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(Received for publication, August 6, 1996, and in revised form, November 7, 1996)
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From the Hepatocyte growth factor (HGF) activator is a
serine protease that is produced and secreted by the liver and
circulates in the blood as an inactive zymogen. In response to tissue
injury, the HGF activator zymogen is converted to the active form by
limited proteolysis. The activated HGF activator converts an inactive single chain precursor of HGF to a biologically active heterodimer in
injured tissue. The activated HGF may be involved in the regeneration of the injured tissue. In this study, we purified an inhibitor of HGF
activator from the conditioned medium of a human MKN45 stomach
carcinoma cell line and molecularly cloned its cDNA. The sequence
of the cDNA revealed that the inhibitor has two well defined Kunitz
domains, suggesting that the inhibitor is a member of the Kunitz family
of serine protease inhibitors. The sequence also showed that the
primary translation product of the inhibitor has a hydrophobic sequence
at the COOH-terminal region. Inhibitory activity toward HGF activator
was detected in the membrane fraction as well as in the conditioned
medium of MKN45 cells. These results suggest that the inhibitor may be
produced as a membrane-associated form and secreted by the producing
cells as a proteolytically truncated form.
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