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Proteolytic processing of the hepatocyte growth factor/scatter factor receptor by furin
Author(s) -
Komada Masayuki,
Hatsuzawa Kiyotaka,
Shibamoto Sayumi,
Ito Fumiaki,
Nakayama Kazuhisa,
Kitamura Naomi
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80958-w
Subject(s) - furin , hepatocyte growth factor , autophosphorylation , receptor , receptor tyrosine kinase , insulin like growth factor 1 receptor , biology , tyrosine kinase , growth factor receptor , microbiology and biotechnology , growth factor , chemistry , signal transduction , biochemistry , phosphorylation , protein kinase a , enzyme
The hepatocyte growth factor/scatter factor (HGF/SF) receptor consists of an α‐ and a β‐subunit, which are derived from a single‐chain precursor by endoproteolytic processing. The precursor is not proteolytically processed in LoVo colon carcinoma cells. The uncleaved receptor immunopurified from the cells was cleaved in vitro by furin. Furthermore, the HGF/SF receptor was proteolytically processed in LoVo cells transfected with furin cDNA. These results indicate that furin is a processing endoprotease for the HGF/SF receptor. Tyrosine autophosphorylation of the uncleaved receptor was induced by HGF/SF, and the growth of the cells expressing the uncleaved receptor was stimulated by HGF/SF, indicating that the proteolytic processing of the receptor is not essential for the signal transduction of HGF/SF.