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, Viktor Magdolen
2010 Biological chemistry  
AbstractHuman 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
more » ... 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.
doi:10.1515/bc.2010.055 pmid:20302517 fatcat:vglxkiszvbe4ln6iqimfqcw6sq