ID | 47725 |
FullText URL | |
Author |
Rajapakse, Sanath
Ogiwara, Katsueki
Yamano, Noriko
Kimura, Atsushi
Hirata, Kensaku
Takahashi, Takayuki
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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 (KIk5) 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.
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Keywords | mouse
protease
kallikrein 5
recombinant enzyme
characterization
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Published Date | 2006-11
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Publication Title |
Zoological Science
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Volume | volume23
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Issue | issue11
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Publisher | Zoological Society of Japan
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Publisher Alternative | 日本動物学会
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Start Page | 963
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End Page | 968
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ISSN | 0289-0003
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NCID | AA10545874
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Content Type |
Journal Article
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language |
English
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Copyright Holders | © 2006 Zoological Society of Japan
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File Version | publisher
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Refereed |
True
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DOI | |
PubMed ID | |
Web of Science KeyUT |