{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T16:09:55Z","timestamp":1761581395424},"reference-count":34,"publisher":"Japanese Society of Veterinary Science","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Veterinary Medical Science","J. Vet. Med. Sci."],"published-print":{"date-parts":[[2016]]},"DOI":"10.1292\/jvms.15-0711","type":"journal-article","created":{"date-parts":[[2016,2,22]],"date-time":"2016-02-22T02:46:52Z","timestamp":1456109212000},"page":"1051-1054","source":"Crossref","is-referenced-by-count":5,"title":["Synovial fluid matrix metalloproteinase-2 and -9 activities in dogs suffering from joint disorders"],"prefix":"10.1292","volume":"78","author":[{"given":"Kohei","family":"MURAKAMI","sequence":"first","affiliation":[{"name":"Department of Veterinary Clinical Pathobiology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1\u20131\u20131 Yayoi, Bunkyo-ku, Tokyo 113\u20138657, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shingo","family":"MAEDA","sequence":"additional","affiliation":[{"name":"Department of Veterinary Clinical Pathobiology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1\u20131\u20131 Yayoi, Bunkyo-ku, Tokyo 113\u20138657, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomohiro","family":"YONEZAWA","sequence":"additional","affiliation":[{"name":"Department of Veterinary Clinical Pathobiology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1\u20131\u20131 Yayoi, Bunkyo-ku, Tokyo 113\u20138657, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoaki","family":"MATSUKI","sequence":"additional","affiliation":[{"name":"Department of Veterinary Clinical Pathobiology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1\u20131\u20131 Yayoi, Bunkyo-ku, Tokyo 113\u20138657, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"122","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1. Ahrens, D., Koch, A. E., Pope, R. M., Stein-Picarella, M. and Niedbala, M. J. 1996. Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis. <i>Arthritis Rheum.<\/i> 39: 1576\u20131587.","DOI":"10.1002\/art.1780390919"},{"key":"2","doi-asserted-by":"crossref","unstructured":"3. Boland, L., Danger, R., Cabon, Q., Rabillard, M., Brouard, S., Bouvy, B. and Gauthier, O. 2014. MMP-2 as an early synovial biomarker for cranial cruciate ligament disease in dogs. <i>Vet. Comp. Orthop. Traumatol.<\/i> 27: 210\u2013215.","DOI":"10.3415\/VCOT-13-06-0082"},{"key":"3","doi-asserted-by":"crossref","unstructured":"4. Charni-Ben Tabassi, N., Desmarais, S., Bay-Jensen, A. C., Delaiss\u00e9, J. M., Percival, M. D. and Garnero, P. 2008. The type II collagen fragments Helix-II and CTX-II reveal different enzymatic pathways of human cartilage collagen degradation. <i>Osteoarthritis Cartilage<\/i> 16: 1183\u20131191.","DOI":"10.1016\/j.joca.2008.02.008"},{"key":"4","doi-asserted-by":"crossref","unstructured":"5. Coughlan, A. R., Robertson, D. H., Bennett, D., May, C., Beynon, R. J. and Carter, S. D. 1998. Matrix metalloproteinases 2 and 9 in canine rheumatoid arthritis. <i>Vet. Rec.<\/i> 143: 219\u2013223.","DOI":"10.1136\/vr.143.8.219"},{"key":"5","doi-asserted-by":"crossref","unstructured":"6. Fujita, Y., Hara, Y., Nezu, Y., Schulz, K. S. and Tagawa, M. 2006. Proinflammatory cytokine activities, matrix metalloproteinase-3 activity, and sulfated glycosaminoglycan content in synovial fluid of dogs with naturally acquired cranial cruciate ligament rupture. <i>Vet. Surg.<\/i> 35: 369\u2013376.","DOI":"10.1111\/j.1532-950X.2006.00159.x"},{"key":"6","doi-asserted-by":"crossref","unstructured":"7. Galloway, R. H. and Lester, S. J. 1995. Histopathological evaluation of canine stifle joint synovial membrane collected at the time of repair of cranial cruciate ligament rupture. <i>J. Am. Anim. Hosp. Assoc.<\/i> 31: 289\u2013294.","DOI":"10.5326\/15473317-31-4-289"},{"key":"7","doi-asserted-by":"crossref","unstructured":"8. Grillet, B., Dequeker, J., Paemen, L., Van Damme, B. and Opdenakker, G. 1997. Gelatinase B in chronic synovitis: immunolocalization with a monoclonal antibody. <i>Br. J. Rheumatol.<\/i> 36: 744\u2013747.","DOI":"10.1093\/rheumatology\/36.7.744"},{"key":"8","doi-asserted-by":"crossref","unstructured":"9. Gruber, B. L., Sorbi, D., French, D. L., Marchese, M. J., Nuovo, G. J., Kew, R. R. and Arbeit, L. A. 1996. Markedly elevated serum MMP-9 (gelatinase B) levels in rheumatoid arthritis: a potentially useful laboratory marker. <i>Clin. Immunol. Immunopathol.<\/i> 78: 161\u2013171.","DOI":"10.1006\/clin.1996.0025"},{"key":"9","doi-asserted-by":"crossref","unstructured":"10. Hegemann, N., Wondimu, A., Kohn, B., Brunnberg, L. and Schmidt, M. F. 2005. Cytokine profile in canine immune-mediated polyarthritis and osteoarthritis. <i>Vet. Comp. Orthop. Traumatol.<\/i> 18: 67\u201372.","DOI":"10.1055\/s-0038-1632931"},{"key":"10","doi-asserted-by":"crossref","unstructured":"11. Hembry, R. M., Bagga, M. R., Reynolds, J. J. and Hamblen, D. L. 1995. Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis. <i>Ann. Rheum. Dis.<\/i> 54: 25\u201332.","DOI":"10.1136\/ard.54.1.25"},{"key":"11","doi-asserted-by":"crossref","unstructured":"12. Hewicker-Trautwein, M., Carter, S. D., Bennett, D. and Kelly, D. F. 1999. Immunocytochemical demonstration of lymphocyte subsets and MHC class II antigen expression in synovial membranes from dogs with rheumatoid arthritis and degenerative joint disease. <i>Vet. Immunol. Immunopathol.<\/i> 67: 341\u2013357.","DOI":"10.1016\/S0165-2427(98)00229-3"},{"key":"12","doi-asserted-by":"crossref","unstructured":"13. Ito, A., Mukaiyama, A., Itoh, Y., Nagase, H., Thogersen, I. B., Enghild, J. J., Sasaguri, Y. and Mori, Y. 1996. Degradation of interleukin 1beta by matrix metalloproteinases. <i>J. Biol. Chem.<\/i> 271: 14657\u201314660.","DOI":"10.1074\/jbc.271.25.14657"},{"key":"13","doi-asserted-by":"crossref","unstructured":"14. Itoh, T., Matsuda, H., Tanioka, M., Kuwabara, K., Itohara, S. and Suzuki, R. 2002. The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. <i>J. Immunol.<\/i> 169: 2643\u20132647.","DOI":"10.4049\/jimmunol.169.5.2643"},{"key":"14","doi-asserted-by":"crossref","unstructured":"15. Konttinen, Y. T., Ainola, M., Valleala, H., Ma, J., Ida, H., Mandelin, J., Kinne, R. W., Santavirta, S., Sorsa, T., L\u00f3pez-Ot\u00edn, C. and Takagi, M. 1999. Analysis of 16 different matrix metalloproteinases (MMP-1 to MMP-20) in the synovial membrane: different profiles in trauma and rheumatoid arthritis. <i>Ann. Rheum. Dis.<\/i> 58: 691\u2013697.","DOI":"10.1136\/ard.58.11.691"},{"key":"15","unstructured":"16. Koolwijk, P., Miltenburg, A. M., van Erck, M. G., Oudshoorn, M., Niedbala, M. J., Breedveld, F. C. and van Hinsbergh, V. W. 1995. Activated gelatinase-B (MMP-9) and urokinase-type plasminogen activator in synovial fluids of patients with arthritis. Correlation with clinical and experimental variables of inflammation. <i>J. Rheumatol.<\/i> 22: 385\u2013393."},{"key":"16","doi-asserted-by":"crossref","unstructured":"17. McQuibban, G. A., Butler, G. S., Gong, J. H., Bendall, L., Power, C., Clark-Lewis, I. and Overall, C. M. 2001. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. <i>J. Biol. Chem.<\/i> 276: 43503\u201343508.","DOI":"10.1074\/jbc.M107736200"},{"key":"17","doi-asserted-by":"crossref","unstructured":"18. McQuibban, G. A., Gong, J. H., Wong, J. P., Wallace, J. L., Clark-Lewis, I. and Overall, C. M. 2002. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties <i>in vivo<\/i>. <i>Blood<\/i> 100: 1160\u20131167.","DOI":"10.1182\/blood.V100.4.1160.h81602001160_1160_1167"},{"key":"18","doi-asserted-by":"crossref","unstructured":"19. Mizui, T., Ishimaru, J., Miyamoto, K. and Kurita, K. 2001. Matrix metalloproteinase-2 in synovial lavage fluid of patients with disorders of the temporomandibular joint. <i>Br. J. Oral Maxillofac. Surg.<\/i> 39: 310\u2013314.","DOI":"10.1054\/bjom.2001.0634"},{"key":"19","doi-asserted-by":"crossref","unstructured":"20. Muir, P., Danova, N. A., Argyle, D. J., Manley, P. A. and Hao, Z. 2005. Collagenolytic protease expression in cranial cruciate ligament and stifle synovial fluid in dogs with cranial cruciate ligament rupture. <i>Vet. Surg.<\/i> 34: 482\u2013490.","DOI":"10.1111\/j.1532-950X.2005.00073.x"},{"key":"20","doi-asserted-by":"crossref","unstructured":"21. Muir, P., Schaefer, S. L., Manley, P. A., Svaren, J. P., Oldenhoff, W. E. and Hao, Z. 2007. Expression of immune response genes in the stifle joint of dogs with oligoarthritis and degenerative cranial cruciate ligament rupture. <i>Vet. Immunol. Immunopathol.<\/i> 119: 214\u2013221.","DOI":"10.1016\/j.vetimm.2007.05.016"},{"key":"21","doi-asserted-by":"crossref","unstructured":"22. Murakami, K., Yonezawa, T. and Matsuki, N. 2016. Synovial fluid total protein concentration as a possible marker for canine idiopathic polyarthritis. <i>J. Vet. Med. Sci.<\/i> 77: 1715\u20131717.","DOI":"10.1292\/jvms.15-0263"},{"key":"22","doi-asserted-by":"crossref","unstructured":"23. Nagase, H., Visse, R. and Murphy, G. 2006. Structure and function of matrix metalloproteinases and TIMPs. <i>Cardiovasc. Res.<\/i> 69: 562\u2013573.","DOI":"10.1016\/j.cardiores.2005.12.002"},{"key":"23","doi-asserted-by":"crossref","unstructured":"24. Parks, W. C., Wilson, C. L. and L\u00f3pez-Boado, Y. S. 2004. Matrix metalloproteinases as modulators of inflammation and innate immunity. <i>Nat. Rev. Immunol.<\/i> 4: 617\u2013629.","DOI":"10.1038\/nri1418"},{"key":"24","doi-asserted-by":"crossref","unstructured":"25. Peake, N. J., Foster, H. E., Khawaja, K., Cawston, T. E. and Rowan, A. D. 2006. Assessment of the clinical significance of gelatinase activity in patients with juvenile idiopathic arthritis using quantitative protein substrate zymography. <i>Ann. Rheum. Dis.<\/i> 65: 501\u2013507.","DOI":"10.1136\/ard.2005.039032"},{"key":"25","doi-asserted-by":"crossref","unstructured":"26. Rabillard, M., Danger, R., Doran, I. P., Niebauer, G. W., Brouard, S. and Gauthier, O. 2012. Matrix metalloproteinase activity in stifle synovial fluid of cranial cruciate ligament deficient dogs and effect of postoperative doxycycline treatment. <i>Vet. J.<\/i> 193: 271\u2013273.","DOI":"10.1016\/j.tvjl.2011.10.028"},{"key":"26","unstructured":"27. Ries, C. and Petrides, P. E. 1995. Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease. <i>Biol. Chem. Hoppe Seyler<\/i> 376: 345\u2013355."},{"key":"27","doi-asserted-by":"crossref","unstructured":"28. Sch\u00f6nbeck, U., Mach, F. and Libby, P. 1998. Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing. <i>J. Immunol.<\/i> 161: 3340\u20133346.","DOI":"10.4049\/jimmunol.161.7.3340"},{"key":"28","doi-asserted-by":"crossref","unstructured":"29. Springman, E. B., Angleton, E. L., Birkedal-Hansen, H. and Van Wart, H. E. 1990. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a \u201ccysteine switch\u201d mechanism for activation. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i> 87: 364\u2013368.","DOI":"10.1073\/pnas.87.1.364"},{"key":"29","doi-asserted-by":"crossref","unstructured":"30. Tamamoto, T., Ohno, K., Takahashi, M., Fukushima, K., Kanemoto, H., Fujino, Y. and Tsujimoto, H. 2014. Plasma matrix metalloproteinase-9 activity in cats with lymphoma. <i>Vet. Comp. Oncol.<\/i>","DOI":"10.1111\/vco.12097"},{"key":"30","unstructured":"31. Van den Steen, P. E., Proost, P., Wuyts, A., Van Damme, J. and Opdenakker, G. 2000. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. <i>Blood<\/i> 96: 2673\u20132681."},{"key":"31","doi-asserted-by":"crossref","unstructured":"32. Van Den Steen, P. E., Wuyts, A., Husson, S. J., Proost, P., Van Damme, J. and Opdenakker, G. 2003. Gelatinase B\/MMP-9 and neutrophil collagenase\/MMP-8 process the chemokines human GCP-2\/CXCL6, ENA-78\/CXCL5 and mouse GCP-2\/LIX and modulate their physiological activities. <i>Eur. J. Biochem.<\/i> 270: 3739\u20133749.","DOI":"10.1046\/j.1432-1033.2003.03760.x"},{"key":"32","doi-asserted-by":"crossref","unstructured":"33. Van den Steen, P. E., Grillet, B. and Opdenakker, G. 2005. Gelatinase B participates in collagen II degradation and releases glycosylated remnant epitopes in rheumatoid arthritis. <i>Adv. Exp. Med. Biol.<\/i> 564: 45\u201355.","DOI":"10.1007\/0-387-25515-X_10"},{"key":"33","doi-asserted-by":"crossref","unstructured":"34. Xue, M., McKelvey, K., Shen, K., Minhas, N., March, L., Park, S. Y. and Jackson, C. J. 2014. Endogenous MMP-9 and not MMP-2 promotes rheumatoid synovial fibroblast survival, inflammation and cartilage degradation. <i>Rheumatology (Oxford)<\/i> 53: 2270\u20132279.","DOI":"10.1093\/rheumatology\/keu254"},{"key":"34","doi-asserted-by":"crossref","unstructured":"35. Yu, Q. and Stamenkovic, I. 2000. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. <i>Genes Dev.<\/i> 14: 163\u2013176.","DOI":"10.1101\/gad.14.2.163"}],"container-title":["Journal of Veterinary Medical Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jvms\/78\/6\/78_15-0711\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,8,16]],"date-time":"2023-08-16T23:46:06Z","timestamp":1692229566000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jvms\/78\/6\/78_15-0711\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016]]},"references-count":34,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2016]]}},"URL":"https:\/\/doi.org\/10.1292\/jvms.15-0711","relation":{},"ISSN":["0916-7250","1347-7439"],"issn-type":[{"value":"0916-7250","type":"print"},{"value":"1347-7439","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016]]}}}