[HTML][HTML] Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa
M Peek, P Moran, N Mendoza… - Journal of Biological …, 2002 - ASBMB
Hepatocyte growth factor (HGF), the ligand for the receptor tyrosine kinase c-Met, is
composed of an α-chain containing four Kringle domains (K1–K4) and a serine protease
domain-like β-chain. Receptor activation by HGF is contingent upon prior proteolytic
conversion of the secreted inactive single chain form (pro-HGF) into the biologically active
two chain form by a single cleavage at the Arg 494-Val 495 bond. By screening a panel of
serine proteases we identified two new HGF activators, plasma kallikrein and coagulation …
composed of an α-chain containing four Kringle domains (K1–K4) and a serine protease
domain-like β-chain. Receptor activation by HGF is contingent upon prior proteolytic
conversion of the secreted inactive single chain form (pro-HGF) into the biologically active
two chain form by a single cleavage at the Arg 494-Val 495 bond. By screening a panel of
serine proteases we identified two new HGF activators, plasma kallikrein and coagulation …