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Mediators of Inflammation
Volume 2014, Article ID 215140, 7 pages
http://dx.doi.org/10.1155/2014/215140
Research Article

YKL-40 as a Novel Factor Associated with Inflammation and Catabolic Mechanisms in Osteoarthritic Joints

1The Immunopharmacology Research Group, University of Tampere School of Medicine and Tampere University Hospital, 33014 Tampere, Finland
2Coxa Hospital for Joint Replacement, P.O. Box 652, 33101 Tampere, Finland

Received 19 June 2014; Accepted 4 July 2014; Published 15 July 2014

Academic Editor: Luca Cantarini

Copyright © 2014 Tuija Väänänen 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. C. G. Lee, C. A. Da Silva, C. S. Dela Cruz et al., “Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury,” Annual Review of Physiology, vol. 73, pp. 479–501, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. B. Volck, J. S. Johansen, M. Stoltenberg et al., “Studies on YKL-40 in knee joints of patients with rheumatoid arthritis and osteoarthritis. Involvement of YKL-40 in the joint pathology,” Osteoarthritis & Cartilage, vol. 9, no. 3, pp. 203–214, 2001. View at Publisher · View at Google Scholar · View at Scopus
  3. H. Ling and A. D. Recklies, “The chitinase 3-like protein human cartilage glycoprotein 39 inhibits cellular responses to the inflammatory cytokines interleukin-1 and tumour necrosis factor-α,” Biochemical Journal, vol. 380, no. 3, pp. 651–659, 2004. View at Publisher · View at Google Scholar · View at Scopus
  4. J. S. Johansen, M. K. Williamson, J. S. Rice, and P. A. Price, “Identification of proteins secreted by human osteoblastic cells in culture,” Journal of Bone and Mineral Research, vol. 7, no. 5, pp. 501–512, 1992. View at Google Scholar · View at Scopus
  5. B. E. Hakala, C. White, and A. D. Recklies, “Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family,” Journal of Biological Chemistry, vol. 268, no. 34, pp. 25803–25810, 1993. View at Google Scholar · View at Scopus
  6. M. Kawasaki, Y. Hasegawa, S. Kondo, and H. Iwata, “Concentration and localization of YKL-40 in hip joint diseases,” Journal of Rheumatology, vol. 28, no. 2, pp. 341–345, 2001. View at Google Scholar · View at Scopus
  7. J. R. Connor, R. A. Dodds, J. G. Emery, R. B. Kirkpatrick, M. Rosenberg, and M. Gowen, “Human cartilage glycoprotein 39 (HC gp-39) mRNA expression in adult and fetal chondrocytes, osteoblasts and osteocytes by in-situ hybridization,” Osteoarthritis and Cartilage, vol. 8, no. 2, pp. 87–95, 2000. View at Publisher · View at Google Scholar · View at Scopus
  8. K. Huang and L. Wu, “YKL-40: a potential biomarker for osteoarthritis,” Journal of International Medical Research, vol. 37, no. 1, pp. 18–24, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. J. S. Johansen, H. S. Jensen, and P. A. Price, “A new biochemical marker for joint injury. Analysis of YKL 40 in serum and synovial fluid,” British Journal of Rheumatology, vol. 32, no. 11, pp. 949–955, 1993. View at Publisher · View at Google Scholar · View at Scopus
  10. T. Conrozier, M.-C. Carlier, P. Mathieu et al., “Serum levels of YKL-40 and C reactive protein in patients with hip osteoarthritis and healthy subjects: a cross sectional study,” Annals of the Rheumatic Diseases, vol. 59, no. 10, pp. 828–831, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Takahashi, K. Naito, M. Abe, T. Sawada, and A. Nagano, “Relationship between radiographic grading of osteoarthritis and the biochemical markers for arthritis in knee osteoarthritis,” Arthritis Research & Therapy, vol. 6, no. 3, pp. R208–R212, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Kapoor, J. Martel-Pelletier, D. Lajeunesse, J. Pelletier, and H. Fahmi, “Role of proinflammatory cytokines in the pathophysiology of osteoarthritis,” Nature Reviews Rheumatology, vol. 7, no. 1, pp. 33–42, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. G. Murphy and H. Nagase, “Reappraising metalloproteinases in rheumatoid arthritis and osteoarthritis: destruction or repair?” Nature Clinical Practice Rheumatology, vol. 4, no. 3, pp. 128–135, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Altman, E. Asch, and D. Bloch, “Development of criteria for the classification and reporting of osteoarthritis. Classification of osteoarthritis of the knee,” Arthritis and Rheumatism, vol. 29, no. 8, pp. 1039–1052, 1986. View at Publisher · View at Google Scholar · View at Scopus
  15. A. Koskinen, K. Vuolteenaho, R. Nieminen, T. Moilanen, and E. Moilanen, “Leptin enhances MMP-1, MMP-3 and MMP-13 production in human osteoarthritic cartilage and correlates with MMP-1 and MMP-3 in synovial fluid from oa patients,” Clinical and Experimental Rheumatology, vol. 29, no. 1, pp. 57–64, 2011. View at Google Scholar · View at Scopus
  16. A. Koskinen, S. Juslin, R. Nieminen, T. Moilanen, K. Vuolteenaho, and E. Moilanen, “Adiponectin associates with markers of cartilage degradation in osteoarthritis and induces production of proinflammatory and catabolic factors through mitogen-activated protein kinase pathways,” Arthritis Research & Therapy, vol. 13, no. 6, article R184, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. M. B. Goldring and S. R. Goldring, “Osteoarthritis,” Journal of Cellular Physiology, vol. 213, no. 3, pp. 626–634, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. R. Shao, K. Hamel, L. Petersen et al., “YKL-40, a secreted glycoprotein, promotes tumor angiogenesis,” Oncogene, vol. 28, no. 50, pp. 4456–4468, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Pap and J. Bertrand, “Syndecans in cartilage breakdown and synovial inflammation,” Nature Reviews Rheumatology, vol. 9, no. 1, pp. 43–55, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. I. Rego-Pérez, M. Fernández-Moreno, M. Deberg et al., “Mitochondrial DNA haplogroups modulate the serum levels of biomarkers in patients with osteoarthritis,” Annals of the Rheumatic Diseases, vol. 69, no. 5, pp. 910–917, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. B. Volck, K. Østergaard, J. S. Johansen, C. Garbarsch, and P. A. Price, “The distribution of YKL-40 in osteoarthritic and normal human articular cartilage,” Scandinavian Journal of Rheumatology, vol. 28, no. 3, pp. 171–179, 1999. View at Publisher · View at Google Scholar · View at Scopus
  22. J. S. Johansen, T. Olee, P. A. Price, S. Hashimoto, R. L. Ochs, and M. Lotz, “Regulation of YKL-40 production by human articular chondrocytes,” Arthritis & Rheumatism, vol. 44, no. 4, pp. 826–837, 2001. View at Google Scholar
  23. G. H. Renkema, R. G. Boot, F. L. Au et al., “Chitotriosidase a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages,” European Journal of Biochemistry, vol. 251, no. 1-2, pp. 504–509, 1998. View at Publisher · View at Google Scholar · View at Scopus
  24. F. Fusetti, T. Pijning, K. H. Kalk, E. Bos, and B. W. Dijkstra, “Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37753–37760, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. H. F. Bigg, R. Wait, A. D. Rowan, and T. E. Cawston, “The mammalian chitinase-like lectin, YKL-40, binds specifically to type I collagen and modulates the rate of type I collagen fibril formation,” The Journal of Biological Chemistry, vol. 281, no. 30, pp. 21082–21095, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. P. Garnero, M. Piperno, E. Gineyts, S. Christgau, P. D. Delmas, and E. Vignon, “Cross sectional evaluation of biochemical markers of bone, cartilage, and synovial tissue metabolism in patients with knee osteoarthritis: relations with disease activity and joint damage,” Annals of the Rheumatic Diseases, vol. 60, no. 6, pp. 619–626, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. T. Knorr, F. Obermayr, E. Bartnik, A. Zien, and T. Aigner, “YKL-39 (chitinase 3-like protein 2), but not YKL-40 (chitinase 3-like protein 1), is up regulated in osteoarthritic chondrocytes,” Annals of the Rheumatic Diseases, vol. 62, no. 10, pp. 995–998, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. E. Steck, S. Breit, S. J. Breusch, M. Axt, and W. Richter, “Enhanced expression of the human chitinase 3-like 2 gene (YKL-39) but not chitinase 3-like 1 gene (YKL-40) in osteoarthritic cartilage,” Biochemical and Biophysical Research Communications, vol. 299, no. 1, pp. 109–115, 2002. View at Publisher · View at Google Scholar · View at Scopus