Characterization of mouse tissue kallikrein 5

Rajapakse, Sanath; Ogiwara, Katsueki; Yamano, Noriko; Kimura, Atsushi; Hirata, Kensaku; Takahashi, Sumio; Takahashi, Takayuki

Characterization of mouse tissue kallikrein 5

Rajapakse, Sanath; Ogiwara, Katsueki; Yamano, Noriko et al.

ZOOLOGICAL SCIENCE, 2006, 23(11), 963-968

Permalink : https://hdl.handle.net/2115/18640

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論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/18640
タイトル	Characterization of mouse tissue kallikrein 5
著者	Rajapakse, Sanath ; Ogiwara, Katsueki ; Yamano, Noriko ; Kimura, Atsushi ; Hirata, Kensaku ; Takahashi, Sumio ; Takahashi, Takayuki
著者名 Rajapakse, Sanath
e-Rad_Researcher 00422006 著者名 Ogiwara, Katsueki
著者名 Yamano, Noriko
e-Rad_Researcher 90422005 著者名 Kimura, Atsushi
著者名 Hirata, Kensaku
著者名 Takahashi, Sumio
e-Rad_Researcher 80197152 著者名 Takahashi, Takayuki
言語	英語
キーワード	mouse
	protease
	kallikrein 5
	recombinant enzyme
	characterization
発行日	2006-11
出版者	Zoological Society of Japan
収録物名	ZOOLOGICAL SCIENCE
巻(号)	23(11)
ページ	963-968
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0289-0003
関連情報	PMID 17189908
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.2108/zsj.23.963