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Publication Date:
June 2006
ISSN:
1437-4315
DOI:
10.1515/BC.2006.103

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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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Inhibition profiles of human tissue kallikreins by serine protease inhibitors

Liu-Ying Luo1 / Weiping Jiang2

1.

2.

Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 6, Pages 813–816, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.103, June 2006

Publication History:
Received:
October 31, 2005
Accepted:
March 13, 2006
Published Online:
2006-06-26

Abstract

Accumulated evidence has shown that human tissue kallikreins (hKs), a group of 15 homologous secreted serine proteases, are novel cancer biomarkers. We report here the inhibition profiles of selected hKs, including hK5, hK7, hK8, hK11, hK12, hK13, and hK14, by several common serine protease inhibitors (serpins) found in plasma. The association constants for the binding of serpins to kallikreins were determined and compared. Protein C inhibitor was found to be the fastest-binding serpin for most of these hKs. α2-Antiplasmin, α1-antichymotrypsin, and α1-antitrypsin also showed rapid inhibition of certain hKs. Kallistatin exhibited fast inhibition only with hK7. Our data demonstrate that these hKs are specifically regulated by certain serpins and their distinct inhibition profiles will be valuable aids in various aspects of kallikrein research.

Keywords: association constant; cancer biomarker; kallistatin; protein C inhibitor; serpin

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