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Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
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Katerina Oikonomopoulou
Published/Copyright:
February 24, 2010
Abstract
The exact mechanism(s) by which kallikrein-related peptidases (KLKs) function, their levels of activity and their potential endogenous targets in vivo have only recently begun to be revealed. Our group and others have shown that KLKs can have hormonal properties by signaling via proteinase-activated receptors (PARs), a family of G-protein-coupled receptors. Signals by PAR1, PAR2, and PAR4 can regulate calcium release or mitogen-activated protein kinase activation and lead to platelet aggregation, vascular relaxation, cell proliferation, cytokine release, and inflammation. We have further documented the presence of active KLK6 and 10 (by activity-based ELISA or proteomics) and the presence of proteinase inhibitors, such as α1-antitrypsin, in cancer-derived fluids. We suggest that tumors and inflamed tissues can release active KLKs, which are under tight regulation by proteinase inhibitors. These enzymes can potentially control cell/tissue behavior by regulating PAR activation in specific settings and disease stages.
Keywords: hormone; inflammation; kallikrein-related peptidases; proteases; proteinase-activated receptors; proteinases; signaling; trypsin
Received: 2009-11-2
Accepted: 2010-1-11
Published Online: 2010-02-24
Published in Print: 2010-04-01
©2010 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Guest Editorial
- The 3rd International Symposium on Kallikreins and Kallikrein-Related Peptidases
- HIGHLIGHT: 3RD INTERNATIONAL SYMPOSIUM ON KALLIKREINS AND KALLIKREIN-RELATED PEPTIDASES
- Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
- Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
- Kallikrein-related peptidases: bridges between immune functions and extracellular matrix degradation
- Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer
- Tissue kallikrein in cardiovascular, cerebrovascular and renal diseases and skin wound healing
- Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia
- Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
- Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid
- Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer
- Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
- Dysregulation of kallikrein-related peptidases in renal cell carcinoma: potential targets of miRNAs
- Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
- Increased blood pressure and water intake in transgenic mice expressing rat tonin in the brain
- A structural network associated with the kallikrein-kinin and renin-angiotensin systems
- Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
- Expression of PSA-RP2, an alternatively spliced variant from the PSA gene, is increased in prostate cancer tissues but the protein is not secreted from prostate cancer cells
- KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
- Identification of IGFBP-3 fragments generated by KLK2 and prevention of fragmentation by KLK2-inhibiting peptides
Keywords for this article
hormone;
inflammation;
kallikrein-related peptidases;
proteases;
proteinase-activated receptors;
proteinases;
signaling;
trypsin
Articles in the same Issue
- Guest Editorial
- The 3rd International Symposium on Kallikreins and Kallikrein-Related Peptidases
- HIGHLIGHT: 3RD INTERNATIONAL SYMPOSIUM ON KALLIKREINS AND KALLIKREIN-RELATED PEPTIDASES
- Kallikrein-related peptidases: proteolysis and signaling in cancer, the new frontier
- Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
- Kallikrein-related peptidases: bridges between immune functions and extracellular matrix degradation
- Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer
- Tissue kallikrein in cardiovascular, cerebrovascular and renal diseases and skin wound healing
- Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia
- Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
- Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid
- Polyclonal antibodies against kallikrein-related peptidase 4 (KLK4): immunohistochemical assessment of KLK4 expression in healthy tissues and prostate cancer
- Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
- Dysregulation of kallikrein-related peptidases in renal cell carcinoma: potential targets of miRNAs
- Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation
- Increased blood pressure and water intake in transgenic mice expressing rat tonin in the brain
- A structural network associated with the kallikrein-kinin and renin-angiotensin systems
- Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
- Expression of PSA-RP2, an alternatively spliced variant from the PSA gene, is increased in prostate cancer tissues but the protein is not secreted from prostate cancer cells
- KLK5 gene expression is severely upregulated in androgen-independent prostate cancer cells after treatment with the chemotherapeutic agents docetaxel and mitoxantrone
- Identification of IGFBP-3 fragments generated by KLK2 and prevention of fragmentation by KLK2-inhibiting peptides
