About this Journal Submit a Manuscript Table of Contents
Mediators of Inflammation
Volume 2013 (2013), Article ID 183653, 6 pages
http://dx.doi.org/10.1155/2013/183653
Clinical Study

Serum Matrix Metalloproteinase-3 in Comparison with Acute Phase Proteins as a Marker of Disease Activity and Radiographic Damage in Early Rheumatoid Arthritis

1Department of Internal Medicine, Faculty of Health Sciences, University of Pretoria, Private Bag X663, Pretoria 0001, South Africa
2Division of Rheumatology, Department of Medicine, Chris Hani Baragwanath Hospital, University of the Witwatersrand, Johannesburg, South Africa
3Medical Research Council Unit for Inflammation and Immunity, Department of Immunology, Faculty of Health Sciences, University of Pretoria and Tshwane Academic Division of the National Health Laboratory Service, Pretoria, South Africa
4Biostatistics and Epidemiology Division, School of Public Health, Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, South Africa

Received 10 December 2012; Accepted 26 February 2013

Academic Editor: Antonio Macciò

Copyright © 2013 Mahmood M. T. M. Ally et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. G. Pratt, J. D. Isaacs, and D. L. Mattey, “Current concepts in the pathogenesis of early rheumatoid arthritis,” Best Practice and Research: clinical Rheumatology, vol. 23, no. 1, pp. 37–48, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. E. Karouzakis, M. Neidhart, R. E. Gay, and S. Gay, “Molecular and cellular basis of rheumatoid joint destruction,” Immunology Letters, vol. 106, no. 1, pp. 8–13, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Kobayashi, S. Naito, H. Enomoto et al., “Serum levels of matrix metalloproteinase 3 (stromelysin 1) for monitoring synovitis in rheumatoid arthritis,” Archives of Pathology and Laboratory Medicine, vol. 131, no. 4, pp. 563–570, 2007. View at Scopus
  4. G. C. Jones, G. P. Riley, and D. J. Buttle, “The role of proteases in pathologies of the synovial joint,” International Journal of Biochemistry and Cell Biology, vol. 40, no. 6-7, pp. 1199–1218, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. E. Galliera, G. Banfi, and M. M. Corsi, “Human bone disorders: pathological role and diagnostic potential of matrix metalloproteinases,” International Journal of Biochemistry and Cell Biology, vol. 42, no. 10, pp. 1590–1593, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. A. M. Manicone and J. K. McGuire, “Matrix metalloproteinases as modulators of inflammation,” Seminars in Cell and Developmental Biology, vol. 19, no. 1, pp. 34–41, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. A. J. Hueber, D. L. Asquith, I. B. McInnes, and A. M. Miller, “Embracing novel cytokines in RA—complexity grows as does opportunity!,” Best Practice and Research, vol. 24, no. 4, pp. 479–487, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. T. E. Cawston and A. J. Wilson, “Understanding the role of tissue degrading enzymes and their inhibitors in development and disease,” Best Practice and Research, vol. 20, no. 5, pp. 983–1002, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Connolly, R. H. Mullan, J. McCormick, et al., “Acute-phase serum amyloid A regulates tumor necrosis factor α and matrix turnover and predicts disease progression in patients with inflammatory arthritis before and after biologic therapy,” Arthritis and Rheumatism, vol. 64, no. 4, pp. 1035–1045, 2012.
  10. C. Chizzolini, N. C. Brembilla, E. Montanari, and M. E. Truchetet, “Fibrosis and immune dysregulation in systemic sclerosis,” Autoimmunity Reviews, vol. 10, no. 5, pp. 276–281, 2011. View at Publisher · View at Google Scholar · View at Scopus
  11. G. Cunnane, F. Oliver, C. Beeton, et al., “Early joint erosions and serum levels of matrix metalloproteinase 1, matrix metalloproteinase 3, and tissue inhibitor of metalloproteinases 1 in rheumatoid arthritis,” Arthritis and Rheumatism, vol. 44, no. 10, pp. 2263–2274, 2001.
  12. Z. Szekanecz and A. E. Koch, “Angiogenesis and its targeting in rheumatoid arthritis,” Vascular Pharmacology, vol. 51, no. 1, pp. 1–7, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. A. Mamehara, T. Sugimoto, D. Sugiyama et al., “Serum matrix metalloproteinase-3 as predictor of joint destruction in rheumatoid arthritis, treated with non-biological disease modifying anti-rheumatic drugs,” Kobe Journal of Medical Sciences, vol. 56, no. 3, pp. E98–E107, 2010. View at Scopus
  14. C. Ribbens, M. Martin y Porras, N. Franchimont et al., “Increased matrix metalloproteinase-3 serum levels in rheumatic diseases: relationship with synovitis and steroid treatment,” Annals of the Rheumatic Diseases, vol. 61, no. 2, pp. 161–166, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. S. Young-Min, T. Cawston, N. Marshall et al., “Biomarkers predict radiographic progression in early rheumatoid arthritis and perform well compared with traditional markers,” Arthritis and Rheumatism, vol. 56, no. 10, pp. 3236–3247, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. D. L. Mattey, N. B. Nixon, P. T. Dawes, W. E. R. Ollier, and A. H. Hajeer, “Association of matrix metalloproteinase 3 promoter genotype with disease outcome in rheumatoid arhtritis,” Genes and Immunity, vol. 5, no. 2, pp. 147–149, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. I. Tchetverikov, L. R. Lard, J. DeGroot et al., “Matrix metalloproteinases-3, -8, -9 as markers of disease activity and joint damage progression in early rheumatoid arthritis,” Annals of the Rheumatic Diseases, vol. 62, no. 11, pp. 1094–1099, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. M. J. Green, A. K. S. Gough, J. Devlin et al., “Serum MMP-3 and MMP-1 and progression of joint damage in early rheumatoid arthritis,” Rheumatology, vol. 42, no. 1, pp. 83–88, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. M. D. Posthumus, P. C. Limburg, J. Westra, M. A. Van Leeuwen, and M. H. Van Rijswijk, “Serum matrix metalloproteinase 3 levels during treatment with sulfasalazine or combination of methotrexate and sulfasalazine in patients with early rheumatoid arthritis,” Journal of Rheumatology, vol. 29, no. 5, pp. 883–889, 2002. View at Scopus
  20. C. Ribbens, B. Andre, J. M. Jaspar et al., “Matrix metalloproteinase-3 serum levels are correlated with disease activity and predict clinical response in rheumatoid arthritis,” Journal of Rheumatology, vol. 27, no. 4, pp. 888–893, 2000. View at Scopus
  21. M. D. Posthumus, P. C. Limburg, J. Westra, M. A. Van Leeuwen, and M. H. Van Rijswijk, “Serum matrix metalloproteinase 3 in early rheumatoid arthritis is correlated with disease activity and radiological progression,” Journal of Rheumatology, vol. 27, no. 12, pp. 2761–2768, 2000. View at Scopus
  22. H. Yamanaka, Y. Matsuda, M. Tanaka, et al., “Serum matrix metalloproteinase 3 as a predictor of the degree of joint destruction during the six months after measurement, in patients with early rheumatoid arthritis,” Arthritis and Rheumatism, vol. 43, no. 4, pp. 852–858, 2000.
  23. N. T. Cheung, P. T. Dawes, K. V. Poulton, W. E. R. Ollier, D. J. Taylor, and D. L. Mattey, “High serum levels of pro-matrix metalloproteinase-3 are associated with greater radiographic damage and the presence of the shared epitope in patients with rheumatoid arthritis,” Journal of Rheumatology, vol. 27, no. 4, pp. 882–887, 2000. View at Scopus
  24. Y. Ichikawa, C. Yamada, T. Horiki, Y. Hoshina, and M. Uchiyama, “Serum matrix metalloproteinase-3 and fibrin degradation product levels correlate with clinical disease activity in rheumatoid arthritis,” Clinical and Experimental Rheumatology, vol. 16, no. 5, pp. 533–540, 1998. View at Scopus
  25. A. So, A. M. Chamot, V. Péclat, and J. C. Gerster, “Serum MMP-3 in rheumatoid arthritis: correlation with systemic inflammation but not with erosive status,” Rheumatology, vol. 38, no. 5, pp. 407–410, 1999. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Kokubun, Y. Imafuku, M. Okada et al., “Serum amyloid A (SAA) concentration varies among rheumatoid arthritis patients estimated by SAA/CRP ratio,” Clinica Chimica Acta, vol. 360, no. 1-2, pp. 97–102, 2005. View at Publisher · View at Google Scholar · View at Scopus
  27. P. W. A. Meyer, B. Hodkinson, M. Ally et al., “Circulating cytokine profiles and their relationships with autoantibodies, acute phase reactants, and disease activity in patients with rheumatoid arthritis,” Mediators of Inflammation, vol. 2010, Article ID 158514, 10 pages, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. B. Hodkinson, E. Musenge, M. Ally, et al., “Response to traditional disease-modifying anti-rheumatic drugs in indigent South Africans with early rheumatoid arthritis,” Clinical Rheumatology, vol. 31, no. 4, pp. 613–619, 2012.
  29. P. W. Meyer, B. Hodkinson, M. Ally, et al., “HLA-DRB1 shared epitope genotyping using the revised classification and its association with circulating autoantibodies, acute phase reactants, cytokines and clinical indices of disease activity in a cohort of South African rheumatoid arthritis patients,” Arthritis Research and Therapy, vol. 13, no. 5, article R160, 2011.
  30. S. Tezenas Du Montcel, L. Michou, E. Petit-Teixeira et al., “New classification of HLA-DRB1 alleles supports the shared epitope hypothesis of rheumatoid arthritis susceptibility,” Arthritis and Rheumatism, vol. 52, no. 4, pp. 1063–1068, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. P. A. Gourraud, J. F. Boyer, T. Barnetche et al., “A new classification of HLA-DRB1 alleles differentiates predisposing and protective alleles for rheumatoid arthritis structural severity,” Arthritis and Rheumatism, vol. 54, no. 2, pp. 593–599, 2006. View at Publisher · View at Google Scholar · View at Scopus
  32. A. A. Tadbir, S. Purshahidi, H. Ebrahimi et al., “Serum level of MMP-3 in patients with oral squamous cell carcinoma—lack of association with clinico-pathological features,” Asian Pacific Journal of Cancer Prevention, vol. 13, no. 9, pp. 4545–4548, 2012. View at Publisher · View at Google Scholar
  33. J. M. Jordan, “Cartilage oligomeric matrix protein as a marker of osteoarthritis,” Journal of Rheumatology, vol. 31, no. 70, pp. 45–49, 2004. View at Scopus
  34. K. Migita, Y. Kawabe, M. Tominaga, T. Origuchi, T. Aoyagi, and K. Eguchi, “Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts,” Laboratory Investigation, vol. 78, no. 5, pp. 535–539, 1998. View at Scopus
  35. H. Nagasawa, H. Kameda, K. Amano, and T. Takeuchi, “Clinical significance of elevated serum levels of matrix metalloproteinase-3 and C-reactive protein in patients with rheumatoid arthritis,” APLAR Journal of Rheumatology, vol. 10, no. 4, pp. 295–299, 2007. View at Publisher · View at Google Scholar · View at Scopus
  36. S. Visvanathan, J. C. Marini, J. S. Smolen et al., “Changes in biomarkers of inflammation and bone turnover and associations with clinical efficacy following infliximab plus methotrexate therapy in patients with early rheumatoid arthritis,” Journal of Rheumatology, vol. 34, no. 7, pp. 1465–1474, 2007. View at Scopus
  37. K. Fujikawa, A. Kawakami, M. Tamai et al., “High serum cartilage oligomeric matrix protein determines the subset of patients with early-stage rheumatoid arthritis with high serum C-reactive protein, matrix metalloproteinase-3, and MRI-proven bone erosion,” Journal of Rheumatology, vol. 36, no. 6, pp. 1126–1129, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. G. Morozzi, M. Fabbroni, F. Bellisai, S. Cucini, A. Simpatico, and M. Galeazzi, “Low serum level of COMP, a cartilage turnover marker, predicts rapid and high ACR70 response to adalimumab therapy in rheumatoid arthritis,” Clinical Rheumatology, vol. 26, no. 8, pp. 1335–1338, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. G. Morozzi, M. Fabbroni, F. Bellisai, G. Pucci, and M. Galeazzi, “Cartilage oligomeric matrix protein level in rheumatic diseases: potential use as a marker for measuring articular cartilage damage and/or the therapeutic efficacy of treatments,” Annals of the New York Academy of Sciences, vol. 1108, pp. 398–407, 2007. View at Publisher · View at Google Scholar · View at Scopus
  40. K. L. Posey and J. T. Hecht, “The role of cartilage oligomeric matrix protein (COMP) in skeletal disease,” Current Drug Targets, vol. 9, no. 10, pp. 869–877, 2008. View at Scopus