Matrix metalloproteinase 10 promotion of collagenolysis via procollagenase activation: implications for cartilage degradation in arthritis
| Autor: | Angela M. Patterson, T. Robson, Tim E. Cawston, H. E. Barksby, Jim Middleton, J. M. Milner, N. J. Peake, Wang Hui, Andrew D. Rowan, Carl D. Richards, Rachel L. Lakey |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Pathology
medicine.medical_specialty Immunology Connective tissue Arthritis Cartilage metabolism Oncostatin M Matrix metalloproteinase Arthritis Rheumatoid Mice Chondrocytes Rheumatology Matrix Metalloproteinase 10 Osteoarthritis medicine Immunology and Allergy Synovial fluid Animals Humans Pharmacology (medical) Collagenases Cells Cultured Enzyme Precursors biology business.industry Cartilage Synovial Membrane Fibroblasts medicine.disease Growth Inhibitors medicine.anatomical_structure Matrix Metalloproteinase 8 Gene Expression Regulation biology.protein Tumor necrosis factor alpha Cattle Collagen Matrix Metalloproteinase 1 business Interleukin-1 |
| Zdroj: | Arthritis and rheumatism. 54(10) |
| ISSN: | 0004-3591 |
| Popis: | Objective We have previously reported the up-regulation of matrix metalloproteinase 10 (MMP-10) following treatment with the procatabolic stimulus of interleukin-1 (IL-1) and oncostatin M (OSM) in chondrocytes. Although MMP-10 is closely related to MMP-3, little is known about the role of MMP-10 in cartilage catabolism. The purpose of this study was to determine whether MMP-10 is expressed in connective tissue cells and to assess how it may contribute to cartilage collagenolysis. Methods MMP gene expression was assessed by real-time polymerase chain reaction using RNA from human articular chondrocytes and synovial fibroblasts stimulated with IL-1 plus OSM or tumor necrosis factor α (TNFα) plus OSM. Synovial fluid levels of MMP-10 were determined by specific immunoassay. Recombinant procollagenases were used in activation studies. Immunohistochemistry assessed MMP-10 expression in diseased joint tissues. Results MMP-10 expression was confirmed in both chondrocytes and synovial fibroblasts following stimulation with either IL-1 plus OSM or TNFα plus OSM, and MMP-10 was detected in synovial fluid samples from patients with various arthropathies. Exogenous MMP-10 significantly enhanced collagenolysis from IL-1 plus OSM–stimulated cartilage, and MMP-10 activated proMMP-1, proMMP-8, and proMMP-13. Immunohistochemistry revealed the presence of MMP-10 in the synovium and cartilage of an IL-1 plus OSM–induced model of arthritis as well as in samples of diseased human tissues. Conclusion We confirm that both synovial fibroblasts and articular chondrocytes express MMP-10 following treatment with procatabolic stimuli. Furthermore, the detectable levels of synovial fluid MMP-10 and the histologic detection of this proteinase in diseased joint tissues strongly implicate MMP-10 in the cartilage degradome during arthritis. The ability of MMP-10 to superactivate procollagenases that are relevant to cartilage degradation suggests that this activation represents an important mechanism by which this MMP contributes to tissue destruction in arthritis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text