The role of oncostatin M in animal and human connective tissue collagen turnover and its localization within the rheumatoid joint
Autor: | P. J. T. Koshy, Graham P. Riley, J. R. Spaull, P. F. Life, C. A. Summers, V. A. Curry, Tim E. Cawston, Andrew D. Rowan, Ian M. Clark, Mary B. Goldring, W. D. Shingleton |
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Rok vydání: | 1998 |
Předmět: |
Pathology
medicine.medical_specialty biology business.industry Cartilage fungi Immunology Oncostatin M Connective tissue Matrix metalloproteinase Molecular biology Chondrocyte medicine.anatomical_structure Rheumatology Proteoglycan Collagenase biology.protein Immunology and Allergy Medicine Synovial fluid Pharmacology (medical) business medicine.drug |
Zdroj: | Arthritis & Rheumatism. 41:1760-1771 |
ISSN: | 1529-0131 0004-3591 |
Popis: | Objective. To study the interaction of interleukin-la (IL-la) and oncostatin M (OSM) in promoting cartilage collagen destruction. Methods. Bovine, porcine, and human cartilage and human chondrocytes were studied in culture. The levels of collagenase (matrix metalloproteinase 1 [MMP-I]) and tissue inhibitor of metalloproteinases 1 (WMP-1) were measured by bioassay and enzyme-linked immunosorbent assay (ELISA). The levels of OSM in rheumatoid synovial fluid were measured by ELISA. Results. When combined with OSM, 1L-la, ILlp, and tumor necrosis factor a released proteoglycan and collagen from cartilage. OSM was the only member of the IL-6 family to have this effect. Human tendon also responded to IL-la and OSM. OSM increased the production of MMP-1 and TIMP-1 but when combined with IL-la, synergistically promoted MMP-1 production in human chondrocytes and synovial fibroblasts. High levels of OSM were found in human rheumatoid synovial fluids, and confocal microscopy showed that OSM was produced by macmphages in rheumatoid synovial tissue. Conclusion. These results highlight an important |
Databáze: | OpenAIRE |
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