2. Academic Validation
  3. Inhibition of kallikrein-related peptidases by the serine protease inhibitor of Kazal-type 6

Inhibition of kallikrein-related peptidases by the serine protease inhibitor of Kazal-type 6

  • Peptides. 2011 Jun;32(6):1187-92. doi: 10.1016/j.peptides.2011.03.009.
Tomasz Kantyka 1,  Jan Fischer,  Zhihong Wu,  Wim Declercq,  Karina Reiss,  Jens-Michael Schröder,  Ulf Meyer-Hoffert
Affiliations

Affiliation

  • 1 Department of Dermatology, University Hospital Schleswig-Holstein, Campus Kiel, Schittenhelmstr. 7, D-24105 Kiel, Germany.
PMID: 21439340 DOI: 10.1016/j.peptides.2011.03.009
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.

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