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Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis
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Michael Blaber
Published/Copyright:
February 3, 2010
Abstract
A large body of emerging evidence indicates a functional interaction between the kallikrein-related peptidases (KLKs) and proteases of the thrombostasis axis. These interactions appear relevant for both normal health as well as pathologies associated with inflammation, tissue injury, and remodeling. Regulatory interactions between the KLKs and thrombostasis proteases could impact several serious human diseases, including neurodegeneration and cancer. The emerging network of specific interactions between these two protease families appears to be complex, and much work remains to elucidate it. Complete understanding how this functional network resolves over time, given specific initial conditions, and how it might be controllably manipulated, will probably contribute to the emergence of novel diagnostics and therapeutic agents for major diseases.
Keywords: activation cascade; kallikrein; kallikrein-related peptidase (KLK); plasmin; thrombogenesis; thrombolysis; thrombostasis
Received: 2009-10-10
Accepted: 2009-11-22
Published Online: 2010-02-03
Published in Print: 2010-04-01
©2010 by Walter de Gruyter Berlin New York
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- 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
activation cascade;
kallikrein;
kallikrein-related peptidase (KLK);
plasmin;
thrombogenesis;
thrombolysis;
thrombostasis
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
