Best Practice & Research Clinical Rheumatology
Volume 22, Issue 2 , Pages 351-384 , April 2008

Cartilage in normal and osteoarthritis conditions

  • Johanne Martel-Pelletier, PhD (Professor)

      Affiliations

    • Corresponding Author InformationCorresponding author. Osteoarthritis Research Unit, University of Montreal Hospital Centre, Notre-Dame Hospital, 1560 Sherbrooke Street East, Montreal, Quebec H2L 4M1, Canada. Tel.: +1 514 890 8000x26658; Fax: +1 514 412 7582.
    • ,
  • Christelle Boileau, PhD (Doctor)
    • ,
  • Jean-Pierre Pelletier, MD (Professor)

References 

  1. Venn MF. Chemical composition of human femoral and head cartilage: influence of topographical position and fibrillation. Annals of the Rheumatic Diseases. 1979;38:57–62
  2. Stockwell RA. Morphology of cartilage. In:  Maroudas A,  Keuttner K editor. Methods in cartilage research. San Diego: Academic Press; 1990;p. 61–63
  3. Jones GC, Riley GP. ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Research & Therapy. 2005;7:160–169
  4. Prockop DJ, Sieron AL, Li SW. Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling. Matrix Biology. 1998;16:399–408
  5. Takahashi M, Kushida K, Ohishi T, et al. Quantitative analysis of crosslinks pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders. Arthritis and Rheumatism. 1994;37:724–728
  6. Verzijl N, DeGroot J, Thorpe SR, et al. Effect of collagen turnover on the accumulation of advanced glycation end products. The Journal of Biological Chemistry. 2000;275:39027–39031
  7. Reboul P, Pelletier JP, Tardif G, et al. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes: A role in osteoarthritis. The Journal of Clinical Investigation. 1996;97:2011–2019
  8. Byers PH. Folding defects in fibrillar collagens. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 2001;356:151–157
  9. Ahmad NN, Ala-Kokko L, Knowlton RG, et al. Stop codon in the procollagen II gene (COL2A1) in a family with the Stickler syndrome (arthro-ophthalmopathy). Proceedings of the National Academy of Sciences of the United States of America. 1991;88:6624–6627
  10. Pun YL, Moskowitz RW, Lie S, et al. Clinical correlations of osteoarthritis associated with a single-base mutation (arginine519 to cysteine) in type II procollagen gene. A newly defined pathogenesis. Arthritis and Rheumatism. 1994;37:264–269
  11. Eyre DR, Weis MA, Wu JJ. Articular cartilage collagen: an irreplaceable framework?. European Cells & Materials. 2006;12:57–63
  12. Eyre DR. Collagens and cartilage matrix homeostasis. Clinical Orthopaedics and Related Research. 2004;(427 Suppl):S118–S122
  13. Wu JJ, Woods PE, Eyre DR. Identification of cross-linking sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX bonding. The Journal of Biological Chemistry. 1992;267:23007–23014
  14. Muragaki Y, Kimura T, Ninomiya Y, Olsen BR. The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains. European Journal of Biochemistry. 1990;192:703–708
  15. Ala-Kokko L. Genetic risk factors for lumbar disc disease. Annals of Medicine. 2002;34:42–47
  16. Soder S, Hambach L, Lissner R, et al. Ultrastructural localization of type VI collagen in normal adult and osteoarthritic human articular cartilage. Osteoarthritis and Cartilage. 2002;10:464–470
  17. Pullig O, Weseloh G, Swoboda B. Expression of type VI collagen in normal and osteoarthritic human cartilage. Osteoarthritis and Cartilage. 1999;7:191–202
  18. Boos N, Nerlich AG, Wiest I, et al. Immunohistochemical analysis of type-X-collagen expression in osteoarthritis of the hip joint. Journal of Orthopaedic Research. 1999;17:495–502
  19. Bateman JF. The molecular genetics of inherited cartilage disease. Osteoarthritis and Cartilage. 2001;9(Suppl. A):S141–S149
  20. Bateman J. Genetic aspects of osteoarthritis. Seminars in Arthritis and Rheumatism. 2005;34:15–18
  21. Chen L, Wu Y, Lee V, et al. The folded modules of aggrecan G3 domain exert two separable functions in glycosaminoglycan modification and product secretion. The Journal of Biological Chemistry. 2002;277:2657–2665
  22. Roughley PJ, White RJ. Age-related changes in the structure of the proteoglycan subunits from human articular cartilage. The Journal of Biological Chemistry. 1980;255:217–224
  23. Dudhia J, Davidson CM, Wells TM, et al. Studies on the G3 domain of aggrecan from human cartilage. Annals of the New York Academy of Sciences. 1996;785:245–247
  24. Roughley PJ, Mort JS. Ageing and the aggregating proteoglycans of human articular cartilage. Clinical Science (London, England). 1986;71:337–344
  25. Tortorella MD, Pratta M, Liu RQ, et al. Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4). The Journal of Biological Chemistry. 2000;275:18566–18573
  26. Roughley P, Martens D, Rantakokko J, et al. The involvement of aggrecan polymorphism in degeneration of human intervertebral disc and articular cartilage. European Cells & Materials. 2006;11:1–7
  27. Nguyen Q, Murphy G, Hughes CE, et al. Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. The Biochemical Journal. 1993;295:595–598
  28. Mort JS, Poole AR, Roughley PJ. Age-related changes in the structure of proteoglycan link proteins present in normal human articular cartilage. The Biochemical Journal. 1983;214:269–272
  29. Melching LI, Roughley PJ. Studies on the interaction of newly secreted proteoglycan subunits with hyaluronate in human articular cartilage. Biochimica et Biophysica Acta. 1990;1035:20–28
  30. Rodriguez E, Roughley P. Link protein can retard the degradation of hyaluronan in proteoglycan aggregates. Osteoarthritis and Cartilage. 2006;14:823–829
  31. Holmes MW, Bayliss MT, Muir H. Hyaluronic acid in human articular cartilage. Age-related changes in content and size. The Biochemical Journal. 1988;250:435–441
  32. Imai K, Hiramatsu A, Fukushima D, et al. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. The Biochemical Journal. 1997;322:809–814
  33. Monfort J, Tardif G, Reboul P, et al. Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13: identification of a new biglycan cleavage site. Arthritis Research & Therapy. 2006;8:R26
  34. Heathfield TF, Onnerfjord P, Dahlberg L, Heinegard D. Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13. The Journal of Biological Chemistry. 2004;279:6286–6295
  35. Geng Y, McQuillan D, Roughley PJ. SLRP interaction can protect collagen fibrils from cleavage by collagenases. Matrix Biology. 2006;25:484–491
  36. Scott PG, McEwan PA, Dodd CM, et al. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proceedings of the National Academy of Sciences of the United States of America. 2004;101:15633–15638
  37. Sztrolovics R, Grover J, Cs-Szabo G, et al. The characterization of versican and its message in human articular cartilage and intervertebral disc. Journal of Orthopaedic Research. 2002;20:257–266
  38. Bengtsson E, Morgelin M, Sasaki T, et al. The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor. The Journal of Biological Chemistry. 2002;277:15061–15068
  39. Chang Z, Meyer K, Rapraeger AC, Friedl A. Differential ability of heparan sulfate proteoglycans to assemble the fibroblast growth factor receptor complex in situ. The FASEB Journal. 2000;14:137–144
  40. Arikawa-Hirasawa E, Watanabe H, Takami H, et al. Perlecan is essential for cartilage and cephalic development. Nature Genetics. 1999;23:354–358
  41. Arikawa-Hirasawa E, Wilcox WR, Le AH, et al. Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene. Nature Genetics. 2001;27:431–434
  42. Arikawa-Hirasawa E, Le AH, Nishino I, et al. Structural and functional mutations of the perlecan gene cause Schwartz-Jampel syndrome, with myotonic myopathy and chondrodysplasia. American Journal of Human Genetics. 2002;70:1368–1375
  43. Cs-Szabo G, Roughley PJ, Plaas AH, Glant TT. Large and small proteoglycans of osteoarthritic and rheumatoid articular cartilage. Arthritis and Rheumatism. 1995;38:660–668
  44. Malemud CJ, Papay RS, Hering TM, et al. Phenotypic modulation of newly synthesized proteoglycans in human cartilage and chondrocytes. Osteoarthritis and Cartilage. 1995;3:227–238
  45. Struglics A, Larsson S, Pratta MA, et al. Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments. Osteoarthritis and Cartilage. 2006;14:101–113
  46. Chambers MG, Cox L, Chong L, et al. Matrix metalloproteinases and aggrecanases cleave aggrecan in different zones of normal cartilage but colocalize in the development of osteoarthritic lesions in STR/ort mice. Arthritis and Rheumatism. 2001;44:1455–1465
  47. Moldovan F, Pelletier JP, Hambor J, et al. Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: in vitro mimicking effect by transforming growth factor beta. Arthritis and Rheumatism. 1997;40:1653–1661
  48. Fernandes JC, Martel-Pelletier J, Lascau-Coman V, et al. Collagenase-1 and collagenase-3 synthesis in early experimental osteoarthritic canine cartilage. An immunohistochemical study. The Journal of Rheumatology. 1998;25:1585–1594
  49. Lohmander LS, Ionescu M, Jugessur H, Poole AR. Changes in joint cartilage aggrecan after knee injury and in osteoarthritis. Arthritis and Rheumatism. 1999;42:534–544
  50. Poole AR, Rosenberg LC, Reiner A, et al. Contents and distributions of the proteoglycans decorin and biglycan in normal and osteoarthritic human articular cartilage. Journal of Orthopaedic Research. 1996;14:681–689
  51. Witsch-Prehm P, Miehlke R, Kresse H. Presence of small proteoglycan fragments in normal and arthritic human cartilage. Arthritis and Rheumatism. 1992;35:1042–1052
  52. Tesche F, Miosge N. Perlecan in late stages of osteoarthritis of the human knee joint. Osteoarthritis and Cartilage. 2004;12:852–862
  53. Chen AC, Temple MM, Ng DM, et al. Induction of advanced glycation end products and alterations of the tensile properties of articular cartilage. Arthritis and Rheumatism. 2002;46:3212–3217
  54. DeGroot J, Verzijl N, Wenting-Van Wijk MJ, et al. Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products. Arthritis and Rheumatism. 2001;44:2562–2571
  55. Verzijl N, DeGroot J, Ben ZC, et al. Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis. Arthritis and Rheumatism. 2002;46:114–123
  56. Lum ZP, Hakala BE, Mort JS, Recklies AD. Modulation of the catabolic effects of interleukin-1 beta on human articular chondrocytes by transforming growth factor-beta. Journal of Cellular Physiology. 1996;166:351–359
  57. Takahashi N, Rieneck K, van der Kraan PM, et al. Elucidation of IL-1/TGF-beta interactions in mouse chondrocyte cell line by genome-wide gene expression. Osteoarthritis and Cartilage. 2005;13:426–438
  58. Scharstuhl A, van Beuningen HM, Vitters EL, et al. Loss of transforming growth factor counteraction on interleukin 1 mediated effects in cartilage of old mice. Annals of the Rheumatic Diseases. 2002;61:1095–1098
  59. Moulharat N, Lesur C, Thomas M, et al. Effects of transforming growth factor-beta on aggrecanase production and proteoglycan degradation by human chondrocytes in vitro. Osteoarthritis and Cartilage. 2004;12:296–305
  60. Fukui N, Zhu Y, Maloney WJ, et al. Stimulation of BMP-2 expression by pro-inflammatory cytokines IL-1 and TNF-alpha in normal and osteoarthritic chondrocytes. The Journal of Bone and Joint Surgery. American Volume. 2003;85-A(Suppl. 3):59–66
  61. Nakase T, Miyaji T, Tomita T, et al. Localization of bone morphogenetic protein-2 in human osteoarthritic cartilage and osteophyte. Osteoarthritis and Cartilage. 2003;11:278–284
  62. Chubinskaya S, Merrihew C, Cs-Szabo G, et al. Human articular chondrocytes express osteogenic protein-1. The Journal of Histochemistry and Cytochemistry. 2000;48:239–250
  63. Bobacz K, Gruber R, Soleiman A, et al. Cartilage-derived morphogenetic protein-1 and -2 are endogenously expressed in healthy and osteoarthritic human articular chondrocytes and stimulate matrix synthesis. Osteoarthritis and Cartilage. 2002;10:394–401
  64. Fan Z, Chubinskaya S, Rueger DC, et al. Regulation of anabolic and catabolic gene expression in normal and osteoarthritic adult human articular chondrocytes by osteogenic protein-1. Clinical and Experimental Rheumatology. 2004;22:103–106
  65. Bobacz K, Gruber R, Soleiman A, et al. Expression of bone morphogenetic protein 6 in healthy and osteoarthritic human articular chondrocytes and stimulation of matrix synthesis in vitro. Arthritis and Rheumatism. 2003;48:2501–2508
  66. Glansbeek HL, van Beuningen HM, Vitters EL, et al. Bone morphogenetic protein 2 stimulates articular cartilage proteoglycan synthesis in vivo but does not counteract interleukin-1alpha effects on proteoglycan synthesis and content. Arthritis and Rheumatism. 1997;40:1020–1028
  67. van Beuningen HM, Glansbeek HL, van der Kraan PM, van den Berg WB. Differential effects of local application of BMP-2 or TGF-beta 1 on both articular cartilage composition and osteophyte formation. Osteoarthritis and Cartilage. 1998;6:306–317
  68. Tardif G, Hum D, Pelletier JP, et al. Differential gene expression and regulation of the bone morphogenetic protein antagonists follistatin and gremlin in normal and osteoarthritic human chondrocytes and synovial fibroblasts. Arthritis and Rheumatism. 2004;50:2521–2530
  69. Tardif G, Pelletier JP, Hum D, et al. Differential regulation of the bone morphogenic protein antagonist chordin in human normal and osteoarthritic chondrocytes. Annals of the Rheumatic Diseases. 2006;65:261–264
  70. Zoricic S, Maric I, Bobinac D, Vukicevic S. Expression of bone morphogenetic proteins and cartilage-derived morphogenetic proteins during osteophyte formation in humans. Journal of Anatomy. 2003;202(Pt3):269–277
  71. Middleton JF, Tyler JA. Upregulation of insulin-like growth factor-1 gene expression in the lesions of osteoarthritic human articular cartilage. Annals of the Rheumatic Diseases. 1992;51:440–447
  72. Mi Z, Ghivizzani SC, Lechman ER, et al. Adenovirus-mediated gene transfer of insulin-like growth factor 1 stimulates proteoglycan synthesis in rabbit joints. Arthritis and Rheumatism. 2000;43:2563–2570
  73. Madry H, Zurakowski D, Trippel SB. Overexpression of human insulin-like growth factor-I promotes new tissue formation in an ex vivo model of articular chondrocyte transplantation. Gene Therapy. 2001;8:1443–1449
  74. Loeser RF, Todd MD, Seely BL. Prolonged treatment of human osteoarthritic chondrocytes with insulin-like growth factor-I stimulates proteoglycan synthesis but not proteoglycan matrix accumulation in alginate cultures. The Journal of Rheumatology. 2003;30:1565–1570
  75. Rogachefsky RA, Dean DD, Howell DS, Altman RD. Treatment of canine osteoarthritis with sodium pentosan polysulfate and insulin-like growth factor-1. Annals of the New York Academy of Sciences. 1994;732:392–394
  76. Wang J, Elewaut D, Veys EM, Verbruggen G. Insulin-like growth factor 1-induced interleukin-1 receptor II overrides the activity of interleukin-1 and controls the homeostasis of the extracellular matrix of cartilage. Arthritis and Rheumatism. 2003;48:1281–1291
  77. Okazaki K, Jingushi S, Ikenoue T, et al. Expression of insulin-like growth factor I messenger ribonucleic acid in developing osteophytes in murine experimental osteoarthritis and in rats inoculated with growth hormone-secreting tumor. Endocrinology. 1999;140:4821–4830
  78. Doré S, Pelletier JP, Di Battista JA, et al. Human osteoarthritic chondrocytes possess an increased number of insulin-like growth factor 1 binding sites but are unresponsive to its stimulation. Possible role of IGF-1-binding proteins. Arthritis and Rheumatism. 1994;37:253–263
  79. Tardif G, Reboul P, Pelletier JP, et al. Normal expression of type 1 insulin-like growth factor receptor by human osteoarthritic chondrocytes with increased expression and synthesis of insulin-like growth factor binding proteins. Arthritis and Rheumatism. 1996;39:968–978
  80. Tavera C, Abribat T, Reboul P, et al. IGF and IGF-binding protein system in the synovial fluid of osteoarthritic and rheumatoid arthritic patients. Osteoarthritis and Cartilage. 1996;4:263–274
  81. Smeets RL, Veenbergen S, Arntz OJ, et al. A novel role for suppressor of cytokine signaling 3 in cartilage destruction via induction of chondrocyte desensitization toward insulin-like growth factor. Arthritis and Rheumatism. 2006;54:1518–1528
  82. Nakanishi T, Nishida T, Shimo T, et al. Effects of CTGF/Hcs24, a product of a hypertrophic chondrocyte-specific gene, on the proliferation and differentiation of chondrocytes in culture. Endocrinology. 2000;141:264–273
  83. Nishida T, Kubota S, Nakanishi T, et al. CTGF/Hcs24, a hypertrophic chondrocyte-specific gene product, stimulates proliferation and differentiation, but not hypertrophy of cultured articular chondrocytes. Journal of Cellular Physiology. 2002;192:55–63
  84. Inoki I, Shiomi T, Hashimoto G, et al. Connective tissue growth factor binds vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis. The FASEB Journal. 2002;16:219–221
  85. Enomoto H, Inoki I, Komiya K, et al. Vascular endothelial growth factor isoforms and their receptors are expressed in human osteoarthritic cartilage. The American Journal of Pathology. 2003;162:171–181
  86. Pufe T, Petersen W, Tillmann B, Mentlein R. The splice variants VEGF121 and VEGF189 of the angiogenic peptide vascular endothelial growth factor are expressed in osteoarthritic cartilage. Arthritis and Rheumatism. 2001;44:1082–1088
  87. Pfander D, Cramer T, Weseloh G, et al. Hepatocyte growth factor in human osteoarthritic cartilage. Osteoarthritis and Cartilage. 1999;7:548–559
  88. Guévremont M, Martel-Pelletier J, Massicotte F, et al. Human adult chondrocytes express hepatocyte growth factor (HGF) isoforms but not HGF: potential implication of osteoblasts on the presence of HGF in cartilage. Journal of Bone and Mineral Research. 2003;18:1073–1081
  89. Reboul P, Pelletier JP, Tardif G, et al. Hepatocyte growth factor induction of collagenase 3 production in human osteoarthritic cartilage: involvement of the stress-activated protein kinase/c-Jun N-terminal kinase pathway and a sensitive p38 mitogen-activated protein kinase inhibitor cascade. Arthritis and Rheumatism. 2001;44:73–84
  90. Shimoaka T, Ogasawara T, Yonamine A, et al. Regulation of osteoblast, chondrocyte, and osteoclast functions by fibroblast growth factor (FGF)-18 in comparison with FGF-2 and FGF-10. The Journal of Biological Chemistry. 2002;277:7493–7500
  91. Au A, Polotsky A, Krzyminski K, et al. Evaluation of thermoreversible polymers containing fibroblast growth factor 9 (FGF-9) for chondrocyte culture. Journal of Biomedical Materials Research. Part A. 2004;69:367–372
  92. Moore EE, Bendele AM, Thompson DL, et al. Fibroblast growth factor-18 stimulates chondrogenesis and cartilage repair in a rat model of injury-induced osteoarthritis. Osteoarthritis and Cartilage. 2005;13:623–631
  93. Hakala BE, White C, Recklies AD. Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. The Journal of Biological Chemistry. 1993;268:25803–25810
  94. Connor JR, Dodds RA, Emery JG, et al. Human cartilage glycoprotein 39 (HC gp-39) mRNA expression in adult and fetal chondrocytes, osteoblasts and osteocytes by in-situ hybridization. Osteoarthritis and Cartilage. 2000;8:87–95
  95. Recklies AD, White C, Ling H. The chitinase 3-like protein human cartilage glycoprotein 39 (HC-gp39) stimulates proliferation of human connective-tissue cells and activates both extracellular signal-regulated kinase- and protein kinase B-mediated signalling pathways. The Biochemical Journal. 2002;365:119–126
  96. De Ceuninck F, Gaufillier S, Bonnaud A, et al. YKL-40 (cartilage gp-39) induces proliferative events in cultured chondrocytes and synoviocytes and increases glycosaminoglycan synthesis in chondrocytes. Biochemical and Biophysical Research Communications. 2001;285:926–931
  97. Ling H, Recklies AD. The chitinase 3-like protein human cartilage glycoprotein 39 inhibits cellular responses to the inflammatory cytokines interleukin-1 and tumour necrosis factor-alpha. The Biochemical Journal. 2004;380:651–659
  98. Jacques C, Recklies AD, Levy A, Berenbaum F. HC-gp39 contributes to chondrocyte differentiation by inducing SOX9 and type II collagen expressions. Osteoarthritis and Cartilage. 2007;15:138–146
  99. Guévremont M, Martel-Pelletier J, Boileau C, et al. Galectin-3 surface expression on human adult chondrocytes: a potential substrate for collagenase-3. Annals of the Rheumatic Diseases. 2004;63:636–643
  100. Boileau C, Poirier F, Pelletier JP, et al. Intracellular localization of galectin-3 has a protective role. Annals of the Rheumatic Diseases. 2008;67:175–181
  101. Janelle-Montcalm A, Boileau C, Poirier F, et al. Extracellular localization of galectin-3 has a deleterious role in joint tissues. Arthritis Research & Therapy. 2007;9:R20
  102. Martel-Pelletier J, Tardif G, Fernandes JC, Pelletier JP. Metalloproteases and their modulation as treatment in osteoarthritis. In:  Tsokos GC editors. Molecular rheumatology. Totowa, New Jersey: Humana Press Inc.; 2000;p. 499–514
  103. Benderdour M, Tardif G, Pelletier J, et al. Interleukin-17 (IL-17) induces collagenase-3 production in human osteoarthritic chondrocytes via an AP-1 dependent activation: Differential activation of AP-1 members by IL-17 and IL-1ß. The Journal of Rheumatology. 2002;29:1262–1272
  104. Tardif G, Pelletier JP, Dupuis M, et al. Collagenase 3 production by human osteoarthritic chondrocytes in response to growth factors and cytokines is a function of the physiological state of the cells. Arthritis and Rheumatism. 1999;42:1147–1158
  105. Benderdour M, Tardif G, Pelletier J-P, et al. A novel negative regulatory element in the human collagenase-3 proximal promoter region. Biochemical and Biophysical Research Communications. 2002;291:1151–1159
  106. Fan Z, Tardif G, Boileau C, et al. Identification in human osteoarthritic chondrocytes of proteins binding to the novel regulatory site AGRE in the human matrix metalloprotease 13 proximal promoter. Arthritis and Rheumatism. 2006;54:2471–2480
  107. Aigner T, Zien A, Hanisch D, Zimmer R. Gene expression in chondrocytes assessed with use of microarrays. The Journal of Bone and Joint Surgery. American Volume. 2003;85-A(Suppl. 2):117–123
  108. Okada Y, Konomi H, Yada T, et al. Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells. FEBS Letters. 1989;244:473–476
  109. Mohtai M, Smith RL, Schurman DJ, 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. 1993;92:179–185
  110. Sandy JD, Flannery CR, Neame PJ, Lohmander LS. The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. The Journal of Clinical Investigation. 1992;89:1512–1516
  111. Glasson SS, Askew R, Sheppard B, et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature. 2005;434:644–648
  112. Stanton H, Rogerson FM, East CJ, et al. ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature. 2005;434:648–652
  113. Martel-Pelletier J, Faure MP, McCollum R, et al. Plasmin, plasminogen activators and inhibitor in human osteoarthritic cartilage. The Journal of Rheumatology. 1991;18:1863–1871
  114. Eeckhout Y, Vaes G. Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation. The Biochemical Journal. 1977;166:21–31
  115. Zwicky R, Baici A. Cytoskeletal architecture and cathepsin B trafficking in human articular chondrocytes. Histochemistry and Cell Biology. 2000;114:363–372
  116. Kafienah W, Bromme D, Buttle DJ, et al. Human cathepsin K cleaves native type I and II collagens at the N- terminal end of the triple helix. The Biochemical Journal. 1998;331(Pt 3):727–732
  117. Homandberg GA, Wen C, Hui F. Cartilage damaging activities of fibronectin fragments derived from cartilage and synovial fluid. Osteoarthritis and Cartilage. 1998;6:231–244
  118. Brown RA, Jones KL. The synthesis and accumulation of fibronectin by human articular cartilage. The Journal of Rheumatology. 1990;17:65–72
  119. Wurster NB, Lust G. Synthesis of fibronectin in normal and osteoarthritic articular cartilage. Biochimica et biophysica acta. 1984;800:52–58
  120. Homandberg GA, Meyers R, Williams JM. Intraarticular injection of fibronectin fragments causes severe depletion of cartilage proteoglycans in vivo. The Journal of Rheumatology. 1993;20:1378–1382
  121. Xie D, Hui F, Homandberg GA. Fibronectin fragments alter matrix protein synthesis in cartilage tissue cultured in vitro. Archives of Biochemistry and Biophysics. 1993;307:110–118
  122. Stanton H, Ung L, Fosang AJ. The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases. The Biochemical Journal. 2002;364:181–190
  123. Xie D, Hui F, Meyers R, Homandberg GA. Cartilage chondrolysis by fibronectin fragments is associated with release of several proteinases: Stromelysin plays a major role in chondrolysis. Archives of Biochemistry and Biophysics. 1994;311:205–212
  124. Gemba T, Valbracht J, Alsalameh S, Lotz M. Focal adhesion kinase and mitogen-activated protein kinases are involved in chondrocyte activation by the 29-kDa amino-terminal fibronectin fragment. The Journal of Biological Chemistry. 2002;277:907–911
  125. Forsyth CB, Pulai J, Loeser RF. Fibronectin fragments and blocking antibodies to alpha2beta1 and alpha5beta1 integrins stimulate mitogen-activated protein kinase signaling and increase collagenase 3 (matrix metalloproteinase 13) production by human articular chondrocytes. Arthritis and Rheumatism. 2002;46:2368–2376
  126. Homandberg GA, Costa V, Ummadi V, Pichika R. Antisense oligonucleotides to the integrin receptor subunit alpha(5) decrease fibronectin fragment mediated cartilage chondrolysis. Osteoarthritis and Cartilage. 2002;10:381–393
  127. Yasuda T, Kakinuma T, Julovi SM, et al. COOH-terminal heparin-binding fibronectin fragment induces nitric oxide production in rheumatoid cartilage through CD44. Rheumatology (Oxford, England). 2004;43:1116–1120
  128. Yasuda T, Julovi SM, Hiramitsu T, et al. Requirement of mitogen-activated protein kinase for collagenase production by the fibronectin fragment in human articular chondrocytes in culture. Modern Rheumatology. 2004;14:54–60
  129. Teichtahl AJ, Wluka AE, Proietto J, Cicuttini FM. Obesity and the female sex, risk factors for knee osteoarthritis that may be attributable to systemic or local leptin biosynthesis and its cellular effects. Medical Hypotheses. 2005;65:312–315
  130. Dumond H, Presle N, Terlain B, et al. Evidence for a key role of leptin in osteoarthritis. Arthritis and Rheumatism. 2003;48:3118–3129
  131. Figenschau Y, Knutsen G, Shahazeydi S, et al. Human articular chondrocytes express functional leptin receptors. Biochemical and Biophysical Research Communications. 2001;287:190–197
  132. Otero M, Lago R, Lago F, et al. Signalling pathway involved in nitric oxide synthase type II activation in chondrocytes: synergistic effect of leptin with interleukin-1. Arthritis Research & Therapy. 2005;7:R581–R591
  133. Kimball ES, Persico FJ, Vaught JL. Substance P, neurokinin A, and neurokinin B induce generation of IL-1- like activity in P388D1 cells. Possible relevance to arthritic disease. Journal of Immunology. 1988;141:3564–3569
  134. Iannone F, Lapadula G. Neuropeptides and human osteoarthritis. The Journal of Rheumatology. 1998;25:386–388
  135. Langdon C, Kerr C, Hassen M, et al. Murine oncostatin M stimulates mouse synovial fibroblasts in vitro and induces inflammation and destruction in mouse joints in vivo. The American Journal of Pathology. 2000;157:1187–1196
  136. Plater-Zyberk C, Buckton J, Thompson S, et al. Amelioration of arthritis in two murine models using antibodies to oncostatin M. Arthritis and Rheumatism. 2001;44:2697–2702
  137. Hui W, Barksby HE, Young DA, et al. Oncostatin M in combination with tumour necrosis factor {alpha} induces a chondrocyte membrane associated aggrecanase that is distinct from ADAMTS aggrecanase-1 or -2. Annals of the Rheumatic Diseases. 2005;64:1624–1632
  138. Barksby HE, Hui W, Wappler I, et al. Interleukin-1 in combination with oncostatin M up-regulates multiple genes in chondrocytes: implications for cartilage destruction and repair. Arthritis and Rheumatism. 2006;54:540–550
  139. Saha N, Moldovan F, Tardif G, et al. Interleukin-1β-converting enzyme/Caspase-1 in human osteoarthritic tissues: localization and role in the maturation of IL-1β and IL-18. Arthritis and Rheumatism. 1999;42:1577–1587
  140. Boileau C, Martel-Pelletier J, Moldovan F, et al. The in situ up-regulation of chondrocyte interleukin-1-converting enzyme and interleukin-18 levels in experimental osteoarthritis is mediated by nitric oxide. Arthritis and Rheumatism. 2002;46:2637–2647
  141. Notoya K, Jovanovic DV, Reboul P, et al. The induction of cell death in human osteoarthritis chondrocytes by nitric oxide is related to the production of prostaglandin E2 via the induction of cyclooxygenase-2. Journal of Immunology. 2000;165:3402–3410
  142. Pelletier JP, Jovanovic DV, Lascau-Coman V, et al. Selective inhibition of inducible nitric oxide synthase reduces progression of experimental osteoarthritis in vivo: possible link with the reduction in chondrocyte apoptosis and caspase 3 level. Arthritis and Rheumatism. 2000;43:1290–1299
  143. Kojima F, Naraba H, Miyamoto S, et al. Membrane-associated prostaglandin E synthase-1 is upregulated by proinflammatory cytokines in chondrocytes from patients with osteoarthritis. Arthritis Research & Therapy. 2004;6:R355–R365
  144. Masuko-Hongo K, Berenbaum F, Humbert L, et al. Up-regulation of microsomal prostaglandin E synthase 1 in osteoarthritic human cartilage: critical roles of the ERK-1/2 and p38 signaling pathways. Arthritis and Rheumatism. 2004;50:2829–2838
  145. Li X, Afif H, Cheng S, et al. Expression and regulation of microsomal prostaglandin E synthase-1 in human osteoarthritic cartilage and chondrocytes. The Journal of Rheumatology. 2005;32:887–895
  146. Wittenberg RH, Willburger RE, Kleemeyer KS, Peskar BA. In vitro release of prostaglandins and leukotrienes from synovial tissue, cartilage, and bone in degenerative joint diseases. Arthritis and Rheumatism. 1993;36:1444–1450
  147. Jovanovic DV, Fernandes JC, Martel-Pelletier J, et al. The in vivo dual inhibition of cyclooxygenase and lipoxygenase by ML-3000 reduces the progression of experimental osteoarthritis. Suppression of collagenase-1 and interleukin-1beta synthesis. Arthritis and Rheumatism. 2001;44:2320–2330
  148. He W, Pelletier JP, Martel-Pelletier J, et al. The synthesis of interleukin-1beta, tumour necrosis factor-a and interstitial collagenase (MMP-1) is eicosanoid dependent in human OA synovial membrane explants: interactions with anti-inflammatory cytokines. The Journal of Rheumatology. 2002;29:546–553
  149. Paredes Y, Massicotte F, Pelletier JP, et al. Study of the role of leukotriene B4 in abnormal function of human subchondral osteoarthritis osteoblasts: effects of cyclooxygenase and/or 5-lipoxygenase inhibition. Arthritis and Rheumatism. 2002;46:1804–1812
  150. Celotti F, Durand T. The metabolic effects of inhibitors of 5-lipoxygenase and of cyclooxygenase 1 and 2 are an advancement in the efficacy and safety of anti-inflammatory therapy. Prostaglandins & Other Lipid Mediators. 2003;71:147–162
  151. Macfarlane SR, Seatter MJ, Kanke T, et al. Proteinase-activated receptors. Pharmacological Reviews. 2001;53:245–282
  152. Lindner JR, Kahn ML, Coughlin SR, et al. Delayed onset of inflammation in protease-activated receptor-2-deficient mice. Journal of Immunology. 2000;165:6504–6510
  153. Ferrell WR, Lockhart JC, Kelso EB, et al. Essential role for proteinase-activated receptor-2 in arthritis. The Journal of Clinical Investigation. 2003;111:35–41
  154. Boileau C, Amiable N, Martel-Pelletier J, et al. Activation of proteinase-activated receptor 2 in human osteoarthritic cartilage upregulates catabolic and proinflammatory pathways capable of inducing cartilage degradation: a basic science study. Arthritis Research and Therapy. 2007;9:R121
  155. Xiang Y, Masuko-Hongo K, Sekine T, et al. Expression of proteinase-activated receptors (PAR)-2 in articular chondrocytes is modulated by IL-1beta, TNF-alpha and TGF-beta. Osteoarthritis and Cartilage. 2006;14:1163–1173
  156. Massicotte F, Lajeunesse D, Benderdour M, et al. Can altered production of interleukin 1β, interleukin-6, transforming growth factor-ß and prostaglandin E2 by isolated human subchondral osteoblasts identify two subgroups of osteoarthritic patients. Osteoarthritis and Cartilage. 2002;10:491–500
  157. Konttinen YT, Mandelin J, Li TF, et al. Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis. Arthritis and Rheumatism. 2002;46:953–960
  158. Nakase T, Kaneko M, Tomita T, et al. Immunohistochemical detection of cathepsin D, K, and L in the process of endochondral ossification in the human. Histochemistry and Cell Biology. 2000;114:21–27
  159. Garnero P, Delmas PD. Biomarkers in osteoarthritis. Current Opinion in Rheumatology. 2003;15:641–646
  160. Garnero P. Use of biochemical markers to study and follow patients with osteoarthritis. Current Rheumatology Reports. 2006;8:37–44
  161. Sugiyama S, Itokazu M, Suzuki Y, Shimizu K. Procollagen II C propeptide level in the synovial fluid as a predictor of radiographic progression in early knee osteoarthritis. Annals of the Rheumatic Diseases. 2003;62:27–32
  162. Rousseau JC, Zhu Y, Miossec P, et al. Serum levels of type IIA procollagen amino terminal propeptide (PIIANP) are decreased in patients with knee osteoarthritis and rheumatoid arthritis. Osteoarthritis and Cartilage. 2004;12:440–447
  163. Lohmander LS, Yoshihara Y, Roos H, et al. Procollagen II C-propeptide in joint fluid: changes in concentration with age, time after knee injury, and osteoarthritis. The Journal of Rheumatology. 1996;23:1765–1769
  164. Poole AR, Dieppe P. Biological markers in rheumatoid arthritis. Seminars in Arthritis and Rheumatism. 1994;23:17–31
  165. Saito S, Kondo S, Mishima S, et al. Analysis of cartilage-derived retinoic-acid-sensitive protein (CD-RAP) in synovial fluid from patients with osteoarthritis and rheumatoid arthritis. The Journal of Bone and Joint Surgery. British Volume. 2002;84:1066–1069
  166. Schmidt-Rohlfing B, Schneider U, Thomsen M, Bosserhoff AK. Correlation of a novel matrix protein with the degree of cartilage degradation. Rheumatology International. 2002;22:165–169
  167. Garnero P, Christgau S, Delmas PD. The bisphosphonate zoledronate decreases type II collagen breakdown in patients with Paget's disease of bone. Bone. 2001;28:461–464
  168. Christgau S, Cloos PAC. Cartilage degradation products as markers for evaluation of patients with rheumatic disease. Clinical and Applied Immunology Reviews. 2004;4:277–294
  169. Downs JT, Lane CL, Nestor NB, et al. Analysis of collagenase-cleavage of type II collagen using a neoepitope ELISA. Journal of Immunological Methods. 2001;247:25–34
  170. Billinghurst RC, Wu W, Ionescu M, et al. Comparison of the degradation of type II collagen and proteoglycan in nasal and articular cartilages induced by interleukin-1 and the selective inhibition of type II collagen cleavage by collagenase. Arthritis and Rheumatism. 2000;43:664–672
  171. Charni N, Juillet F, Garnero P. Urinary type II collagen helical peptide (HELIX-II) as a new biochemical marker of cartilage degradation in patients with osteoarthritis and rheumatoid arthritis. Arthritis and Rheumatism. 2005;52:1081–1090
  172. Oldberg A, Antonsson P, Lindblom K, Heinegard D. COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. The Journal of Biological Chemistry. 1992;267:22346–22350
  173. Di Cesare PE, Fang C, Leslie MP, et al. Expression of cartilage oligomeric matrix protein (COMP) by embryonic and adult osteoblasts. Journal of Orthopaedic Research. 2000;18:713–720
  174. Rosenberg K, Olsson H, Morgelin M, Heinegard D. Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. The Journal of Biological Chemistry. 1998;273:20397–20403
  175. Sharif M, Kirwan JR, Elson CJ, et al. Suggestion of nonlinear or phasic progression of knee osteoarthritis based on measurements of serum cartilage oligomeric matrix protein levels over five years. Arthritis and Rheumatism. 2004;50:2479–2488
  176. Wislowska M, Jablonska B. Serum cartilage oligomeric matrix protein (COMP) in rheumatoid arthritis and knee osteoarthritis. Clinical Rheumatology. 2005;24:278–284
  177. Conrozier T, Carlier MC, Mathieu P, 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. 2000;59:828–831
  178. Skoumal M, Haberhauer G, Kolarz G, et al. Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction. Arthritis Research & Therapy. 2005;7:R65–R70
  179. Garnero P. Use of biochemical markers to study and follow patients with osteoarthritis. Current Primary Care Reports. 2007;2:10–17
  180. Gineyts E, Garnero P, Delmas PD. Urinary excretion of glucosyl-galactosyl pyridinoline: a specific biochemical marker of synovium degradation. Rheumatology (Oxford, England). 2001;40:315–323
  181. Gineyts E, Mo JA, Ko A, et al. Effects of ibuprofen on molecular markers of cartilage and synovium turnover in patients with knee osteoarthritis. Annals of the Rheumatic Diseases. 2004;63:857–861
  182. Senolt L, Braun M, Olejarova M, et al. Increased pentosidine, an advanced glycation end product, in serum and synovial fluid from patients with knee osteoarthritis and its relation with cartilage oligomeric matrix protein. Annals of the Rheumatic Diseases. 2005;64:886–890
  183. Kauffmann C, Gravel P, Godbout B, et al. Computer-aided method for quantification of cartilage thickness and volume changes using MRI: validation study using a synthetic model. IEEE Transactions on Bio-medical Engineering. 2003;50:978–988
  184. Raynauld JP, Kauffmann C, Beaudoin G, et al. Reliability of a quantification imaging system using magnetic resonance images to measure cartilage thickness and volume in human normal and osteoarthritic knees. Osteoarthritis and Cartilage. 2003;11:351–360
  185. Cicuttini F, Forbes A, Morris K, et al. Gender differences in knee cartilage volume as measured by magnetic resonance imaging. Osteoarthritis and Cartilage. 1999;7:265–271
  186. Jones G, Glisson M, Hynes K, Cicuttini F. Sex and site differences in cartilage development: a possible explanation for variations in knee osteoarthritis in later life. Arthritis and Rheumatism. 2000;43:2543–2549
  187. Raynauld JP, Martel-Pelletier J, Berthiaume MJ, et al. Quantitative magnetic resonance imaging evaluation of knee osteoarthritis progression over two years and correlation with clinical symptoms and radiologic changes. Arthritis and Rheumatism. 2004;50:476–487
  188. Berthiaume MJ, Raynauld JP, Martel-Pelletier J, et al. Meniscal tear and extrusion are strongly associated with the progression of knee osteoarthritis as assessed by quantitative magnetic resonance imaging. Annals of the Rheumatic Diseases. 2005;64:556–563

PII: S1521-6942(08)00013-2

doi: 10.1016/j.berh.2008.02.001

Best Practice & Research Clinical Rheumatology
Volume 22, Issue 2 , Pages 351-384 , April 2008

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