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Licensed Unlicensed Requires Authentication Published by De Gruyter March 20, 2010

Interdependence of kallikrein-related peptidases in proteolytic networks

  • Nathalie Beaufort , Karolina Plaza , Daniel Utzschneider , Amelie Schwarz , Julia M. Burkhart , Sabine Creutzburg , Mekdes Debela , Manfred Schmitt , Christian Ries and Viktor Magdolen
From the journal Biological Chemistry

Abstract

Human kallikrein-related peptidases (KLKs) are 15 homologous serine proteases involved in several (patho)physiological processes, including cancer. Secreted as precursors, they are activated upon proteolytic release of a short pro-peptide. We searched for interconnection of KLKs within extracellular proteolytic networks leading to activation of protease zymogens and found that (i) pro-KLK activation by other KLKs is scarce, with the exception of pro-KLK11, which is efficiently activated by KLK4 and 5; (ii) pro-KLK4 is activated by matrix metalloproteinase 3; and (iii) trypsin-like KLKs efficiently activate the serine protease urokinase. Our observations provide new insights into the regulation of these important tumor-associated proteases.


Corresponding author

Received: 2010-1-5
Accepted: 2010-2-9
Published Online: 2010-3-20
Published in Print: 2010-5-1

©2010 by Walter de Gruyter Berlin New York

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