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

被引：0
作者：
Giuseppe Verdile
Samuel E Gandy
Ralph N. Martins
机构：
[1] Edith Cowan University,Centre of Excellence for Alzheimer’s disease Research and Care, and the Sir James McCusker Alzheimer’s Disease Research Unit, School of Exercise, Biomedical and Health Sciences
[2] Hollywood Private Hospital,School of Psychiatry and Clinical Neurosciences
[3] University of Western Australia,Farber Institute for Neurosciences
[4] Thomas Jefferson University,undefined
来源：
Neurochemical Research | 2007年 / 32卷
关键词：
Alzheimer’s disease; Amyloid precursor protein; Beta amyloid; Presenilin; Interacting proteins; Gamma secretase;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The biogenesis and accumulation of the beta amyloid protein (Aβ) 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 Aβ 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 (γ-secretase) that cleaves APP to generate Aβ. Reconstitution studies in yeast and insect cells have provided strong evidence that these four proteins are the major components of the γ-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 γ-secretase play important roles in modulating Aβ production. This review will discuss the components of the γ-secretase complex and the role of presenilin interacting proteins on γ-secretase activity.
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页码：609 / 623
页数：14
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