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