Inhibition profiles of human tissue kallikreins by serine protease inhibitors.
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. alpha2-Antiplasmin, alpha1-antichymotrypsin, and alpha1-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.
Luo
Liu-Ying
LY
R&D Systems, Inc., 614 McKinley Place N.E., Minneapolis, MN 55413, USA. liuyingl@rndsystems.com
Jiang
Weiping
W
D045744:Cell Line, Tumor; D005260:Female; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D020840:Tissue Kallikreins / Q000037:antagonists & inhibitors* / Q000235:genetics; D014162:Transfection
D015842:Serine Proteinase Inhibitors; D020840:Tissue Kallikreins