Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases
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Hyesook Yoon
Abstract
The 15 human kallikrein-related peptidases (KLKs) are clinically important biomarkers and therapeutic 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 regulation. 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 activation relationships among the KLKs with the potential for more extensive activation cascades. More recent work has asked whether functional intersection of KLKs with other types of regulatory proteases exists. Such studies show a capacity for members of the thrombostasis axis to act as broad activators of pro-KLKs. In the present report, we ask whether such functional intersection is possible between the KLKs and the members of the matrix metalloproteinase (MMP) family by evaluating the ability of the MMPs to activate pro-KLKs. The results identify MMP-20 as a broad activator of pro-KLKs, suggesting the potential for intersection of the KLK and MMP axes under pathological dysregulation of MMP-20 expression.
©2012 by Walter de Gruyter Berlin Boston
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Artikel in diesem Heft
- Masthead
- Masthead
- Reviews
- Exosomes: the ideal nanovectors for biodelivery
- Biological applications of the electrochemical sensing of nitric oxide: fundamentals and recent developments
- Minireview
- Cerebral cavernous malformation is a vascular disease associated with activated RhoA signaling
- Research Articles/Short Communications
- Protein Structure and Function
- Diversity, abundance, and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis
- Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment
- An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2
- Reengineering of subtilisin Carlsberg for oxidative resistance
- New insight into the molecular switch mechanism of human Rho family proteins: shifting a paradigm
- Cell Biology and Signaling
- HbG200-mediated preinduction of heme oxygenase-1 improves bile flow and ameliorates pericentral downregulation of Bsep and Mrp2 following experimental liver ischemia and reperfusion
- Effect of silver nanoparticles on human primary keratinocytes
- Multifunctional silica nanoparticles for optical and magnetic resonance imaging
- Proteolysis
- Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases
