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

被引：44

作者：

Kantyka, Tomasz ^{[1
,2
]}

Fischer, Jan ^{[1
]}

Wu, Zhihong ^{[1
]}

Declercq, Wim ^{[3
,4
]}

Reiss, Karina ^{[1
]}

Schroeder, Jens-Michael ^{[1
]}

Meyer-Hoffert, Ulf ^{[1
]}

机构：

[1] Univ Hosp Schleswig Holstein, Dept Dermatol, D-24105 Kiel, Germany

[2] Jagiellonian Univ, Fac Biochem Biophys & Biotechnol, Dept Microbiol, PL-30387 Krakow, Poland

[3] VIB, Dept Mol Biomed Res, Mol Signaling & Cell Death Unit, Ghent, Belgium

[4] Univ Ghent, Dept Biomed Mol Biol, B-9000 Ghent, Belgium

来源：

PEPTIDES | 2011年 / 32卷 / 06期

关键词：

Atopic dermatitis; Prostate cancer; Epidermal barrier; Protease inhibitor; HUMAN SKIN; NETHERTON-SYNDROME; STRATUM-CORNEUM; GENE FAMILY; EXPRESSION; LEKTI; IDENTIFICATION; DESQUAMATION; DEGRADATION; ACTIVATION;

D O I：

10.1016/j.peptides.2011.03.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 1 nM, KLK4 with K-i = 27.3 nM, KLK6 with K-i = 140 nM, caspase-14 with a K-i approximating 1 mu M and no activity against KLK1, KLK3 and KLK11. Taken together, SPINK6 is a potent inhibitor of distinct KLKs members. (C) 2011 Elsevier Inc. All rights reserved.

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收藏

页码：1187 / 1192

页数：6

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