PROTEOLYTIC ACTIVATION OF A SINGLE-CHAIN PRECURSOR OF HEPATOCYTE GROWTH-FACTOR BY EXTRACELLULAR SERINE-PROTEASE

被引：53

作者：

MIZUNO, K ^{[1
]}

TAKEHARA, T ^{[1
]}

NAKAMURA, T ^{[1
]}

机构：

[1] KYUSHU UNIV,FAC SCI,DEPT BIOL,FUKUOKA 812,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 189卷 / 03期

关键词：

D O I：

10.1016/0006-291X(92)90264-L

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：

Hepatocyte growth factor (HGF) is biosynthesized as a single-chain precursor (pro-HGF) and is proteolytically processed to a two-chain mature form. When MRC-5 fibroblasts were pulse-radiolabeled under serum-free conditions, pro-HGF was the predominant molecular form of HGF in the culture medium. CHO cells transfected with an expression plasmid containing a full-size human HGF cDNA produced pro-HGF when these cells were cultured in serum-free medium. These findings suggest that HGF is secreted as a pro-form, which is then converted to a two-chain form by extracellular protease. Single-chain HGF exhibited mitogenic activity on cultured hepatocytes, with a potency similar to that of mature HGF, but this activity was remarkably inhibited by leupeptin. We postulate that inactive pro-HGF is converted to an active two-chain form by a leupeptin-sensitive serine-protease expressed by hepatocytes. Neither plasminogen activators nor plasmin showed any processing activity of pro-HGF in vitro. © 1992.

引用

页码：1631 / 1638

页数：8

共 23 条

[21] ISOLATION AND EXPRESSION OF CDNA FOR DIFFERENT FORMS OF HEPATOCYTE GROWTH-FACTOR FROM HUMAN-LEUKOCYTE [J].