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Research Article

Definition of peptide inhibitors from a synthetic peptide library by targeting gelatinase B/matrix metalloproteinase-9 (MMP-9) and TNF-α converting enzyme (TACE/ADAM-17)

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Pages 533-540 | Received 25 Nov 2010, Accepted 20 Jun 2011, Published online: 10 Aug 2011

References

  • Barrett AJ, Rawlings ND, Woessner JF. Handbook of Proteolytic enzymes. London: Academic Press, 2003.
  • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001;17:463–516.
  • Overall CM, López-Otín C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2002;2:657–672.
  • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990;87:5578–5582.
  • Van den Steen PE, Dubois B, Nelissen I, Rudd PM, Dwek RA, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 2002;37:375–536.
  • Van den Steen PE, Proost P, Grillet B, Brand DD, Kang AH, Van Damme J et al. Cleavage of denatured natural collagen type II by neutrophil gelatinase B reveals enzyme specificity, post-translational modifications in the substrate, and the formation of remnant epitopes in rheumatoid arthritis. Faseb J 2002;16:379–389.
  • Itoh T, Matsuda H, Tanioka M, Kuwabara K, Itohara S, Suzuki R. The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J Immunol 2002;169:2643–2647.
  • Van den Steen PE, Proost P, Wuyts A, Van Damme J, Opdenakker G. 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. Blood 2000;96:2673–2681.
  • Liu Z, Zhou X, Shapiro SD, Shipley JM, Twining SS, Diaz LA et al. The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 2000;102:647–655.
  • Cauwe B, Van den Steen PE, Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol 2007;42:113–185.
  • Hu J, Van den Steen PE, Sang QX, Opdenakker G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat Rev Drug Discov 2007;6:480–498.
  • Hu J, Fiten P, Van den Steen PE, Chaltin P, Opdenakker G. Simulation of evolution-selected propeptide by high-throughput selection of a peptidomimetic inhibitor on a capillary DNA sequencer platform. Anal Chem 2005;77:2116–2124.
  • Parrillo JE. Pathogenetic mechanisms of septic shock. N Engl J Med 1993;328:1471–1477.
  • Beutler B. Toll-like receptors: how they work and what they do. Curr Opin Hematol 2002;9:2–10.
  • Weiss SJ. Tissue destruction by neutrophils. N Engl J Med 1989;320:365–376.
  • Masure S, Proost P, Van Damme J, Opdenakker G. Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8. Eur J Biochem 1991;198:391–398.
  • Van den Steen PE, Van Aelst I, Hvidberg V, Piccard H, Fiten P, Jacobsen C et al. The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors. J Biol Chem 2006;281:18626–18637.
  • Whittaker M, Floyd CD, Brown P, Gearing AJ. Design and therapeutic application of matrix metalloproteinase inhibitors. Chem Rev 1999;99:2735–2776.
  • Hu J, Dubois V, Chaltin P, Fiten P, Dillen C, Van den Steen PE et al. Inhibition of lethal endotoxin shock with an L-pyridylalanine containing metalloproteinase inhibitor selected by high-throughput screening of a new peptide library. Comb Chem High Throughput Screen 2006;9:599–611.
  • Konings DA, Wyatt JR, Ecker DJ, Freier SM. Strategies for rapid deconvolution of combinational libraries: comparative evaluation using a model system. J Med Chem 1997;40:4386–4395.
  • Knight CG, Willenbrock F, Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett 1992;296:263–266.
  • Hu J, Van den Steen PE, Dillen C, Opdenakker G. Targeting neutrophil collagenase/matrix metalloproteinase-8 and gelatinase B/matrix metalloproteinase-9 with a peptidomimetic inhibitor protects against endotoxin shock. Biochem Pharmacol 2005;70:535–544.
  • Solorzano CC, Ksontini R, Pruitt JH, Auffenberg T, Tannahill C, Galardy RE et al. A matrix metalloproteinase inhibitor prevents processing of tumor necrosis factor alpha (TNF alpha) and abrogates endotoxin-induced lethality. Shock 1997;7:427–431.
  • Koivunen E, Arap W, Valtanen H, Rainisalo A, Medina OP, Heikkilä P et al. Tumor targeting with a selective gelatinase inhibitor. Nat Biotechnol 1999;17:768–774.
  • Kridel SJ, Chen E, Kotra LP, Howard EW, Mobashery S, Smith JW. Substrate hydrolysis by matrix metalloproteinase-9. J Biol Chem 2001;276:20572–20578.
  • McGeehan GM, Bickett DM, Green M, Kassel D, Wiseman JS, Berman J. Characterization of the peptide substrate specificities of interstitial collagenase and 92-kDa gelatinase. Implications for substrate optimization. J Biol Chem 1994;269:32814–32820.
  • Xu HM, Yin R, Chen L, Siraj S, Huang X, Wang M et al. An RGD-modified endostatin-derived synthetic peptide shows antitumor activity in vivo. Bioconjug Chem 2008;19:1980–1986.
  • Yin R, Zheng H, Xi T, Xu HM. Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide. Bioconjug Chem 2010;21:1142–1147.

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