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Biochemistry & Molecular Biology

Effects of heparin and cholesterol sulfate on the activity and stability of human matrix metalloproteinase 7

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Pages 41-48 | Received 15 Mar 2013, Accepted 21 Oct 2013, Published online: 16 Apr 2014

References

  • Woessner JF Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 1991;5:2145–2154.
  • Matrisian LM. The matrix degrading metalloproteinases. BioEssays. 1992;14:455–463.
  • Nagase H, Woessner JF Jr. Matrix metalloproteinases. J. Biol. Chem. 1999;274:21491–21494.
  • Woessner JF Jr, Taplin CJ. Purification and properties of a small latent matrix metallo-proteinase of the rat uterus. J. Biol. Chem. 1988;263:16918–16925.
  • Browner MF, Smith WW, Castelhano AL. Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry. 1995;34:6602–6610.
  • Pajouh MS, Nagle RB, Breathnach R, Finch JS, Brawer MK, Bowden GT. Expression of metalloproteinase genes in human prostate cancer. J. Cancer Res. Clin. Oncol. 1991;117:144–150.
  • Yoshimoto M, Itoh F, Yamamoto H, Hinoda Y, Imai K, Yachi A. Expression of MMP-7 (PUMP-1) mRNA in human colorectal cancers. Int. J. Cancer. 1993;54:614–618.
  • Nakano A, Tani E, Miyazaki K, Yamamoto Y, Furuyama J. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human gliomas. J. Neurosurg. 1995;83:298–307.
  • Adachi Y, Itoh F, Yamamoto H, Matsuno K, Arimura Y, Kusano M, Endo T, Hinoda Y, Oohara M, Hosokawa M, Imai K. Matrix metalloproteinase matrilysin (MMP-7) participates in the progression of human gastric and esophageal cancers. Int. J. Oncol. 1998;13:1031–1035.
  • Muller D, Breathnach R, Engelmann A, Millon R, Bronner G, Flesch H, Dumont P, Eber M, Abecassis J. Expression of collagenase-related metalloproteinase genes in human lung or head and neck tumours. Int. J. Cancer. 1991;48:550–556.
  • Happner kJ, Matrisian LM, Jensen RA, Rodgers WH. Expression of most matrix metalloproteinase family members in breast cancer represents a tumour-induced host response. Am. J. Pathol. 1996;149:273–282.
  • Muta Y, Oneda H, Inouye K. Inhibitory effects of alcohols on the activity of human matrix metalloproteinase 7 (matrilysin). Biosci. Biotechnol. Biochem. 2004;68:2649–2652.
  • Oneda H, Inouye K. Interactions of human matrix metalloproteinase 7 (matrilysin) with the inhibitors thiorphan and R-94138. J. Biochem. 2001;129:429–435.
  • Muta Y, Oyama S, Umezawa T, Shimada M, Inouye K. Inhibitory effects of lignans on the activity of human matrix metalloproteinase 7 (matrilysin). J. Agric. Food Chem. 2004;52:5888–5894.
  • Oneda H, Shiihara M, Inouye K. Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (matrilysin). J. Biochem. 2003;133:571–576.
  • Miyake T, Yasukawa K, Inouye K. Analysis of the mechanism of inhibition of human matrix metalloproteinase 7 (MMP-7) activity by green tea catechins. Biosci. Biotechnol. Biochem. 2011;75:1564–1569.
  • Samukange V, Yasukawa K, Inouye K. Interaction of 8-anilinonaphthalene 1-sulphonate (ANS) and human matrix metalloproteinase 7 (MMP-7) as examined by MMP-7 activity and ANS fluorescence. J. Biochem. 2012;151:533–540.
  • Muta Y, Oneda H, Inouye K. Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues. Biochem. J. 2005;386:263–270.
  • Muta Y, Inouye K. Tyr219 of human matrix metalloproteinase 7 (MMP-7) is not critical for catalytic activity, but is involved in the broad pH-dependence of the activity. J. Biochem. 2011;150:183–188.
  • Takeharu H, Yasukawa K, Inouye K. Thermodynamic analysis of ionizable groups involved in the catalytic mechanism of human matrix metalloproteinase 7 (MMP-7). Biochim. Biophys. Acta. 2011;1814:1940–1946.
  • Morishima A, Yasukawa K, Inouye K. A possibility of a protein-bound water molecule as the ionizable group responsible for pKe at the alkaline side in human matrix metalloproteinase 7 activity. J. Biochem. 2012;151:501–509.
  • Yu WH, Woessner JF Jr. Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J. Biol. Chem. 2000;275:4183–4191.
  • Yu WH, Woessner JF Jr. Heparin-enhanced zymographic detection of matrilysin and collagenases. Anal. Biochem. 2001;293:38–42.
  • Yamamoto K, Higashi S, Kioi M, Tsunezumi J, Honke K, Miyazaki K. Binding of active matrilysin to cell surface cholesterol sulfate is essential for its membrane-associated proteolytic action and induction of homotypic cell adhesion. J. Biol. Chem. 2006;281:9170–9180.
  • Higashi S, Oeda M, Yamamoto K, Miyazaki K. Identification of amino acid residues of matrix metalloproteinase 7 essential for binding to cholesterol sulfate. J. Biol. Chem. 2008;283:35735–35744.
  • Yamamoto K, Miyazaki K, Higashi S. Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin. J. Biol. Chem. 2010;285:28862–28873.
  • 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.
  • Muta Y, Yasui N, Matsumiya Y, Kubo M, Inouye K. Expression in Escherichia coli, refolding, and purification of the recombinant mature form of human matrix metalloproteinase 7 (MMP-7). Biosci. Biotechnol. Biochem. 2010;74:2515–2517.
  • Oneda H, Inouye K. Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia Coli. J. Biochem. 1999;126:905–911.
  • Oneda H, Inouye K. Effects of dimethyl sulfoxide, temperature, and sodium chloride on the activity of human matrix metalloproteinase 7 (matrilysin). J. Biochem. 2000;128:785–791.
  • Kjellen L, Lindahl U. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 1991;60:443–475.
  • Gambetti S, Dondi A, Cervellati C, Squerzanti M, Pansini FS, Bergamini CM. Interaction with heparin protects tissue transglutaminase against inactivation by heating and by proteolysis. Biochimie. 2005;87:551–555.
  • O’Farrell F, Loog M, Janson IM, Ek P. Kinetic study of the inhibition of CK2 by heparin fragments of different length. Biochim. Biophys. Acta. 1999;1433:68–75.
  • Ganguly B, Banerjee J, Elegbede AI, Klocke DJ, Mallik S, Srivastava DK. Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes. FEBS Lett. 2007;581:5723–5726.
  • Vemuri S, Beylin I, Sluzky V, Stratton P, Eberlein G, Wang YJ. The stability of bFGF against thermal denaturation. J. Pharm. Pharmacol. 1994;46:481–486.
  • Bugs MR, Bortoleto-Bugs RK, Cornélio ML. The interaction between heparin and Lys49 phospholipase A2 reveals the natural binding of heparin on the enzyme. Int. J. Biol. Macromol. 2005;37:21–27.
  • Golabek AA, Walus M, Wisniewski KE, Kida E. Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo. J. Biol. Chem. 2005;280:7550–7561.
  • Bágel’ová J, Antalík M, Bona M. Studies on cytochrome c-heparin interactions by differential scanning calorimetry. Biochem. J. 1994;297:99–101.
  • Strott CA, Higashi Y. Cholesterol sulfate in human physiology: what’s it all about? J. Lipid Res. 2003;44:1268–1278.
  • Nakae H, Hiroi H, Momoeda M, Koizumi M, Iwamori M, Taketani Y. Inhibition of cell invasion and protease activity by cholesterol sulfate. Fertil. Steril. 2010;94:2455–2457.
  • Kallen J, Schlaeppi JM, Bitsch F, Delhon I, Fournier B. Crystal structure of the human RORα ligand binding domain in complex with cholesterol sulfate at 2.2 Å. J. Biol. Chem. 2004;279:14033–14038.

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