Functional characterization of human hepatocyte growth factor mutants obtained by deletion of structural domains.
作者： Mitsuhiko Okigaki , Masayuki Komada , Yoshihiko Uehara , Keiji Miyazawa , Naomi Kitamura
DOI: 10.1021/BI00155A007
关键词: DNA synthesis 、 Cell growth 、 Mutant protein 、 Growth factor 、 Cell biology 、 Tyrosine phosphorylation 、 Mutant 、 Kringle domain 、 Biology 、 Biochemistry 、 Immunoglobulin light chain
摘要: Human hepatocyte growth factor (hHGF) consists of characteristic structural domains. In this study, we prepared mutant proteins lacking each these domains and examined their biological activities for stimulation DNA synthesis, inhibition Meth A cell growth, induction MDCK dissociation. We also interactions with the c-met/HGF receptor by competition analysis levels tyrosine phosphorylation. The N-terminal, first kringle, or second kringle domain were not biologically effective could compete hHGF bound to receptor. results indicate that are necessary mediated binding third fourth moderately retained binding. relative phosphorylation correlated well potencies when compared wild-type hHGF. protein light chain was in receptor, but competed These suggest heavy plays an important role interaction is further required
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