DOI 10.1515/hsz-2012-0249      Biol. Chem. 2012; 394(1): 137–147

Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases Abstract: The 15 human kallikrein-related peptidases (KLKs) are clinically important biomarkers and thera-peutic targets of interest in inflammation, cancer, and neurodegenerative disease. KLKs are secreted as inactive pro-forms (pro-KLKs) that are activated extracellularly by specific proteolytic release of their amino-terminal pro-peptide, and this is a key step in their functional regula-tion. Physiologically relevant KLK regulatory cascades of activation have been described in skin desquamation and semen liquefaction, and work by a large number of investigators has elucidated pairwise and autolytic activa-tion relationships among the KLKs with the potential for more extensive activation cascades. More recent work ha