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Journal of Biochemistry Advance Access published online on March 10, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp036
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Role of the Stem Domain of Matriptase in the Interaction with its Physiological Inhibitor, Hepatocyte Growth Factor Activator Inhibitor Type I

Kenji Kojima1, Satoshi Tsuzuki2, Tohru Fushiki2 and Kuniyo Inouye1,*

1Laboratory of Enzyme Chemistry and 2Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

*To whom correspondence should be addressed: Tel: +81-75-753-6266, Fax:+81-75-753-6265, E-mail inouye{at}kais.kyoto-u.ac.jp.

Received December 30, 2008; Accepted February 23, 2009


  Abstract

Matriptase is a type II transmembrane serine protease containing the non-catalytic domains (stem domain) and catalytic domain in the extracellular region. Our aim is to address the role of the stem domain in the interaction between matriptase and its physiological inhibitor, hepatocyte growth factor activator inhibitor type I (HAI-1). We prepared secreted variants of recombinant matriptase containing the entire extracellular domain (HL-matriptase) or only the catalytic domain (L-matriptase), and compared the inhibition activities of a cell membrane-anchored form of recombinant HAI-1 (maHAI-1) against the matriptase variants in the hydrolysis of peptidyl–4-methyl-coumaryl-7-amide (MCA) substrates. HL-matriptase and L-matriptase were inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl (Boc)-Gln-Ala-Arg-MCA (1) and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA (2) were used as substrates. However, HL-matriptase was inhibited more strongly than L-matriptase by maHAI-1 in the hydrolysis of Boc-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-MCA (3). These results show that the stem domain of matriptase facilitates the inhibitory interaction of this protease with maHAI-1 in the hydrolysis of substrate 3, although it has no effect in the hydrolysis of substrates 1 and 2. To our knowledge, this is the first evidence that the stem domain of matriptase can affect the interaction between this protease and HAI-1.

Key Words: hepatocyte growth factor activator inhibitor type I, inhibitory interaction, matriptase, membrane-type serine protease, stem domain


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