The Biochemistry and Regulation of S100A10: A Multifunctional Plasminogen Receptor Involved in Oncogenesis
| Autor: | Alexi P. Surette, Patricia A. Madureira, David M. Waisman, Paul A. O'Connell, Victoria A Miller |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Plasmin
Health Toxicology and Mutagenesis Cytosolic Phospholipase A(2) Regulator lcsh:Medicine Human epithelial-cells Review Article medicine.disease_cause chemistry.chemical_compound 0302 clinical medicine Acute promyelocytic leukemia Epidermal growth factor Annexin-Ii tetramer Disease Receptor Annexin A2 Light-chain P11 0303 health sciences biology S100 Proteins General Medicine Cell Transformation Neoplastic Biochemistry Organ Specificity 030220 oncology & carcinogenesis Molecular Medicine Keratinocyte growth factor Ef-hand proteins Biotechnology medicine.drug Calcium-binding proteins lcsh:Biotechnology Molecular Sequence Data Calpactin-I Receptors Urokinase Plasminogen Activator 03 medical and health sciences lcsh:TP248.13-248.65 Genetics medicine Animals Humans Amino Acid Sequence Molecular Biology 030304 developmental biology Site-directed mutagenesis lcsh:R S100A10 chemistry Cancer cell biology.protein Human peripheral monocytes Carcinogenesis |
| Zdroj: | Journal of Biomedicine and Biotechnology Journal of Biomedicine and Biotechnology, Vol 2012 (2012) Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| ISSN: | 1110-7251 1110-7243 |
| DOI: | 10.1155/2012/353687 |
| Popis: | The plasminogen receptors mediate the production and localization to the cell surface of the broad spectrum proteinase, plasmin. S100A10 is a key regulator of cellular plasmin production and may account for as much as 50% of cellular plasmin generation. In parallel to plasminogen, the plasminogen-binding site on S100A10 is highly conserved from mammals to fish. S100A10 is constitutively expressed in many cells and is also induced by many diverse factors and physiological stimuli including dexamethasone, epidermal growth factor, transforming growth factor-alpha, interferon-gamma, nerve growth factor, keratinocyte growth factor, retinoic acid, and thrombin. Therefore, S100A10 is utilized by cells to regulate plasmin proteolytic activity in response to a wide diversity of physiological stimuli. The expression of the oncogenes, PML-RAR alpha and KRas, also stimulates the levels of S100A10, suggesting a role for S100A10 in pathophysiological processes such as in the oncogenic-mediated increases in plasmin production. The S100A10-null mouse model system has established the critical role that S100A10 plays as a regulator of fibrinolysis and oncogenesis. S100A10 plays two major roles in oncogenesis, first as a regulator of cancer cell invasion and metastasis and secondly as a regulator of the recruitment of tumor-associated cells, such as macrophages, to the tumor site. Canadian Cancer Society Research Institute; Canadian Institutes of Health Research; Foundation for Science and Technology of Portugal |
| Databáze: | OpenAIRE |
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