Two‐way cleavage of β‐amyloid protein precursor by multicatalytic proteinase

FEBS Letters

Kojima, Shin-ichi¹  Omori, Motoko¹ 

[1] Research Institute, Sumitomo Pharmaceuticals Co., 1-98, Kasugade Naka 3-Chome, Konohana-Ku, Osaka 554, Japan

关键词: β-Amyloid protein precursor;    Multicatalytic proteinase;    Macropain;    Rat brain;    Calcium ion;   

DOI  :  10.1016/0014-5793(92)80588-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The β-amyloid protein (β-AP) derived from a β-amyloid protein precursor (APP) is a hallmark of Alzheimer's disease. The abundant generation of β-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 β-AP, but altered to cleave at the N-terminus of β-AP to release the extracellular domain of β-AP in the presence of Ca²⁺. These findings suggest that the functional change in this multicatalytic proteinase may result in abnormal processing of APP.

【 授权许可】

Unknown