ?-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 ?-secretase play important roles in modulating Aß production. This review will discuss the components of the ?-secretase complex and the role of presenilin interacting proteins on ?-secretase activity. 2007 Journal Article http://hdl.handle.net/20.500.11937/14145 10.1007/s11064-006-9131-x Kluwer Academic Publishers-Plenum Publishers unknown
spellingShingle Verdile, Giuseppe
Gandy, S.
Martins, R.
The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title_full The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title_fullStr The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title_full_unstemmed The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title_short The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid
title_sort role of presenilin and its interacting proteins in the biogenesis of alzheimer’s beta amyloid
url http://hdl.handle.net/20.500.11937/14145