Structural Features of Human Memapsin 2 (β-Secretase) and Their Biological and Pathological Implications


Lin Hong;Xiang-Yuan He;Xiang-Ping Huang;Wan-Pin Chang;Jordan Tang

Key Words

memapsin 2 ; β-secretase ; Alzheimer's disease ; β-amyloid ; β-amyloid precursor protein ; aspartic protease ; endocytosis ; cellular trafficking


Acta Biochimica et Biophysica Sinica

Volume or Term/Year and Month of Publication

36卷12期(2004 / 12 / 01)

Page #

787 - 792

Content Language


English Abstract

Memapsin 2 (β-secretase) is the membrane-anchored aspartic protease that initiates the cleavage of -amyloid precursor protein (APP) leading to the production of amyloid-β (Aβ), a major factor in the pathogenesis of Alzheimer's disease (AD). Since memapsin 2 is a major target for the development of inhibitor drugs for AD, it has been intensively studied during the past five years. Here we discuss the structural features of the catalytic/specificity apparatus, transmembrane domain, cytosolic domain and the implications of these features in the physiological and pathological roles of this protease.

Topic Category 基礎與應用科學 > 物理
基礎與應用科學 > 化學
生物農學 > 生物科學