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Characterization of mouse tissue kallikrein 5

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/18640

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)

Submitter: 高橋 孝行

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