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• W2170991844 abstract "Equine Veterinary JournalVolume 26, Issue 4 p. 263-277 Joint structure, biochemistry and biochemical disequilibrium in synovitis and equine joint disease JAN L. PALMER, JAN L. PALMER Orthopaedic Research Laboratory, Department of Veterinary Clinical Sciences, College of Veterinary Medicine, The Ohio State University, 601 Vernon L. Tharp St., Columbus, Ohio 43210-1089, USA.Search for more papers by this authorALICIA L. BERTONE, ALICIA L. BERTONE Orthopaedic Research Laboratory, Department of Veterinary Clinical Sciences, College of Veterinary Medicine, The Ohio State University, 601 Vernon L. Tharp St., Columbus, Ohio 43210-1089, USA.Search for more papers by this author JAN L. PALMER, JAN L. PALMER Orthopaedic Research Laboratory, Department of Veterinary Clinical Sciences, College of Veterinary Medicine, The Ohio State University, 601 Vernon L. Tharp St., Columbus, Ohio 43210-1089, USA.Search for more papers by this authorALICIA L. BERTONE, ALICIA L. BERTONE Orthopaedic Research Laboratory, Department of Veterinary Clinical Sciences, College of Veterinary Medicine, The Ohio State University, 601 Vernon L. Tharp St., Columbus, Ohio 43210-1089, USA.Search for more papers by this author First published: July 1994 https://doi.org/10.1111/j.2042-3306.1994.tb04386.xCitations: 49AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References Abbas, A.K., Lichtman, A.H. and Pober, J.S. (1991) Cytokines. In: Cellular Molecular Immunology. Eds: A. K. Abbas, A. H. Lichtman and J. S. Pober. Saunders Co., Philadelphia , pp 225–243. Abbot, S.E., Kaul, A., Stevens, C.R. and Blake, D.R. (1992) Isolation and culture of synovial microvascular endothelial cells. Arth. Rheum. 35, 401–406. Amer, E.C. and Pratta, M.A. (1991) Modulation of interleukin-1 induced alterations in cartilage proteoglycan metabolism by activation of protein kinase C. Arth. Rheum. 37, 1006–1013. Aydelotte, M.B., Schumacher, B.L., Kuszak, J.R. and Kuettner, K.E. (1990) Ultrastructural changes in cultures of bovine articular chondrocytes treated with interleukin-1. Proc. 36th Ann. Mtg, Orlhop, Res. Soc, New Orleans, p 322. Barrett, A.J. (1981) Which enzymes degrade cartilage matrix? In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier. Amsterdam , pp 185–193. Bunning, R.A.D., Richardson, H.J., Crawford, A., Skjodt, H., Hughes, D., Evans, D.B., Gowen, M., Dobson, P.R.M., Brown, B.L. and Russell, R.G.G. (1986) The effect of interleukin-1 on connective tissue metabolism and its relevance to arthritis. Recent Adv. Conn. Tiss. Res. 18, 131–152. Burba, D.J., Collier, M.A., DeBault, L.E., and Painton, O.H. (1992) In vivo kinetic study of intramuscular tritium-labeled polysulfated glycosaminoglycan in equine body fluid compartments and articular cartilage in a physically induced arthritis model. Proc: 18th Ann. Conf. Vet. Orthop. Soc. p 2. Caron, J.P., Eberhart, S.W. and Nachreiner, R. (1991) Influence of polysulfated glycosaminoglycans on equine articular cartilage in explant culture. Am. J. vet. Res. 52, 1622–1625. Carter, B.G., Bertone, A.L., Weisbrode, S.E., Bailey, M.Q., Andrews, J.M., and Palmer, J.L. (1992) Influence of Steroid supression on osteochondral healing in stressed equine tarsocrural joints. Vet. Surg. 22, 386. Chang, J., Gilman, S.C. and Lewis, A.J. (1986) Interleukin 1 activates phospholipase A2 in rabbit chondrocytes: a possible signal for IL-1 action. J. Immunol. 136, 1283–1287. Chin, J.E., Winterrowd, G.E., Krzesicki, R.F. and Sanders, M.E. (1990) Role of cytokines in inflammatory synovitis: coordinate regulation of intercellular adhesion molecule 1 and HLA class I and class II antigens in rheumatoid synovial fibroblasts. Arth. Rheum. 33, 1776–1785. Chunekamrai, S., Krook, L.P., Lust, G. and Maylin, G.A. (1989) Changes in articular cartilage after intra-articular injections of methylprednisolone acetate in horses. Am. J. vet. Res. 50, 1733–1741. Collier, S. and Ghosh, P. (1988) The role of plasminogen in interleukin-1 mediated cartilage degradation. J. Rheum. 15, 1129–1137. Cronstein, B.N. and Weissmann, G. (1993) The adhesion molecules of inflammation. Arth. Rheum. 36, 147–157. Davies, P., Bonney, R.J., Humes, J.L. and Kuehl, F.A. (1981) Secretory functions of macrophages participating in inflammatory responses. In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier, Amsterdam , pp 35–42. Dayer, J.M. and Seckinger, P. (1988) Interleukin 1 and interleukin 1 inhibitors and their relation to connective tissue destruction. In: the Control of Tissue Damage. Ed: A. M. Glauert Elsevier, Amsterdam , pp 151–163. Dingle, J.T., Thomas, D.P.P., King, B. and Bard, D.R. (1987) In vivo studies of articular tissue damage mediated by catabolin/interleukin 1. Ann. rheum. Dis. 46, 527–533. Dingle, J.T. and Tyler, J.A. (1986) Role of intercellular messengers in the control of cartilage matrix dynamics. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 181–193. Docherty, A.J.P. and Murphy, G. (1990) The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins. Ann. rheum. Dis. 49, 469–479. Ehrlich, M.G., Armstrong, A.L., Treadwell, B.V. and Mankin, H.J. (1986) Degradative enzyme systems in cartilage. Clin. Orthop. rel. Res. 213, 62–67. Eyre, D.R., Wu, J.-J. and Woods, P. (1992) Cartilage-specific collagens: structural studies. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York . pp. 119–131. Fava, R.A., Olsen, N.J., Postlethwaite, A.E., Broadley, K.N., Davidson, J.M., Nanney, L.B., Lucas, C. and Townes, A.S. (1991) Transforming growth factor B1 induced neutrophil recruitment to synovial tissues: implications for TGF-B driven synovial inflammation and hyperplasia. J. exp. Med. 173, 1121–1132. Fell, H.B. and Jubb, R.W. (1977) The effect of synovial tissue on the breakdown of articular cartilage in organ culture. Arth. Rheum. 20, 1359–1371. Fujii, K., Tajiri, K., Tanaka, T. and Murota, K. (1989) Effects of nonsteroidal antiinflammatory drugs on collagen biosynthesis of cultured chondrocytes. Sem. Arth. Rheum. 18 (Suppl 1), 16–18 Ghosh, P. (1989) Therapeutic modulation of cartilage catabolism by nonsteroidal antiinflammatory drugs in arthritis. Sem. Arth. Rheum. 18 (Suppl 1), 2–6. Ghosh, P. and Brooks, P. (1991) Chondroprotection - exploring the concept. J. Rheum. 18, 161–165. Ghosh, P., Collier, S. and Andrews, J. (1987) Synovial membrane-cartilage interactions - the role of serine proteinase inhibitors in interleukin-1 mediated degradation of articular damage. J. Rheum. 14 (Suppl), 122–124. Glade, M.J. (1990) Polysulfated glycosaminoglycan accelerates net synthesis of collagen and glycosaminoglycans by arthritic equine cartilage tissues and chondrocytes. Am. J. vet. Res. 51, 779–785. Greenwald, R.A., Moy, W.W. and Seibold, J. (1978) Functional properties of cartilage proteoglycans. Sem. Arth. Rheum. 8, 53–67. Greiling, H., Kleesiek, K. and Reinards, R. (1986) Interaction of synovial cells and synovial fluid with cartilage. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 195–210. Greisen, H.A., Summers, B.A. and Lust, G. (1982) Ultrastructure of the articular cartilage and synovium in the early stages of degenerative joint disease in canine hip joints. Am. J. vet. Res. 43, 1963–1971. Guerne, P.A., Zuraw, B.L., Vaughan, J.H., Carson, D.A. and Lou, M. (1989) Synovium as a source of interleukin 6 in-vitro. J. clin. Invest. 83, 585–592. Hardingham, T.E. (1988) Biosynthesis, assembly, and turnover of cartilage proteoglycans. In: The Control of Tisssue Damage. Ed: A. M. Glauert Elsevier, Amsterdam , pp 41–53. Hardingham, T. and Bayliss, M. (1990) Proteoglycans of articular cartilage: changes in ageing and joint disease. Sem. Arth. Rheum. 20, 12–33. Hardingham, T.E., Fosang, A.J. (1992) Proteoglycans; many forms and functions. FASEB J. 6, 861–870. Hardingham, T.E., Fosang, A.J. and Dudhia, J. (1992) Aggrecan, the chondroitin sulfate/keratan sulfate proteoglycan from cartilage. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 5–20. Hasty, K.A., Reife, R.A., Kang, A.H. and Stuart, J.M. (1990) The role of stromelysin in the cartilage destruction that accompanies inflammatory arthritis. Arth. Rheum. 33, 388–397. Heinegard, D.K. and Pimental, E.R. (1992) Cartilage matrix proteins. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 95–111. Henderson, B. and Pettipher, E.R. (1985) The synovial lining cell: biology and pathobiology. Sem. Arth. Rheum. 15, 1–32. Henderson, B., Thompson, R.C., Hardingham, T. and Lewthwaite, J.L. (1991) Inhibition of interleukin-1 induced synovitis and articular cartilage proteoglycan loss in the rabbit knee by recombinant human interleukin-1 receptor antagonist. Cytokines 3, 246–249. Henson, P.M., Webster, R.O. and Henson, J.E. (1981) Neutrophil and monocyte activation and secretion: role in surfaces in inflammatory reactions and in-vitro. In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier, Amsterdam , pp 43–56. Houssiau, F.A., Devogelaer, J.P., Van Damme, J., Deuxchaisnes, C.N. and Van Snick, J. (1988) Interleukin-6 in synovial fluid and serum of patients with rheumatoid arthritis and other inflammatory arthritides. Arth. Rheum. 31, 784–788. Howard, R.D. and McIlwraith, C.W. (1993) Sodium hyaluronate in the treatment of equine joint disease. Comp. com. educ. pract. Vet. 15, 473–481. Hunziker, E.B. (1992) Articular cartilage structure in humans and experimental animals. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 183–199. Irvine, R.F. (1988) The role of phospholipids in the generation and action of mediators. In: the Control of Tissue Damage. Ed: A. M. Glauert Elsevier, Amsterdam , pp 111–123. Johansson, H.E. and Rejno, S. (1976) Light and electron microscopic investigation of equine synovial membrane. Acta vet. Scand. 17, 153–168. Johnson, B.A., Haines, G.K., Harlow, L.A. and Koch, A.E. (1993) Adhesion molecule expression in human synovial tissue. Arth. Rheum. 36, 137–146. Jones, I.L., Larsson, S.E. and Lemperg, R. (1977) The glycosaminoglycans of human articular cartilage. Clin. Orthop. rel. Res. 127, 257–264. Jubb, R.W. and Fell, H.B. (1980) The effect of synovial tissue on the synthesis of proteoglycan by the articular cartilage of young pigs. Arth. Rheum. 23, 545–554. Kahle, P., Saal, J.G., Schaudt, K., Zacher, J., Firtz, P. and Pawelec, G. (1992) Determination of cytokines in synovial fluids: correlation with diagnosis and histomorphometrical characteristics of synovial tissue. Ann. Rheum. Dis. 51, 731–734. Kandel, R.A., Petelycky, M., Dinarello, C.A., Minden, M., Pritzker, K.P.H. and Cruz, T.F. (1990) Comparison of effect of interleukin-6 and interleukin-1 on collagenase and proteoglycan production by chondrocytes. J. Rheum. 17, 953–957. Kitsis, E. and Weissmann, G. (1991) The role of the neutrophil in rheumatoid arthritis. Clin. Orthop. rel. Res. 265, 63–72. Kowanko, I.C., Bates, E.J. and Ferrante, A. (1992) Platelet-activating factor inhibits proteoglycan synthesis and enhances neutrophil-mediated proteoglycan degradation in cartilage explants. Arth. Rheum. 35, 918–925. Krane, S.M. and Amento, E.P. (1983) Cellular interactions and control of collagenase secretion in the synovium. J. Rheum. 11 (Suppl), 7–12. Krane, S.M., Amento, E.P., Goldring, M.B., Goldring, S.R., Stephenson, M.L., Plloa, B., Bhan, A.K. and Kumick, J.T. (1986) Cellular interaction and matrix destruction during inflammatory processes within the joints. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 413–422. Larsen, N.E., Lombard, K.M., Parent, E.G., and Balazs, E.A. (1992) Effect of hylan on cartilage and chondrocyte cultures. J. orthop. Res. 10, 23–32. Lazarus, G.S., Thomas, C.A. and Balakrishnan, C.V. (1981) Proteinases as mediators of inflammation. In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier, Amsterdam , pp 197–203. Lin, C.W., Phillips, S.L., Brinckerhoff, C.E., Georgescu, H.I., Bandara, G. and Evans, C.H. (1988) Induction of collagenase mRNA in lapine articular chondrocytes by synovial factors and interleukin-1. Arch. Biochem. 264, 351–354. Lindahl, U. and Roden, L. (1972) Carbohydrate-peptide linkages in proteoglycans of animal, plant and bacterial origin. In: Glycoproteins: Their Composition, Structure and Function. Ed: A. Gottschalk Elsevier, Amsterdam , pp 491–517. Lohmander, L.S. and Kimura, J.H. (1986) Biosynthesis of cartilage proteoglycans. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 93–112. Lowther, D.A., Sriratana, A. and Baker, M.S. (1992) Effect of inflammation on cartilage metabolism. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 543–558. MacDonald, M.H., Stover, S.M., Willits, N.H. and Benton. H.P. (1992) Regulation of matrix metabolism in equine cartilage explant cultures by interleukin-1. Am. J. vet. Res. 53, 2278–2285. Mankin, H.J. and Lippiello, I. (1969) The turnover of adult rabbit articular cartilage. J. Bone Joint Surg. 51-A, 1591–1600. May, S.A. (1992) Anti-inflammatory Agents. In: Current Therapy in Equine Medicine. Ed: N. E. Robinson. W. B. Saunders, Philadelphia , pp 14–18. May, S.A., Hooke, R.E. and Lees, P. (1988) Bone fragments stimulate equine synovial lining cells to produce the inflammatory mediator prostaglandin E2. Equine vet. J. Suppl. 6, 131–132. May, S.A., Hooke, R.E. and Lees, P. (1990) The characterisation of equine interleukin-1. Vet. Immunol. Immunopath. 24, 169–175. May, S.A., Hooke, R.E. and Lees, P. (1992a) Inhibition of interleukin-1 activity by equine synovial fluid. Equine vet. J. 24, 99–102. May, S.A., Hooke, R.E. and Lees, P. (1992b) Interleukin-1 stimulation of equine articular cells. Res. vet. Sci. 52, 342–348. Mayne, R. (1989) Cartilage Collagens. Arth. Rheum. 32, 241–246. Mayne, R. and Irwin, M.H. (1986) Collagen types in cartilage. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 23–38. McGuire, M.B., Murphy, G., Reynolds, J.J. and Russell, R.G.G. (1981) Production of collagenase and inhibitor (TIMP) by normal, rheumatoid and osteoarthritic synovium in-vitro: effects of hydrocortisone and indomethacin. Clin. Sci. 61, 703–710. McIlwraith, C.W. (1987) Diseases of joints, tendons, ligaments, and related structures. In: Adams Lameness in Horses. Ed: T. S. Stashak Lea and Febiger, Philadelphia , pp 360–395. Mimuro, J. and Loskutoff, D.J. (1989) Purification of a protein from bovine plasma that binds to Type 1 plasminogen activator inhibitor and prevents its interaction with extracellular matrix. J. Biol. Chem. 264, 936–939. Mochan, E. and Uhl, J. (1984) Elevations in synovial fluid plasminogen activator in patients with rheumatoid arthritis. J. Rheum. 11, 123–128. Morales, T.I. (1992) Polypeptide regulators of matrix homeostasis in articular cartilage. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp. 265–279. Morris, E.A., McDonald, B.S., Webb, A.C. and Rosenwasser, L.J. (1990) Identification of interleukin-1 in equine osteoarthritic joint effusions. Am. J. vet. Res. 51, 59–64. Morris, E.A., Wilcon, S. and Treadwell, B.V., (1992) Inhibition of interleukin-1 mediated proteoglycan degradation in bovine articular cartilage explants by addition of sodium hyaluronate. Am. J. vet. Res. 53, 1977–1982. Muirden, K.D. (1972) Lysosomal enzymes in synovial membrane in rheumatoid arthritis. Ann. Rheum. Dis. 31, 265–271. Muller, D., Quantin, B., Gesnel, M., Millon-Collard, R., Abecassis, J. and Breathnach, R. (1988) The collagenase gene family in humans consists of at least four members. Biochem. J. 253, 187–192. Murphy, G., Cockett, M.I., Stephens, P.S., Smith, B.J. and Docherty, A.J.P. (1987) Stromelysin is an activator of procollagenase. Biochem. J. 248, 265–268. Murphy, G., Docherty, A.J.P., Hembry, R.M., and Reynolds, J.J. (1991) Metalloproteinases and tissue damage. Br. J. Rheum. 30 (Suppl.), 25–31. O'Byrne, E.M., Blancuzzi, V., Wilson, D.E., Wong, M. and Jeng, A.Y. (1990) Elevated substance P and accelerated cartilage degradation in rabbit knees injected with interleukin-1 and tumor necrosis factor. Arth. Rheum. 33, 1023–1028. Okada, Y., Nagase, H. and Harris, E.D. (1986) A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. J. Biol. Chem. 261, 14245–14255. Pelletier, J.M., Faure, M.P., McCollum, R., Mineau, F., Cloutier, J.M. and Pelletier, J.P. (1991) Plasmin, plasminogen activators and inhibitor in human osteoarthritic cartilage. J. Rheum. 18, 1863–1871. Pelletier, J.M. and Pelletier, J.P. (1987) Neutral proteases in human osteoarthritic synovium: quantification and characterization. J. Rheum. 14, 38–40. Pelletier, J.M., Pelletier, J.P. and Malemud, C.J. (1988) Activation of neutral metalloproteinases in human osteoarthritic knee cartilage: evidence for degradation in the core protein of sulphated proteoglycan. Ann. Rheum. Dis. 47, 801–808. Pelletier, J.P., Pelletier, J.M., Mehraban, F. and Malemud, C.J. (1992) Immunological analysis of proteoglycan structural changes in the early stage of experimental osteoarthritic canine cartilage lesion. J. Orthop. Res. 10, 511–523. Pelletier, J.P., Pelletier, J.M., Mnaymneh, L.G., Howell, D.S. and Woessner, J.F. (1985) Role of synovial membrane inflammation in cartilage matrix breakdown in the Pond-Nuki dog model of osteoarthritis. Arth. Rheum. 28, 554–561. Pelletier, J.P., Roughley, P.J., DiBattista, J.A., McCollum, R. and Pelletier, J.M. (1991) Are cytokines involved in osteoarthritic pathophysiology Sem. Arth. Rheum. 20, 12–25. Prehm, P. (1986) Mechanism, localization, and inhibition of hyaluronate. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 81–92. Rainsford, K.D. (1985) Effects of anti-inflammatory drugs on catabolin-induced cartilage destruction in-vitro. Int. J. Tiss. Res. 7, 123–126. Rashmir-Raven, A.M., Coyne, C.P., Fenwick, B.W., Gaughan, E.M., Andrews, G.A. and DeBowes, R.M. (1992) Inhibition of equine complement activity by polysulfated glycosaminoglycans. Am. J. vet. Res. 53, 87–90. Ratcliffe, A., Azzo, W., Saed-Nejad, F., Lane, N., Rosenwasser, M.P. and Mow, V.C. (1993) In vivo effects of naproxen on composition, proteoglycan metabolism, and matrix metalloproteinase activities in canine articular cartilage. J. Orthop. Res. 11, 163–171. Reynolds, J.J., Bunning, R.A.D., Cawston, TE. and Murphy, G. (1981) Tissue metalloproteinase inhibitors and their role in matrix catabolism. In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier, Amsterdam , pp 205–230. Ridge, S.C., Oronsky, A.L. and Kerwar, S.S. (1980) Induction of the synthesis of latent collagenase and latent neutral protease in chondrocytes by a factor synthesized by activated macrophages. Arth. Rheum. 23, 448–454. Rosenburg, L.C. (1992) Structure and function of dermatan sulfate proteoglycans in articular cartilage. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 45–63. Rosenberg, L.C. and Buckwalter, J.A. (1986) Cartilage proteoglycans. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 39–54. Roughley, P.J., Nguyen, Q. and Mort, J.S. (1992) The role of proteinases and oxygen radicals in the degradation of human articular cartilage. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 305–317. Saklatvala, J. (1986) Tumor necrosis factor alpha stimulates resorption and inhibits synthesis of proteoglycan in cartilage. Nature. 322, 547–549. Saklatvala, J. and Sarsfield, S.J. (1988) How do interleukin 1 and tumor necrosis factor induce degradation of proteoglycan in cartilage? In: The Control of Tissue Damage. Ed: A. M. Glauert, Elsevier, Amsterdam , pp 97–108. Samuelsson, B., Goldyne, M., Granstrom, E., Hamberg, M., Hammarstrom, S. and Malmsten, C. (1978) Prostaglandins and thromboxanes. Ann. Rev. Biochem. 47, 997–1029. Sandy, J.D., Flannery, C.R., Neame, P.J., Lohmander, L.S. (1992) The structure of aggrecan fragments in human synovial fluid. J. clin. Invest. 89, 1512–1516. Schenk, R.K., Eggli, P.S., and Hunziker, E.B. (1986) Articular Cartilage Morphology. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp 3–22. Shimazu, A., Ikko, A., Iwamoto, M., Koike, T., Yan, W., Okada, Y., Shinmei, M., Nakamura, S. and Kato, Y. (1993) Effects of hyaluronic acid on the release of proteoglycan from the cell matrix in rabbit chondrocyte cultures in the presence and absence of cytokines. Arth. Rheum. 36, 247–253. Shinmei, M., Masuda, K., Kikuchi, T. and Shimormura, Y. (1989) Interleukin-1, tumor necrosis factor, and interleukin-6 as mediators of cartilage destruction. Sem. Arth. Rheum. 18, 27–32. Shoemaker, R.S., Bertone, A.L., Martin, G.S., McIlwraith, C.W., Roberts, E.D. and Pechman, R. (1992) Effects of intra-articular methylprednisolone acetate on normal articular cartilage and on the healing of experimentally induced osteochondral defects in horses. Am. J. vet. Res. 53, 1446–1453. Situnayake, R.D., Thurnham, D.I., Kootathep, S., Chirico, S., Lunee, J., Davis, M. and McConkey, B. (1991) Chain breaking antioxidant status in rheumatic arthritis: clinical and laboratory correlates. Ann. Rheum. Dis. 50, 81–86. Sledge, C.B. and Steinberg, J.J. (1981) Co-cultivation models of joint destruction. In: Cellular Interactions. Eds: J. T. Dingle and J. L. Gordon. Elsevier, Amsterdam . pp 263–280. Snyderman, R. (1986) Mechanisms of inflammation and leucocyte chemotaxis in the rheumatic diseases. Med. Clin. N. Am. 70, 217–235. Steinberg, J.J. and Sledge, C.B. (1991) Chondrocyte mediated cartilage degradation: regulation by prostaglandin E2, cyclic AMP, and interferon alpha. J. Rheum. 18, 63–65. Todhunter, R.J. and Lust, G. (1990) Pathophysiology of synovitis: clinical signs and examination in horses. Comp. cont. educ. pract. Vet. 12, 980–992. Torbeck, R.L. and Prieur, D.J. (1979) Plasma and synovial fluid lysozyme activity in horses with experimental cartilage defects. Am J. vet. Res. 40, 1532–1536. Treadwell, B.V. and Mankin, H.J. (1986) The synthetic processes of articular cartilage. Clin. Orthop. rel. Res. 213, 50–61. Treadwell, B.V., Pavia, M., Towle, C.A., Cooley, V.J. and Mankin, H.J. (1991) Cartilage synthesizes the serine protease inhibitor PAI-1: support for the involvement of serine proteases in cartilage remodeling. J. Orthop. Res. 9, 309–316. Trotter, G.W., McIlwraith, C.W., Yovich, J.V., Norrdin, R.W., Wrigley, R.H. and Lamar, C.H. (1990) Effects of intra-articular administration of methylprednisolone acetate on normal equine articular cartilage. Am. J vet. Res. 52, 83–87. Tyler, J.A. (1989) Insulin-like growth factor 1 can decrease degradation and promote synthesis of proteoglycan in cartilage exposed to cytokines. Biochem. J. 260, 543–548. Tyler, J.A., Bolis, S., Dingle, J.T. and Middleton, J.F.S. (1992) Mediators of matrix catabolism. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 251–264. Vachon, A.M., Keeley, F.W., McIlwraith, C.W. and Chapman, P. (1990) Biochemical analysis of normal articular cartilage. Am. J. vet. Res. 51, 1905–1911. Yovich, J.V., Trotter, G.W., McIlwraith, C.W. and Norrdin, R.W. (1987) Effects of polysulfated glycosaminoglycan on chemical and physical defects in equine articular cartilage. Am. J. vet. Res. 48, 1407–1414. Van Kempen, G.P.J., Van de Stadt, R.J., Van de Laar, M.A.F.J. and Van der Korst, J.K. (1992) Two distinct metabolic pools of proteoglycans in articular cartilage. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York , pp 281–289. von der Mark, K., Mollenhauer, J., Pfaffle, M., van Mexel M. and Muller, P.K. (1986) Role of anchorin CII in the interaction of chondrocytes with extracellular collagen. In: Articular Cartilage Biochemistry. Eds: K. Kuettner, R. Schlerebach and V. C. Hascall. Raven Press, New York , pp. 125–142. Werb, Z. (1992) The biological role of metalloproteinases and their inhibitors. In: Articular Cartilage and Osteoarthritis. Ed: K. Kuettner Raven Press, New York . pp 295–304. Williams, T.J. (1979) Prostaglandin E2, prostaglandin I2 and the vascular changes of inflammation. Br. J. Pharm. 65, 517–524. Witsch-Prehm, P., Karbowski, A., Ober, B. and Kresse, H. (1992) Influence of continuous infusion of interleukin-1 alpha on the core protein and the core protein fragments of the small proteoglycan decorin in cartilage. J. Orthop. Res. 10, 276–284. Ziff, M. (1991) Role of the endothelium in chronic inflammatory synovitis. Arth. Rheum. 34, 1345–1351. Citing Literature Volume26, Issue4July 1994Pages 263-277 ReferencesRelatedInformation" @default.
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• W2170991844 cites W1551410107 @default.
• W2170991844 cites W1660900149 @default.
• W2170991844 cites W1772675489 @default.
• W2170991844 cites W1965544173 @default.
• W2170991844 cites W1966334799 @default.
• W2170991844 cites W1972173522 @default.
• W2170991844 cites W1980617741 @default.
• W2170991844 cites W1980978904 @default.
• W2170991844 cites W1984837363 @default.
• W2170991844 cites W1985174304 @default.
• W2170991844 cites W1986022089 @default.
• W2170991844 cites W2002974844 @default.
• W2170991844 cites W2007356946 @default.
• W2170991844 cites W2011234068 @default.
• W2170991844 cites W2017720269 @default.
• W2170991844 cites W2019009662 @default.
• W2170991844 cites W2019650587 @default.
• W2170991844 cites W2021802559 @default.
• W2170991844 cites W2022586945 @default.
• W2170991844 cites W2024863213 @default.
• W2170991844 cites W2038692340 @default.
• W2170991844 cites W2052031545 @default.
• W2170991844 cites W2056406997 @default.
• W2170991844 cites W2063317454 @default.
• W2170991844 cites W2063357735 @default.
• W2170991844 cites W2063946677 @default.
• W2170991844 cites W2073179859 @default.
• W2170991844 cites W2073456348 @default.
• W2170991844 cites W2073645829 @default.
• W2170991844 cites W2074917178 @default.
• W2170991844 cites W2076235892 @default.
• W2170991844 cites W2077555077 @default.
• W2170991844 cites W2080387917 @default.
• W2170991844 cites W2084386397 @default.
• W2170991844 cites W2095359695 @default.
• W2170991844 cites W2102088222 @default.
• W2170991844 cites W2114769400 @default.
• W2170991844 cites W2115645802 @default.
• W2170991844 cites W2120911864 @default.
• W2170991844 cites W2130728604 @default.
• W2170991844 cites W2137468010 @default.
• W2170991844 cites W2138769532 @default.
• W2170991844 cites W2145720435 @default.
• W2170991844 cites W2150602579 @default.
• W2170991844 cites W2153251271 @default.
• W2170991844 cites W2157724807 @default.
• W2170991844 cites W2163684373 @default.
• W2170991844 cites W2185283125 @default.
• W2170991844 cites W2209205153 @default.
• W2170991844 cites W2254579098 @default.
• W2170991844 cites W2317412856 @default.
• W2170991844 cites W2415113118 @default.
• W2170991844 cites W2415881300 @default.
• W2170991844 cites W2439202829 @default.
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