• 1.

    Bertone AL. Infectious arthritis. In: McIlwraight CW, Trotter GW, eds. Joint disease in the horse. Philadelphia: WB Saunders Co, 1996;397409.

    • Search Google Scholar
    • Export Citation
  • 2.

    Nagase H, Woessner J. Jr. Matrix metalloproteinases. J Biol Chem 1999;274:2149121494.

  • 3.

    Cawston TE, Weaver L, Coughlan RJ, et al. Synovial fluids from infected joints contain active metalloproteinases and no inhibitory activity. Br J Rheumatol 1989;28:386392.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 4.

    Koolwijk P, Miltenburg AM, van Erc MG, et al. 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. J Rheumatol 1995;22:385393.

    • Search Google Scholar
    • Export Citation
  • 5.

    Coughlan AR, Robertson DH, Bennett D, et al. Matrix metalloproteinases 2 and 9 in canine rheumatoid arthritis. Vet Rec 1998;143:219223.

  • 6.

    Clegg PD, Coughlan AR, Riggs CM, et al. Matrix metalloproteinases 2 and 9 in equine synovial fluids. Equine Vet J 1997;29:343348.

  • 7.

    Arican M, Coughlan AR, Clegg PD, et al. Matrix metalloproteinases 2 and 9 activity in bovine synovial fluids. J Vet Med A Physiol Pathol Clin Med 2000;47:449456.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 8.

    Mengshol JA, Mix KS, Brinckerhoff CE. Matrix metalloproteinases as therapeutic targets in arthritic diseases: bull's-eye or missing the mark? Arthritis Rheum 2002;46:1320.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 9.

    Murphy G, Docherty AJ. The matrix metalloproteinases and their inhibitors. Am J Respir Cell Mol Biol 1992;7:120125.

  • 10.

    Goldberg GI, Strongin A, Collier IE, et al. Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J Biol Chem 1992;267:45834591.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 11.

    Woessner JF Jr. Matrix metalloproteinase inhibition. From the Jurassic to the third millennium. Ann N Y Acad Sci 1999;878:388403.

  • 12.

    Francoz D, Desrochers A, Fecteau G, et al. Synovial fluid changes in induced infectious arthritis in calves. J Vet Intern Med 2005;19:336343.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 13.

    Francoz D, Desrochers A, Latouche JS. Effect of repeated arthrocentesis and single joint lavage on cytologic evaluation of synovial fluid in 5 young calves. Can J Vet Res 2007;71:129134.

    • Search Google Scholar
    • Export Citation
  • 14.

    Esteve PO, Tremblay P, Houde M, et al. In vitro expression of MMP-2 and MMP-9 in glioma cells following exposure to inflammatory mediators. Biochim Biophys Acta 1998;1403:8596.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 15.

    Lakritz J, Marsh AE, Cockrell M, et al. Characterization of gelatinases in bronchoalveolar lavage fluid and gelatinases produced by alveolar macrophages isolated from healthy calves. Am J Vet Res 2004;65:163172.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 16.

    Simonen-Jokinen TL, Eskelinen UM, Härtel HM, et al. Gelatinolytic matrix metalloproteinases-2 and -9 in tracheobronchial lavage fluid obtained from calves with concurrent infections of Pasteurella multocida and Mycoplasma bovirhinis. Am J Vet Res 2005;66:21012106.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 17.

    Clegg PD, Burke RM, Coughlan AR, et al. Characterisation of equine matrix metalloproteinase 2 and 9; and identification of the cellular sources of these enzymes in joints. Equine Vet J 1997;29:335342.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 18.

    Hibbs MS, Hasty KA, Seyer JM, et al. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Biol Chem 1985;260:24932500.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 19.

    Makowski GS, Ramsby ML. Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: correlation to polymorphonuclear leukocyte infiltration and in response to infection. Clin Chim Acta 2003;329:7781.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 20.

    Lu KH, Yang SF, Chu SC, et al. The significance of altered gelatinase expression in the synovium of patient with arthritic effusions. Clin Rheumatol 2004;23:2126.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 21.

    Calander AM, Starckx S, Opdenakker G, et al. Matrix metalloproteinase-9 (gelatinase B) deficiency leads to increased severity of Staphylococcus aureus-triggered septic arthritis. Microbes Infect 2006;8:14341439.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 22.

    Jouglin M, Robert C, Valette JP, et al. Metalloproteinases and tumor necrosis factor-alpha activities in synovial fluids of horses: correlation with articular cartilage alterations. Vet Res 2000;31:507515.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 23.

    Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem 1997;378:151160.

  • 24.

    Xue M, March L, Sambrook PN, et al. Differential regulation of matrix metalloproteinase 2 and matrix metalloproteinase 9 by activated protein C. Arthritis Rheum 2007;56:28642874.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 25.

    Kouwenhoven M, Carlström C, Özenci V, et al. Matrix metalloproteinase and cytokine profiles in monocytes over the course of stroke. J Clin Immunol 2001;21:365375.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 26.

    Ries C, Loher F, Zang C, et al. Matrix metalloproteinase production by bone marrow mononuclear cells from normal individuals and patients with acute and chronic myeloid leukemia or myelodysplastic syndromes. Clin Cancer Res 1999;5:11151124.

    • Search Google Scholar
    • Export Citation
  • 27.

    Abraham M, Shapiro S, Lahat N, et al. The role of IL-18 and IL-12 in the modulation of matrix metalloproteinases and their tissue inhibitors in monocytic cells. Int Immunol 2002;14:14491457.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 28.

    Lee EO, Kang JL, Chong YH. The amyloid-B peptide suppress transforming growth factor-B1-induced matrix metalloproteinase-2 production via Smad7 expression in human monocytic THP-1 cells. J Biol Chem 2005;280:78457853.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 29.

    Jansen PL, Kever M, Rosch R, et al. Polymeric meshes induce zonal regulation of matrix metalloproteinase-2 gene expression by macrophages and fibroblasts. FASEB J 2007;21:10471057.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 30.

    Brama PA, van de Boom R, DeGroott J, et al. Collagenase-1 (MMP-1) activity in equine synovial fluid: influence of age, joint pathology, exercise and repeated arthrocentesis. Equine Vet J 2004;36:3440.

    • Search Google Scholar
    • Export Citation
  • 31.

    Lohmander LS, Dahlberg L, Eyre D, et al. Longitudinal and cross-sectional variability in markers of joint metabolism in patients with knee pain and articular cartilage abnormalities. Osteoarthritis Cartilage 1998;6:351361.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 32.

    van den Boom R, Brama PA, Kiers GH, et al. The influence of repeated arthrocentesis and exercise on matrix metalloproteinase and tumour necrosis factor alpha activities in normal equine joints. Equine Vet J 2004;36:155159.

    • Search Google Scholar
    • Export Citation
  • 33.

    Manicourt DH, Fujimoto N, Obata K, et al. Serum levels of collagenase, stromelysin-1, and TIMP-1. Age- and sex-related differences in normal subjects and relationship to the extent of joint involvement and serum levels of antigenic keratan sulfate in patients with osteoarthritis. Arthritis Rheum 1994;37:17741783.

    • Search Google Scholar
    • Export Citation
  • 34.

    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 Rheum 2001;44:14551465.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 35.

    Brama PA, TeKoppele JM, Beekman B, et al. Matrix metalloproteinase activity in equine synovial fluid: influence of age, osteoarthritis, and osteochondrosis. Ann Rheum Dis 1998;57:697699.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 36.

    Santavirta S, Takagi M, Konttinen YT, et al. Inhibitory effect of cephalotin on matrix metalloproteinase activity around loose hip prostheses. Antimicrob Agents Chemother 1996;40:244246.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 37.

    Cainelli G, Galletti P, Garbisa S, et al. 4-alkylidene-azetidin-2-ones: novel inhibitors of leukocyte elastase and gelatinase. Bioorg Med Chem 2003;11:53915399.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • 38.

    Itoh T, Matsuda H, Tanioka M, et al. The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J Immunol 2002;169:26432647.

    • Crossref
    • Search Google Scholar
    • Export Citation

Advertisement

Relative expression of matrix metalloproteinase-2 and -9 in synovial fluid from healthy calves and calves with experimentally induced septic arthritis

View More View Less
  • 1 Département des Sciences Cliniques, Faculté de Médecine Vétérinaire, Université de Montréal, CP 5000, St-Hyacinthe, QC J2S 7C6, Canada.
  • | 2 Département des Sciences Cliniques, Faculté de Médecine Vétérinaire, Université de Montréal, CP 5000, St-Hyacinthe, QC J2S 7C6, Canada.
  • | 3 INRS-Institut Armand-Frappier, 531 Boul des Prairies, Laval, QC H7V 1B7, Canada.
  • | 4 INRS-Institut Armand-Frappier, 531 Boul des Prairies, Laval, QC H7V 1B7, Canada.
  • | 5 Département des Sciences Cliniques, Faculté de Médecine Vétérinaire, Université de Montréal, CP 5000, St-Hyacinthe, QC J2S 7C6, Canada.
  • | 6 Département de Pathologie et Microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, CP 5000, St-Hyacinthe, QC J2S 7C6, Canada.
  • | 7 Département de Pathologie et Microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, CP 5000, St-Hyacinthe, QC J2S 7C6, Canada.

Abstract

Objective—To identify changes over time in relative expression of matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) in synovial fluid from healthy calves and calves with experimentally induced septic arthritis.

Animals—12 Holstein calves.

Procedures—In 7 calves, Escherichia coli was injected in the right tarsal joint on day 1. Joint lavage was performed on day 2, and calves were treated with ceftiofur from days 2 through 21. Synovial fluid samples were collected on days 1 (before inoculation), 2 (before joint lavage), 3, 4, 8, 12, 16, 20, and 24. In the remaining 5 calves, joint lavage was performed on day 2 and synovial fluid samples were collected from the left tarsal joint. Relative expression of MMP-2 and MMP-9 was determined by means of gel zymography.

Results—On day 1, MMP-2 was detected in all synovial fluid samples but MMP-9 was not detected. In calves with septic arthritis, values for relative expression of MMP-9 monomer and dimer were significantly increased on days 2 through 20 and days 2 through 24, respectively, and relative expression of MMP-2 was significantly increased on days 3 through 20. There were significant linear associations between relative expression of the monomer and dimer forms of MMP-9 and between neutrophil count and relative expression of the MMP-9 monomer and dimer forms.

Conclusions and Clinical Relevance—Results indicated that relative expression of MMP-9 and MMP-2 increased in synovial fluid from calves with experimentally induced septic arthritis, with relative expression remaining high for several days after infection.

Abstract

Objective—To identify changes over time in relative expression of matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) in synovial fluid from healthy calves and calves with experimentally induced septic arthritis.

Animals—12 Holstein calves.

Procedures—In 7 calves, Escherichia coli was injected in the right tarsal joint on day 1. Joint lavage was performed on day 2, and calves were treated with ceftiofur from days 2 through 21. Synovial fluid samples were collected on days 1 (before inoculation), 2 (before joint lavage), 3, 4, 8, 12, 16, 20, and 24. In the remaining 5 calves, joint lavage was performed on day 2 and synovial fluid samples were collected from the left tarsal joint. Relative expression of MMP-2 and MMP-9 was determined by means of gel zymography.

Results—On day 1, MMP-2 was detected in all synovial fluid samples but MMP-9 was not detected. In calves with septic arthritis, values for relative expression of MMP-9 monomer and dimer were significantly increased on days 2 through 20 and days 2 through 24, respectively, and relative expression of MMP-2 was significantly increased on days 3 through 20. There were significant linear associations between relative expression of the monomer and dimer forms of MMP-9 and between neutrophil count and relative expression of the MMP-9 monomer and dimer forms.

Conclusions and Clinical Relevance—Results indicated that relative expression of MMP-9 and MMP-2 increased in synovial fluid from calves with experimentally induced septic arthritis, with relative expression remaining high for several days after infection.

Contributor Notes

Dr. Latouche's present address is Veterinary Diagnostic Imaging & Cytopathology, 16900 SE 82nd Dr, Clackamas, OR 97023.

Dr. Fortin's present address is Laboratoire d'épidémiosurveillance animale du Québec, 3220 rue Sicotte, St-Hyacinthe, QC J2S 7X9, Canada.

Dr. Simard's present address is University Heath Network, Princess Margaret Hospital, 610 University Ave, Toronto, ON, M5G 2M9, Canada.

Supported by Le Fonds du Centenaire de l'Université de Montréal and a studentship from the Canadian Arthritis Network. Dr. Saint Pierre was supported by the Fonds de la Recherche en Santé du Québec.

The authors thank Guy Beauchamp for assistance with statistical analyses and Edouard F. Potworowski for critical reading of the manuscript.

Address correspondence to Dr. Francoz.