The Oxidative Inactivation of Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) by Hypochlorous Acid (HOCl) is Suppressed by Anti-Rheumatic Drugs

References

• Bigg H. F., Clark I. M., Cawston T. E. Fragments of human fibroblast collagenase: interaction with metalloproteinase inhibitors and substrates. Biochimica et Biophysica Acta 1994; 1208: 157–165
   PubMed Web of Science ®Google Scholar
• Murphy G., Docherty A. J. P., Hembry R. M., Reynolds J. J. Metalloproteinases and tissue damage. British Journal of Rhumatology 1991; 30(suppl l)25–31
   PubMedGoogle Scholar
• Mallya S. K., Mookhiar K. A., Gao Y., Brew K., Diozegi M., Birkedal‐Hansen H., Van Wart H. E. Characterization of 58‐Kilodalton human neutrophile collagenase: Comparison with human fibroblast collagenase. Biochemistry 1990; 29: 10628–10634
   PubMed Web of Science ®Google Scholar
• Oshea M., Willenbrock F., Williamson R. A., Cockett M. I., Freedman R. B., Reynolds J. J., Docherty A. J. P., Murphy G. Site directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases: Importance of the N‐terminal region between cysteine 3 and cystein 13. Biochemistry 1992; 31: 10146–10152
   PubMed Web of Science ®Google Scholar
• Williamson R. A., Bryan J. S., Angal S., Murphy G., Freedman R. B. Structural analysis of tissue inhibitor of metalloproteinases‐1 (TIMP‐1) by tryptic peptide mapping. Biochimica et Biophysica Acta 1993; 1164: 8–16
   PubMedGoogle Scholar
• Denhardt D. T., Feng B., Dylan R. E., Cocuzzi E. T., Malayankar U. M. Tissue inhibitor of metalloproteinases (TIMP, aka EPA): Structure, control of expression and biological functions. Pharmacology and Therapeutics 1993; 59: 329–341
   PubMed Web of Science ®Google Scholar
• Lohmander L. S., Hoerrner L. A., Lark M. W. Metalloproteinases, tissue inhibitor, and proteo‐glycan fragments in knee synovial fluid in human osteoarthritis. Arthritis and Rheumatism 1993; 36: 181–9
   PubMed Web of Science ®Google Scholar
• Birkedal‐Hansen H., Moore W. G. I., Bodden M. K., Windsor L. J., Birkedal‐Hansen B., DeCarlo A., Engler J. Matrix metalloproteinases: A Review. Critical Reviews in Oral Biology and Medicine 1993; 4: 197–250
   PubMedGoogle Scholar
• Weiss S. J. Mechanisms of disease: Tissue destruction by neutrophils. The New England Journal of Medicine 1989; 320: 365–376
   PubMed Web of Science ®Google Scholar
• Laurindo Ieda M. M., Mello suzana B. V., Cossermelli W. Influence of low doses of methotrexate on superoxide anion production by poly‐morphonuclear leukocytes from patients with rheumatoid arthritis. Journal of Rheumatology 1995; 22: 633–8
   PubMed Web of Science ®Google Scholar
• Weiss S. J., Peppin G. J. Collagenolytic metalloenzymes of the human neutrophil. Biochemical Pharmacology 1986; 35: 3189–3197
   PubMed Web of Science ®Google Scholar
• Weiss S. J., Klein R., Slivka A., Wei M. Chlorination of taurine by human neutrophils. Journal of Clinical Investigation 1982; 70: 598–607
   PubMed Web of Science ®Google Scholar
• Zgliczynski J. M., Stelmaszynska T., Domanski J., Ostrowski W. Chloramine as intermediates of oxidation reaction of amino acids by myeloperoxidase. Biochimica et Biophysica Acta 1971; 235: 419–424
   PubMed Web of Science ®Google Scholar
• Grisham M. B., Jefferson M. M., Melton D. F., Thomas E. L. Chlorination of endogenous amines by isolated neutrophiles. Journal of Biological Chemistry 1984; 259: 10404–10412
   PubMed Web of Science ®Google Scholar
• Okada Y., Watanabe S., Nakanish I., Kishi J. I., Hayakawa T., Watorek W., Travis J., Nagase H. Inactivation of tissue inhibitor of metallopro‐teinases by neutrophil elastase and other serine pro‐teinases. FEBS. Letters 1988; 229: 157–160
   Google Scholar
• Davies J. M. S., Horwits D. A., Davies K. J. A. Potential roles of hypochlorous acid and N‐chloroamines in collagen breakdown by phagocytic cells in synovitis. Free Radical Biology & Medicine 1993; 15: 637–643
   PubMed Web of Science ®Google Scholar
• Matheson N. R., Wong P. S., Schuyler M., Travis J. Interaction of human al‐proteinase inhibitor with neutrophile meyloperoxidase. Biochemistry 1981; 20: 331–336
   PubMed Web of Science ®Google Scholar
• Frears E. R., Zhang Z., Blake D. R., O'Connell J. P., Winyard P. G. Inactivation of tissue inhibitor of metalloproteinase‐1 by peroxynitrite. FEBS Letters 1996; 381: 21–24
   PubMed Web of Science ®Google Scholar
• Cuperus R. A., Muijsers A. O., Wever R. Antiarthritic drugs containing thiol groups scavenge hypochlorite and inhibit its formation by myeloperoxidase from human leukocytes. Arthritis and Rheumatism 1985; 28: 1228–1233
   PubMed Web of Science ®Google Scholar
• Pekoe G., Van Dyke K., Mengoli H., Peden D., English D. Comparison of the effects of antioxi‐dant non‐stroidal anti inflammatory drugs against myeloper‐oxidase and hypochlorous acid luminol‐enhanced chemiluminescence. Agents & Actions 1982; 12: 232–238
   PubMedGoogle Scholar
• Matheson N. R. The effect of anti‐arthritic drugs and related compounds on the human neutrophil myeloperoxidase system. Biochemical and Biophysical Research Communications 1982; 108: 159–165
   Web of Science ®Google Scholar
• Bannwart B., Labat L., Moride Y., Schaeverbck T. Methotrexate in rheumatoid arthritis. Drugs 1994; 47: 25–50
   Web of Science ®Google Scholar
• Stevenson G. A., Lyons J. G., Cameron D. A., O'Grady R. L. Rat mammary carcinoma cells in long‐term serum free culture provide a continuing supply of collagenase. Bioscience Report 1985; 5: 1071–1077
   PubMed Web of Science ®Google Scholar
• Netzel‐Arnett S., Mallya S. K., Nagase H., Birkedal‐Hanson H., Van Wart H. E. Continusly recording fluorescent assays optimized for five human matrix metalloproteinases. Analytical Biochemistry 1991; 195: 86–92
   PubMed Web of Science ®Google Scholar
• Test S. T., Weiss S. J. The generation of utilization of chlorinated oxidants by human neutrophils. Free Radical Biology and Medicine 1986; 2: 91–116
   Web of Science ®Google Scholar
• Lark M. W., Saphos C. A., Walakovitz L. A., Moore V. L. In vivo activity of human recombinant tissue inhibitor of metalloproteinases (TIMP). Biochemical Pharmacology 1990; 39: 2041–2049
   PubMed Web of Science ®Google Scholar
• Pace C. N., Shirly B. A., Thompson J. A. Protein structure: a practical approach, T. E. Creighton. IRL Press, Oxford University Press, Oxford, PP311–339
   Google Scholar
• Williamson R. A., Smith B. J., Angal S., Freedman R. B. Chemical modification of tissue inhibitor of metalloproteinases‐1 and its inactivation by diethyl pyro‐carbonate. Biochimica et Biophysica Acta 1993; 1203: 147–154
   PubMedGoogle Scholar
• Stricklin J. P., Hoidal J. R. Oxidant‐mediated inactivation of TIMP. Matrix Supplement 1992; 1: 325
   PubMedGoogle Scholar
• Muijsers A. O., van de Stadt R. J., Henrichs A. M. A., van de Korst J. K. Determination of D‐peni‐cillamine in serum and urine of patients with rheumatoid arthritis. Clinica Chimica Acta 1979; 94: 173–180
   PubMed Web of Science ®Google Scholar
• Van de Stadt R. J., Muijsers A. O., Henrichs A. M. A., van de Korst J. K. D‐penicillamine: biochemical, metabolic, and pharmacological aspects. Scandinavian Journal of Rheumatology 1979, (suppl) 29: 13–20
   Google Scholar
• Hurst N. P., Geojatschko L., Betts W. H., Zalewski P. D., Forbes I. J. Auranofin modulates human neutrophile superoxide production and protein phosphorylation. Rheumatology International 1989; 8: 245–250
   PubMed Web of Science ®Google Scholar
• Jellum E., Munthe E. Fate of the thiomalate part after intramuscular administration of aurothio‐malate in rheumatoid arthritis. Annals of Rheumatic Disease 1982; 41: 431–432
   PubMed Web of Science ®Google Scholar
• Wad M., Halliwell B., Moorehouse C. P., Hutchison D. C., Baum H. Biologically‐significant scavenging of the myeloperoxidase‐derived oxidant hypochlorous acid by some anti‐inflammatory drugs. Biochemical Pharmacology 1987; 36(22)3847–3850
   PubMed Web of Science ®Google Scholar