2-WAY CLEAVAGE OF BETA-AMYLOID PROTEIN-PRECURSOR BY MULTICATALYTIC PROTEINASE

被引：33

作者：

KOJIMA, S

OMORI, M

机构：

[1] Research Institute, Sumitomo Pharmaceuticals Co., Konohana-Ku, Osaka, 554, 1-98

来源：

FEBS LETTERS | 1992年 / 304卷 / 01期

关键词：

BETA-AMYLOID PROTEIN PRECURSOR; MULTICATALYTIC PROTEINASE; MACROPAIN; RAT BRAIN; CALCIUM ION;

D O I：

10.1016/0014-5793(92)80588-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The beta-amyloid protein (beta-AP) derived from a beta-amyloid protein precursor (APP) is a hallmark of Alzheimer's disease. The abundant generation of beta-AP suggests the abnormal processing of APP, but the molecular mechanism remains unclear. The main APP-processing enzyme was purified from the rat brain and identified to be a macropain-like multicatalytic proteinase. The purified enzyme cleaved the Gln15-Lys16 bond of beta-AP, but altered to cleave at the N-terminus of beta-AP to release the extracellular domain of beta-AP in the presence of Ca2+. These findings suggest that the functional change in this multicatalytic proteinase may result in abnormal processing of APP.

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页码：57 / 60

页数：4

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