Characterization of mouse tissue kallikrein 5

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

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)963-968
Number of pages6
JournalZoological science
Issue number11
Publication statusPublished - Nov 2006


  • Characterization
  • Kallikrein 5
  • Mouse
  • Protease
  • Recombinant enzyme

ASJC Scopus subject areas

  • Animal Science and Zoology


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