INHIBITORY SPECTRA OF PURIFIED PROTEASE NEXIN-II AND RELATED PROTEINS TOWARDS CELLULAR PROTEINASES

被引：9

作者：

SHIMOKAWA, M

NAKAMURA, K

MARUYAMA, K

TAGAWA, K

MIYATAKE, T

SUGITA, H

ISHIURA, S

SUZUKI, K

机构：

[1] NATL INST NEUROSCI,TOKYO 187,JAPAN

[2] TOKYO MED & DENT UNIV,DEPT NEUROL,TOKYO 113,JAPAN

[3] TOKYO METROPOLITAN INST MED SCI,DEPT MOLEC BIOL,TOKYO 113,JAPAN

[4] UNIV TOKYO,INST MOLEC & CELLULAR BIOSCI,TOKYO 113,JAPAN

来源：

BIOCHIMIE | 1993年 / 75卷 / 10期

关键词：

ALZHEIMERS DISEASE; AMYLOID PRECURSOR PROTEIN; PROTEASE NEXIN-II; INHIBITION OF SERINE PROTEASE; COS-1; CELL;

D O I：

10.1016/0300-9084(93)90048-W

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：

Amyloid beta protein (beta/A4) is deposited in senile plaques of patients with Alzheimer's disease. This protein is derived from a larger membrane-associated protein, termed amyloid precursor protein (APP). The constitutive processing of APP occurs at the central portion of beta/A4, resulting in the release of large N-terminal peptides. We have purified these peptides from the culture medium of cDNA-transfected COS-1 cells. Some of the isoforms contain the Kunitz-type protease inhibitor (KPI) domain and strongly inhibit trypsin, chymotrypsin and plasmin, but do not inhibit kallikrein, prolyl endopeptidase or granzyme A. The peptides also do not inhibit cysteine proteases such as cathepsin B or calpain. Soluble APPs lacking the KPI domain fail to inhibit any of these proteases. The results indicate that the KPI domain in soluble APPs has protease inhibitory activity against certain serine proteases.

引用

页码：911 / 915

页数：5

共 24 条

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