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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science / Faculty of Science >
Peer-reviewed Journal Articles, etc >
Characterization of mouse tissue kallikrein 5
| Title: | Characterization of mouse tissue kallikrein 5 |
| Authors: | Rajapakse, Sanath Browse this author | | Ogiwara, Katsueki Browse this author →KAKEN DB | | Yamano, Noriko Browse this author | | Kimura, Atsushi Browse this author →KAKEN DB | | Hirata, Kensaku Browse this author | | Takahashi, Sumio Browse this author | | Takahashi, Takayuki Browse this author →KAKEN DB |
| Keywords: | mouse | | protease | | kallikrein 5 | | recombinant enzyme | | characterization |
| Issue Date: | Nov-2006 |
| Publisher: | Zoological Society of Japan |
| Journal Title: | ZOOLOGICAL SCIENCE |
| Volume: | 23 |
| Issue: | 11 |
| Start Page: | 963 |
| End Page: | 968 |
| Publisher DOI: | 10.2108/zsj.23.963 |
| PMID: | 17189908 |
| Abstract: | Mouse tissue kallikreins (Klks) are members of a large, multigene family consisting of 37 genes, 26 of which can code for functional proteins. Mouse tissue kallikrein 5 (Klk5) has long been thought to be one of these functional genes, but the gene product, mK5, has not been isolated and characterized. In the present study, we prepared active recombinant mK5 using an Escherichia coli expression system, followed by column chromatography. We then determined the biochemical and enzymatic properties of purified mK5. mK5 had trypsin-like activity for Arg at the P1 position, and its activity was inhibited by typical serine protease inhibitors. mK5 degraded gelatin, fibronectin, collagen type IV, high-molecular-weight kininogen, and insulin-like growth factor binding protein-3. Our data suggest that mK5 may be implicated in the process of extracellular matrix remodeling. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/18640 |
| Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 荻原 克益
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