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Advances in Orthopedics
Volume 2012 (2012), Article ID 834208, 7 pages
http://dx.doi.org/10.1155/2012/834208
Review Article

Recent Findings on the Role of Gelatinases (Matrix Metalloproteinase-2 and -9) in Osteoarthritis

Department of Orthopaedic and Trauma Surgery, School of Medicine, University Magna Græcia of Catanzaro, Europa Avenue, 88100 Catanzaro, Italy

Received 18 December 2011; Accepted 27 May 2012

Academic Editor: Zoe Dailiana

Copyright © 2012 Olimpio Galasso 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. S. Tanaka, C. Hamanishi, H. Kikuchi, and K. Fukuda, “Factors related to degradation of articular cartilage in osteoarthritis: a review,” Seminars in Arthritis and Rheumatism, vol. 27, no. 6, pp. 392–399, 1998. View at Publisher · View at Google Scholar · View at Scopus
  2. S. D. Shapiro, “Diverse roles of macrophage matrix metalloproteinases in tissue destruction and tumor growth,” Thrombosis and Haemostasis, vol. 82, no. 2, pp. 846–849, 1999. View at Google Scholar · View at Scopus
  3. C. B. Jones, D. C. Sane, and D. M. Herrington, “Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome,” Cardiovascular Research, vol. 59, no. 4, pp. 812–823, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. E. E. Creemers, J. P. Cleutjens, J. F. Smits, and M. J. Daemen, “Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure?” Circulation Research, vol. 89, no. 3, pp. 201–210, 2001. View at Google Scholar · View at Scopus
  5. T. J. Gronski Jr., R. L. Martin, D. K. Kobayashi et al., “Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase,” The Journal of Biological Chemistry, vol. 272, no. 18, pp. 12189–12194, 1997. View at Publisher · View at Google Scholar · View at Scopus
  6. A. I. Sapolsky and D. S. Howell, “Further characterization of a neutral metalloprotease isolated from human articular cartilage,” Arthritis and Rheumatism, vol. 25, no. 8, pp. 981–988, 1982. View at Google Scholar · View at Scopus
  7. W. A. Galloway, G. Murphy, J. D. Sandy, J. Gavrilovic, T. E. Cawtson, and J. J. Reynolds, “Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective-tissue components,” The Biochemical Journal, vol. 209, no. 3, pp. 741–752, 1983. View at Google Scholar · View at Scopus
  8. Z. Gunja-Smith, H. Nagase, and J. F. Woessner, “Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3,” The Biochemical Journal, vol. 258, no. 1, pp. 115–119, 1989. View at Google Scholar · View at Scopus
  9. A. J. Fosang, P. J. Neame, T. E. Hardingham, G. Murphy, and J. A. Hamilton, “Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins,” The Journal of Biological Chemistry, vol. 266, no. 24, pp. 15579–15582, 1991. View at Google Scholar · View at Scopus
  10. A. J. Fosang, P. J. Neame, K. Last, T. E. Hardingham, G. Murphy, and J. A. Hamilton, “The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B,” The Journal of Biological Chemistry, vol. 267, no. 27, pp. 19470–19474, 1992. View at Google Scholar · View at Scopus
  11. A. J. Fosang, K. Last, V. Knauper et al., “Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain,” The Biochemical Journal, vol. 295, no. 1, pp. 273–276, 1993. View at Google Scholar · View at Scopus
  12. A. J. Fosang, K. Last, V. Knäuper, G. Murphy, and P. J. Neame, “Degradation of cartilage aggrecan by collagenase-3 (MMP-13),” FEBS Letters, vol. 380, no. 1-2, pp. 17–20, 1996. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Chakrabarti and K. D. Patel, “Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology,” Experimental Lung Research, vol. 31, no. 6, pp. 599–621, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. A. D. Kandasamy, A. K. Chow, M. A. Ali, and R. Schulz, “Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix,” Cardiovascular Research, vol. 85, no. 3, pp. 413–423, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. T. Turpeenniemi-Hujanen, “Gelatinases (MMP-2 and -9) and their natural inhibitors as prognostic indicators in solid cancers,” Biochimie, vol. 87, no. 3-4, pp. 287–297, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Y. Gasparyan, L. Ayvazyan, H. Blackmore, and G. D. Kitas, “Writing a narrative biomedical review: considerations for authors, peer reviewers, and editors,” Rheumatology International, vol. 31, no. 11, pp. 1409–1417, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. L. A. Liotta, S. Abe, P. G. Robey, and G. R. Martin, “Preferential digestion of basement membrane collagen by an enzyme derived from a metastatic murine tumor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no. 5, pp. 2268–2272, 1979. View at Google Scholar · View at Scopus
  18. T. Salo, L. A. Liotta, and K. Tryggvason, “Purification and characterization of a murine basement membrane collagen-degrading enzyme secreted by metastatic tumor cells,” The Journal of Biological Chemistry, vol. 258, no. 5, pp. 3058–3063, 1983. View at Google Scholar · View at Scopus
  19. M. Hoyhtya, E. Hujanen, T. Turpeenniemi-Hujanen, U. Thorgeirsson, L. A. Liotta, and K. Tryggvason, “Modulation of type-IV collagenase activity and invasive behavior of metastatic human melanoma (A2058) cells in vitro by monoclonal antibodies to type-IV collagenase,” International Journal of Cancer, vol. 46, no. 2, pp. 282–286, 1990. View at Publisher · View at Google Scholar · View at Scopus
  20. T. Vartio, T. Hovi, and A. Vaheri, “Human macrophages synthesize and secrete a major 95,000-dalton gelatin-binding protein distinct from fibronectin,” The Journal of Biological Chemistry, vol. 257, no. 15, pp. 8862–8866, 1982. View at Google Scholar · View at Scopus
  21. T. Salo and J. Oikarinen, “Regulation of type IV collagen degrading enzyme by cortisol during human skin fibroblast growth,” Biochemical and Biophysical Research Communications, vol. 130, no. 2, pp. 588–595, 1985. View at Google Scholar · View at Scopus
  22. D. S. Hipps, R. M. Hembry, A. J. Docherty, J. J. Reynolds, and G. Murphy, “Purification and characterization of human 72-kDa gelatinase (type IV collagenase). Use of immunolocalisation to demonstrate the non-coordinate regulation of the 72-kDa and 95-kDa gelatinases by human fibroblasts.,” Biological Chemistry Hoppe-Seyler, vol. 372, no. 4, pp. 287–296, 1991. View at Google Scholar · View at Scopus
  23. A. Y. Strongin, I. Collier, G. Bannikov, B. L. Marmer, G. Grant, and G. Goldberg, “Mechanism of cell surface activation of 72-kDa type IV collagenase,” The Journal of Biological Chemistry, vol. 270, no. 10, pp. 5331–5338, 1995. View at Publisher · View at Google Scholar · View at Scopus
  24. R. Visse and H. Nagase, “Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry,” Circulation Research, vol. 92, no. 8, pp. 827–839, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. H. Sato and T. Takino, “Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion,” Cancer Science, vol. 101, no. 4, pp. 843–847, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. N. Ramos-De Simone, E. Hahn-Dantona, J. Sipley, H. Nagase, D. L. French, and J. P. Quigley, “Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion,” The Journal of Biological Chemistry, vol. 274, no. 19, pp. 13066–13076, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. J. F. Woessner Jr., “Matrix metalloproteinases,” The Journal of Biological Chemistry, vol. 274, no. 31, pp. 21491–21494, 1999. View at Publisher · View at Google Scholar · View at Scopus
  28. M. D. Sternlicht and Z. Werb, “How matrix metalloproteinases regulate cell behavior,” Annual Review of Cell and Developmental Biology, vol. 17, pp. 463–516, 2001. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Duerr, S. Stremme, S. Soeder, B. Bau, and T. Aigner, “MMP-2/gelatinase A is a gene product of human adult articular chondrocytes and is increased in osteoarthritic cartilage,” Clinical and Experimental Rheumatology, vol. 22, no. 5, pp. 603–608, 2004. View at Google Scholar · View at Scopus
  30. D. B. Logar, R. Komadina, J. Preželj, B. Ostanek, Z. Trošt, and J. Marc, “Expression of bone resorption genes in osteoarthritis and in osteoporosis,” Journal of Bone and Mineral Metabolism, vol. 25, no. 4, pp. 219–225, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. M. E. Fini, J. R. Cook, R. Mohan, and C. E. Brinckerhoff, “Regulation of matrix metalloproteinase gene expression,” in Matrix Metalloproteinases, W. C. Park and R. P. Mecham, Eds., pp. 299–356, New York Academic, 1998. View at Google Scholar
  32. H. Nagase, R. Visse, and G. Murphy, “Structure and function of matrix metalloproteinases and TIMPs,” Cardiovascular Research, vol. 69, no. 3, pp. 562–573, 2006. View at Publisher · View at Google Scholar · View at Scopus
  33. R. Mazzieri, L. Masiero, L. Zanetta et al., “Control of type IV collagenase activity by the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants,” The EMBO Journal, vol. 16, no. 9, pp. 2319–2332, 1997. View at Publisher · View at Google Scholar · View at Scopus
  34. Q. X. Sang, “Complex role of matrix metalloproteinases in angiogenesis,” Cell Research, vol. 8, no. 3, pp. 171–177, 1998. View at Google Scholar · View at Scopus
  35. S. Söder, H. I. Roach, S. Oehler, B. Bau, J. Haag, and T. Aigner, “MMP-9/gelatinase B is a gene product of human adult articular chondrocytes and increased in osteoarthritic cartilage,” Clinical and Experimental Rheumatology, vol. 24, no. 3, pp. 302–304, 2006. View at Google Scholar · View at Scopus
  36. M. Mohtai, R. L. Smith, D. J. Schurman et al., “Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1,” The Journal of Clinical Investigation, vol. 92, no. 1, pp. 179–185, 1993. View at Google Scholar · View at Scopus
  37. T. Kinoshita, H. Sato, A. Okada et al., “TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads,” The Journal of Biological Chemistry, vol. 273, no. 26, pp. 16098–16103, 1998. View at Publisher · View at Google Scholar · View at Scopus
  38. G. W. Wang, M. Q. Wang, X. Y. Wang, S. B. Yu, X. D. Liu, and K. Jiao, “Changes in the expression of MMP-3, MMP-9, TIMP-1 and aggrecan in the condylar cartilage of rats induced by experimentally created disordered occlusion,” Archives of Oral Biology, vol. 55, no. 11, pp. 887–895, 2010. View at Publisher · View at Google Scholar · View at Scopus
  39. H. Hulejová, V. Barešová, Z. Klézl, M. Polanská, M. Adam, and L. Šenolt, “Increased level of cytokines and matrix metalloproteinases in osteoarthritic subchondral bone,” Cytokine, vol. 38, no. 3, pp. 151–156, 2007. View at Publisher · View at Google Scholar · View at Scopus
  40. R. T. Aimes and J. P. Quigley, “Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments,” The Journal of Biological Chemistry, vol. 270, no. 11, pp. 5872–5876, 1995. View at Publisher · View at Google Scholar · View at Scopus
  41. P. A. Hill, A. J. Docherty, K. M. Bottomley et al., “Inhibition of bane resorption in vitro by selective inhibitors of gelatinase and collagenase,” The Biochemical Journal, vol. 308, no. 1, pp. 167–175, 1995. View at Google Scholar · View at Scopus
  42. J. P. Mansell and A. J. Bailey, “Abnormal cancellous bone collagen metabolism in osteoarthritis,” The Journal of Clinical Investigation, vol. 101, no. 8, pp. 1596–1603, 1998. View at Google Scholar · View at Scopus
  43. M. J. Seibel, A. Duncan, and S. P. Robins, “Urinary hydroxy-pyridinium crosslinks provide indices of cartilage and bone involvement in arthritic diseases,” The Journal of Rheumatology, vol. 16, no. 7, pp. 964–970, 1989. View at Google Scholar · View at Scopus
  44. K. Masuhara, T. Nakai, K. Yamaguchi, S. Yamasaki, and Y. Sasaguri, “Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip,” Arthritis & Rheumatism, vol. 46, no. 10, pp. 2625–2631, 2002. View at Publisher · View at Google Scholar · View at Scopus
  45. D. R. Mitrovic and H. Riera, “Synovial, articular cartilage and bone changes in rapidly destructive arthropathy (osteoarthritis) of the hip,” Rheumatology International, vol. 12, no. 1, pp. 17–22, 1992. View at Google Scholar · View at Scopus
  46. N. Buisson-Legendre, S. Smith, L. March, and C. Jackson, “Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2,” Arthritis & Rheumatism, vol. 50, no. 7, pp. 2151–2156, 2004. View at Publisher · View at Google Scholar · View at Scopus
  47. K. Masuhara, S. B. Lee, T. Nakai, N. Sugano, T. Ochi, and Y. Sasaguri, “Matrix metalloproteinases in patients with osteoarthritis of the hip,” International Orthopaedics, vol. 24, no. 2, pp. 92–96, 2000. View at Google Scholar · View at Scopus
  48. K. Naito, M. Takahashi, K. Kushida et al., “Measurement of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases-1 (TIMP-1) in patients with knee osteoarthritis: comparison with generalized osteoarthritis,” Rheumatology, vol. 38, no. 6, pp. 510–515, 1999. View at Publisher · View at Google Scholar · View at Scopus
  49. M. Bellido, L. Lugo, J. A. Roman-Blas et al., “Subchondral bone microstructural damage by increased remodelling aggravates experimental osteoarthritis preceded by osteoporosis,” Arthritis Research and Therapy, vol. 12, no. 4, article R152, 2010. View at Publisher · View at Google Scholar · View at Scopus
  50. H. Duncan, J. Jundt, J. M. Riddle, W. Pitchford, and T. Christopherson, “The tibial subchondral plate. A scanning electron microscopic study,” Journal of Bone and Joint Surgery A, vol. 69, no. 8, pp. 1212–1220, 1987. View at Google Scholar · View at Scopus
  51. A. Shibakawa, K. Yudoh, K. Masuko-Hongo, T. Kato, K. Nishioka, and H. Nakamura, “The role of subchondral bone resorption pits in osteoarthritis: MMP production by cells derived from bone marrow,” Osteoarthritis and Cartilage, vol. 13, no. 8, pp. 679–687, 2005. View at Publisher · View at Google Scholar · View at Scopus
  52. M. E. Duclos, O. Roualdes, R. Cararo, J. C. Rousseau, T. Roger, and D. J. Hartmann, “Significance of the serum CTX-II level in an osteoarthritis animal model: a 5-month longitudinal study,” Osteoarthritis and Cartilage, vol. 18, no. 11, pp. 1467–1476, 2010. View at Publisher · View at Google Scholar · View at Scopus
  53. F. Sharif, J. Kirwan, N. Charni, L. J. Sandell, C. Whittles, and P. Garnero, “A 5-yr longitudinal study of type IIA collagen synthesis and total type II collagen degradation in patients with knee osteoarthritis—association with disease progression,” Rheumatology, vol. 46, no. 6, pp. 938–943, 2007. View at Publisher · View at Google Scholar · View at Scopus
  54. M. Jung, S. Christgau, M. Lukoschek, D. Henriksen, and W. Richter, “Increased urinary concentration of collagen type II C-telopeptide fragments in patients with osteoarthritis,” Pathobiology, vol. 71, no. 2, pp. 70–76, 2004. View at Publisher · View at Google Scholar · View at Scopus
  55. M. F. Sowers, C. A. Karvonen-Gutierrez, M. Yosef et al., “Longitudinal changes of serum COMP and urinary CTX-II predict X-ray defined knee osteoarthritis severity and stiffness in women,” Osteoarthritis and Cartilage, vol. 17, no. 12, pp. 1609–1614, 2009. View at Publisher · View at Google Scholar · View at Scopus
  56. I. Byrjalsen, M. A. Karsdal, P. Qvist, and C. Christiansen, “Increased urinary excretion of C-telopeptides of type II collagen (CTX-II) predicts cartilage loss over 21 months by MRI,” Osteoarthritis and Cartilage, vol. 17, no. 3, pp. 384–389, 2009. View at Publisher · View at Google Scholar · View at Scopus
  57. E. B. Dam, M. Loog, C. Christiansen et al., “Identification of progressors in osteoarthritis by combining biochemical and MRI-based markers,” Arthritis Research and Therapy, vol. 11, no. 4, article R115, 2009. View at Publisher · View at Google Scholar · View at Scopus
  58. K. S. Kim, Y. A. Lee, H. M. Choi, M. C. Yoo, and H. I. Yang, “Implication of MMP-9 and urokinase plasminogen activator (uPA) in the activation of pro-matrix metalloproteinase (MMP)-13,” Rheumatology International. In press.
  59. K. S. Kim, H. M. Choi, Y. A. Lee et al., “Expression levels and association of gelatinases MMP-2 and MMP-9 and collagenases MMP-1 and MMP-13 with VEGF in synovial fluid of patients with arthritis,” Rheumatology International, vol. 31, no. 4, pp. 543–547, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. A. Fraser, U. Fearon, R. Reece, P. Emery, and D. J. Veale, “Matrix metalloproteinase 9, apoptosis, and vascular morphology in early arthritis,” Arthritis and Rheumatism, vol. 44, no. 9, pp. 2024–2028, 2001. View at Google Scholar
  61. H. Li, S. B. Miao, L. H. Dong et al., “Clinicopathological correlation of Krüppel-like factor 5 and matrix metalloproteinase-9 expression and cartilage degeneration in human osteoarthritis,” Pathology, Research and Practice, vol. 208, no. 1, pp. 9–14, 2012. View at Google Scholar
  62. C. Sanchez, L. Pesesse, O. Gabay et al., “Regulation of subchondral bone osteoblast metabolism by cyclic compression,” Arthritis Rheumatism, vol. 64, no. 4, pp. 1193–1203, 2012. View at Google Scholar
  63. J. Guo, W. Zhang, Q. Li, H. Gan, and Z. Wang, “Significance of expressions of matrix metalloproteinase 9 mRNA, transforming growth factor beta1, mRNA and corresponding proteins in osteoarthritis,” Chinese Journal of Reparative and Reconstructive Surgery, vol. 25, no. 8, pp. 992–997, 2011. View at Google Scholar
  64. F. De Ceuninck, M. Sabatini, and P. Pastoureau, “Recent progress toward biomarker identification in osteoarthritis,” Drug Discovery Today, vol. 16, no. 9-10, pp. 443–449, 2011. View at Publisher · View at Google Scholar · View at Scopus