| Literature DB >> 21439340 |
Tomasz Kantyka1, Jan Fischer, Zhihong Wu, Wim Declercq, Karina Reiss, Jens-Michael Schröder, Ulf Meyer-Hoffert.
Abstract
Kallikrein-related peptidases (KLKs) are a group of serine proteases, expressed in several tissues. Their activity is regulated by inhibitors including members of the serine protease of Kazal-type (SPINK) family. Recently, we discovered that SPINK6 is expressed in human skin and inhibits KLK5, KLK7, KLK14 but not KLK8. In this study we tested whether SPINK6 inhibits other members of the KLK family and caspase-14. Using chromogenic substrates, SPINK6 exhibited inhibitory activity against KLK12 and KLK13 with K(i) around 1nM, KLK4 with K(i)=27.3nM, KLK6 with K(i)=140nM, caspase-14 with a K(i) approximating 1μM and no activity against KLK1, KLK3 and KLK11. Taken together, SPINK6 is a potent inhibitor of distinct KLKs members.Entities:
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Year: 2011 PMID： 21439340 DOI： 10.1016/j.peptides.2011.03.009
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750