A structural network associated with the kallikrein-kinin and renin-angiotensin systems
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Veronika Stoka
Abstract
The kallikrein-kinin and renin-angiotensin (KKS-RAS) systems represent two highly regulated proteolytic systems that are involved in several physiological and pathological processes. Although their protein-protein interactions can be studied using experimental approaches, it is difficult to differentiate between direct physical interactions and functional associations, which do not involve direct atomic contacts between macromolecules. This information can be obtained from an atomic-resolution characterization of the protein interfaces. As a result of this, various three-dimensional-based protein-protein interaction databases have become available. To gain insight into the multilayered interaction of the KKS-RAS systems, we present a protein network that is built up on three-dimensional domain-domain interactions. The essential domains that link these systems are as follows: Cystatin, Peptidase_C1, Thyroglobulin_1, Insulin, CIMR (Cation-independent mannose-6-phosphate receptor repeat), fn2 (Fibronectin type II domain), fn1 (Fibronectin type I domain), EGF, Trypsin, and Serpin. We found that the CIMR domain is located at the core of the network, thus connecting both systems. From the latter, all domain interactors up to level 4 were retrieved, thus displaying a more comprehensive representation of the KKS-RAS structural network.
©2010 by Walter de Gruyter Berlin New York
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
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
