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Functional characterization of Kunitz domains in hepatocyte growth factor activator inhibitor type 2
Author(s) -
Qin Li,
Denda Kimitoshi,
Shimomura Takeshi,
Kawaguchi Toshiya,
Kitamura Naomi
Publication year - 1998
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/s0014-5793(98)01105-3
Subject(s) - activator (genetics) , chemistry , hepatocyte , microbiology and biotechnology , hepatocyte growth factor , biochemistry , biology , receptor , in vitro
Hepatocyte growth factor activator inhibitor type 2 (HAI‐2) was identified as a potent inhibitor of hepatocyte growth factor activator (HGF activator). The primary translation product of HAI‐2 contains two Kunitz domains. To characterize their function, we introduced a point mutation into the reactive site of each Kunitz domain, and assayed the mutants for their HGF activator inhibitory activity. A point mutation in the COOH‐terminal Kunitz domain did not affect the activity of HAI‐2, whereas a point mutation in the NH 2 ‐terminal Kunitz domain markedly reduced the activity. These results suggest that the NH 2 ‐terminal Kunitz domain is mainly responsible for the HGF activator inhibitory activity of HAI‐2.