Multiple matrix metalloproteinases in type II collagen induced arthritis

被引:17
作者
Sandya S. [1 ]
Achan M.A. [2 ]
Sudhakaran P.R. [1 ]
机构
[1] Department of Biochemistry, University of Kerala, Kariavattom
[2] Department of Orthopedics, Medical College and Hospital
关键词
Matrix metalloproteinases; Osteoarthritis; Synovial effusate; Synovial fluid;
D O I
10.1007/s12291-009-0007-0
中图分类号
学科分类号
摘要
To study the relative contribution of various matrix degrading enzymes in the pathogenesis of arthritis, changes in the levels of various matrix metalloprtoteinases (MMPs) during the progression of collagen induced arthritis was studied in experimental animals. Arthritis was induced in male wistar rats by injecting an emulsion containing collagen type II and Freund's complete adjuvant. The duration of the experiment was 35 days. Synovial effusate was collected at regular intervals after induction. At the end of the experiment serum and cartilage were collected and analysed. Synovial fluid of osteoarthritic patients was also analyzed. Levels of MMP-2, MMP-3, MMP-9 and MT1-MMP were found to be high in synovial effusate and cartilage of experimental animals. In synovial effusate of arthritic animals the expression of MMP-3 was found to be high during the early stages while increase in MMP-2 and MMP-9 occurred at later stages. Synovial fluid of osteoarthritic patients also showed elevated levels of MMP-2, MMP-3 and MMP-9. Our results indicated that sequential action of MMPs such as MMP-3, MMP-2 and MMP-9 can cause degradation of articular cartilage extracellular matrix. © 2009 Association of Clinical Biochemists of India.
引用
收藏
页码:42 / 48
页数:6
相关论文
共 34 条
[1]
Lotz M., Hashimoto S., Kuhn K., Mechanisms of chondrocyte apoptosis, Osteoarthritis and Cartilage, 7, 4, pp. 389-391, (1999)
[2]
Buttle D.J., Bramwell H., Hollander A.P., Proteolytic mechanisms of cartilage breakdown: A target for arthritis therapy?, Clin Pathol Mol Pathol, 48, pp. 167-177, (1995)
[3]
Murphy G., Reynolds J.J., Current views of collagen degradation. Progress towards understanding the resorption of connective tissues, Bio Essays, 2, pp. 55-60, (1985)
[4]
Didem Kozaci L., Buttle D.J., Hollander A.P., Degradation of type II collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures, Arthritis and Rheumatism, 40, 1, pp. 164-174, (1997)
[5]
Makowski G.S., Ramsby M.L., Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: Correlation to polymorphonuclear leukocyte infiltration and in response to infection, Clinica Chimica Acta, 329, 1-2, pp. 77-81, (2003)
[6]
Matrisian L.M., The matrix-degrading metalloproteinases, Bio Essays, 14, pp. 455-463, (1992)
[7]
Murphy G., Hembry R.M., Hughes C.E., Fosang A.J., Hardingham T.E., Role and regulation of metalloproteinases in connective tissue turnover, Biochemical Society Transactions, 18, 5, pp. 812-815, (1990)
[8]
Murphy G., Reynolds J.J., Hembry R.M., Metalloproteinases and cancer invasion and metastasis, International Journal of Cancer, 44, 4, pp. 757-759, (1989)
[9]
Nagase H., Woessner Jr. J.F., Matrix metalloproteinases, Journal of Biological Chemistry, 274, 31, pp. 21491-21494, (1999)
[10]
Cawston T., Matrix metalloproteinases and TIMPs: Properties and implications for the rheumatic diseases, Molecular Medicine Today, 4, 3, pp. 130-137, (1998)