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Volumn 1814, Issue 12, 2011, Pages 1940-1946

Thermodynamic analysis of ionizable groups involved in the catalytic mechanism of human matrix metalloproteinase 7 (MMP-7)

Author keywords

Ionizable group; Matrix metalloproteinase; MMP 7; Proton dissociation constant; Thermodynamic analysis

Indexed keywords

ARGININE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; HISTIDINE; LYSINE; MATRILYSIN; TYROSINE;

EID: 81755184328     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.07.008     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • J.F. Woessner Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling FASEB J. 5 1991 2145 2154 (Pubitemid 21905847)
    • (1991) FASEB Journal , vol.5 , Issue.8 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 2
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • H. Nagase, and J.F. Woessner Jr. Matrix metalloproteinases J. Biol. Chem. 274 1999 21491 21494
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, Jr.J.F.2
  • 3
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metalloproteinase of the rat uterus
    • J.F. Woessner Jr., and C.J. Taplin Purification and properties of a small latent matrix metalloproteinase of the rat uterus J. Biol. Chem. 263 1988 16918 16925 (Pubitemid 18268875)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.32 , pp. 16918-16925
    • Woessner Jr., J.F.1    Taplin, C.J.2
  • 4
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteinases
    • M.F. Browner, W.W. Smith, and A.L. Castelhano Matrilysin-inhibitor complexes: common themes among metalloproteinases Biochemistry 34 1995 6602 6610
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 6
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • DOI 10.1074/jbc.275.6.4183
    • W.-H. Yu, and J.F. Woessner Jr. Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7) J. Biol. Chem. 275 2000 4183 4191 (Pubitemid 30094653)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 4183-4191
    • Yu, W.-H.1    Woessner Jr., J.F.2
  • 7
    • 33646916682 scopus 로고    scopus 로고
    • Binding of active matrilysin to cell surface cholesterol sulfate is essential for its membrane-associated proteolytic action and induction of homotypic cell adhesion
    • DOI 10.1074/jbc.M510377200
    • K. Yamamoto, S. Higashi, M. Kioi, J. Tsunezumi, K. Honke, and K. Miyazaki 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. 281 2006 9170 9180 (Pubitemid 43864631)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9170-9180
    • Yamamoto, K.1    Higashi, S.2    Kioi, M.3    Tsunezumi, J.4    Honke, K.5    Miyazaki, K.6
  • 8
    • 58149096976 scopus 로고    scopus 로고
    • Identification of amino acid residues of matrix metalloproteinase 7 essential for binding to cholesterol sulfate
    • S. Higashi, M. Oeda, K. Yamamoto, and K. Miyazaki Identification of amino acid residues of matrix metalloproteinase 7 essential for binding to cholesterol sulfate J. Biol. Chem. 283 2008 35735 35744
    • (2008) J. Biol. Chem. , vol.283 , pp. 35735-35744
    • Higashi, S.1    Oeda, M.2    Yamamoto, K.3    Miyazaki, K.4
  • 9
    • 77956497995 scopus 로고    scopus 로고
    • Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin
    • K. Yamamoto, K. Miyazaki, and S. Higashi Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin J. Biol. Chem. 285 2010 28862 28873
    • (2010) J. Biol. Chem. , vol.285 , pp. 28862-28873
    • Yamamoto, K.1    Miyazaki, K.2    Higashi, S.3
  • 10
    • 34547122752 scopus 로고    scopus 로고
    • Matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor
    • DOI 10.1158/0008-5472.CAN-07-0026
    • C.C. Lynch, T. Vargo-Gogola, M.D. Martin, B. Fingleton, H.C. Crawford, and L.M. Matrisian Matrix metalloproteinase 7 mediates mammary epithelial cell tumorigenesis through the ErbB4 receptor Cancer Res. 57 2007 6760 6767 (Pubitemid 47105523)
    • (2007) Cancer Research , vol.67 , Issue.14 , pp. 6760-6767
    • Lynch, C.C.1    Vargo-Gogola, T.2    Martin, M.D.3    Fingleton, B.4    Crawford, H.C.5    Matrisian, L.M.6
  • 11
    • 0038647540 scopus 로고    scopus 로고
    • Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (matrilysin)
    • DOI 10.1093/jb/mvg073
    • H. Oneda, M. Shiihara, and K. Inouye Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (matrilysin) J. Biochem. 133 2003 571 576 (Pubitemid 36759463)
    • (2003) Journal of Biochemistry , vol.133 , Issue.5 , pp. 571-576
    • Oneda, H.1    Shiihara, M.2    Inouye, K.3
  • 12
    • 4644252440 scopus 로고    scopus 로고
    • Inhibitory effects of lignans on the activity of human matrix metalloproteinase 7 (matrilysin)
    • Y. Muta, S. Oyama, T. Umezawa, M. Shimada, and K. Inouye Inhibitory effects of lignans on the activity of human matrix metalloproteinase 7 (matrilysin) J. Agric. Food Chem. 52 2004 5888 5894
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 5888-5894
    • Muta, Y.1    Oyama, S.2    Umezawa, T.3    Shimada, M.4    Inouye, K.5
  • 13
    • 0035054059 scopus 로고    scopus 로고
    • Interactions of human matrix metalloproteinase 7 (Matrilysin) with the inhibitors thiorphan and R-94138
    • H. Oneda, and K. Inouye Interactions of human matrix metalloproteinase 7 (matrilysin) with the inhibitors thiorphan and R-94138 J. Biochem. 129 2001 429 435 (Pubitemid 32304118)
    • (2001) Journal of Biochemistry , vol.129 , Issue.3 , pp. 429-435
    • Oneda, H.1    Inouye, K.2
  • 14
    • 70449726460 scopus 로고    scopus 로고
    • Effects of detergents on catalytic activity of human endometase/ matrilysin 2, a putative cancer biomarker
    • H.I. Park, S. Lee, A. Ullah, Q. Cao, and Q.X. Sang Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker Anal. Biochem. 396 2010 262 268
    • (2010) Anal. Biochem. , vol.396 , pp. 262-268
    • Park, H.I.1    Lee, S.2    Ullah, A.3    Cao, Q.4    Sang, Q.X.5
  • 15
    • 0026775558 scopus 로고
    • Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases
    • T. Crabbe, F. Willenbrock, D. Eaton, P. Hynds, A.F. Carne, G. Murphy, and A.J. Docherty Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases Biochemistry 31 1992 8500 8507
    • (1992) Biochemistry , vol.31 , pp. 8500-8507
    • Crabbe, T.1    Willenbrock, F.2    Eaton, D.3    Hynds, P.4    Carne, A.F.5    Murphy, G.6    Docherty, A.J.7
  • 16
    • 0022996811 scopus 로고
    • Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein
    • G.I. Goldberg, S.M. Wilhelm, A. Kronberger, E.A. Bauer, G.A. Grant, and A.Z. Eisen Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein J. Biol. Chem. 261 1986 6600 6605 (Pubitemid 17204179)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.14 , pp. 6600-6605
    • Goldberg, G.I.1    Wilhelm, S.M.2    Kronberger, A.3
  • 18
    • 0022917253 scopus 로고
    • Comparison of human stromelysin and collagenase by cloning and sequence analysis
    • S.E. Whitham, G. Murphy, P. Angel, H.J. Rahmsdorf, B.J. Smith, A. Lyons, T.J. Harris, J.J. Reynolds, P. Herrlich, and A.J. Docherty Comparison of human stromelysin and collagenase by cloning and sequence analysis Biochem. J. 240 1986 913 916 (Pubitemid 17010016)
    • (1986) Biochemical Journal , vol.240 , Issue.3 , pp. 913-916
    • Whitham, S.E.1    Murphy, G.2    Angel, P.3
  • 20
    • 0025769518 scopus 로고
    • Structure and expression of the cDNA encoding human neutrophil collagenase
    • P. Devarajan, K. Mookhtiar, H. van Wart, and N. Berliner Structure and expression of the cDNA encoding human neutrophil collagenase Blood 77 1991 2731 2738
    • (1991) Blood , vol.77 , pp. 2731-2738
    • Devarajan, P.1    Mookhtiar, K.2    Van Wart, H.3    Berliner, N.4
  • 23
    • 0028940033 scopus 로고
    • Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain
    • T. Takino, H. Sato, E. Yamamoto, and M. Seiki Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain Gene 155 1995 293 298
    • (1995) Gene , vol.155 , pp. 293-298
    • Takino, T.1    Sato, H.2    Yamamoto, E.3    Seiki, M.4
  • 24
    • 0029877524 scopus 로고    scopus 로고
    • Computational sequence analysis of matrix metalloproteinases
    • DOI 10.1007/BF01887395
    • Q.A. Sang, and D.A. Douglas Computational sequence analysis of matrix metalloproteinase J. Protein Chem. 15 1996 137 160 (Pubitemid 26108855)
    • (1996) Journal of Protein Chemistry , vol.15 , Issue.2 , pp. 137-160
    • Sang, Q.A.1    Douglas, D.A.2
  • 25
    • 0029768642 scopus 로고    scopus 로고
    • Metal and pH dependence of heptapeptide catalysis by human matrilysin
    • DOI 10.1021/bi962085f
    • J. Cha, M.V. Pedersen, and D.S. Auld Metal and pH dependence of heptapeptide catalysis by human matrilysin Biochemistry 35 1996 15831 15838 (Pubitemid 26422321)
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15831-15838
    • Cha, J.1    Pedersen, M.V.2    Auld, D.S.3
  • 26
    • 0031439461 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    • DOI 10.1021/bi972223g
    • J. Cha, and D.S. Auld Site-directed mutagenesis of the active site glutamate in human matrilysin: investigation of its role in catalysis Biochemistry 36 1997 16019 16024 (Pubitemid 28027407)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 16019-16024
    • Cha, J.1    Auld, D.S.2
  • 27
    • 14844302862 scopus 로고    scopus 로고
    • Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues
    • DOI 10.1042/BJ20040985
    • Y. Muta, H. Oneda, and K. Inouye Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues Biochem. J. 386 2005 263 270 (Pubitemid 40343783)
    • (2005) Biochemical Journal , vol.386 , Issue.2 , pp. 263-270
    • Muta, Y.1    Oneda, H.2    Inouye, K.3
  • 28
    • 79961090772 scopus 로고    scopus 로고
    • 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
    • Y. Muta, and K. Inouye 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. 150 2011 183 188
    • (2011) J. Biochem. , vol.150 , pp. 183-188
    • Muta, Y.1    Inouye, K.2
  • 29
    • 0004722259 scopus 로고
    • Dipolar ions and acid-base equilibria
    • E.J. Cohn, J.T. Edsall, Hafner Publishing Company New York and London
    • J.T. Edsall Dipolar ions and acid-base equilibria E.J. Cohn, J.T. Edsall, Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions 1943 Hafner Publishing Company New York and London 75 115
    • (1943) Proteins, Amino Acids, and Peptides As Ions and Dipolar Ions , pp. 75-115
    • Edsall, J.T.1
  • 30
    • 33749129720 scopus 로고
    • Studies of the peptides of trivalent amino acids. I. Titration constants of histidyl-histidine and of aspartyl-aspartic acid
    • J.P. Geenstein Studies of the peptides of trivalent amino acids. I. Titration constants of histidyl-histidine and of aspartyl-aspartic acid J. Biol. Chem. 93 1931 479 494
    • (1931) J. Biol. Chem. , vol.93 , pp. 479-494
    • Geenstein, J.P.1
  • 31
    • 0000079252 scopus 로고
    • Studies of the peptides of trivalent amino acids. III. The apparent dissociation constants, free energy changes, and heats of ionization of peptides involving arginine, histidine, lysine, tyrosine, and aspartic and glutamic acids, and the behavior of lysine peptides toward nitrous acid
    • J.P. Greenstein Studies of the peptides of trivalent amino acids. III. The apparent dissociation constants, free energy changes, and heats of ionization of peptides involving arginine, histidine, lysine, tyrosine, and aspartic and glutamic acids, and the behavior of lysine peptides toward nitrous acid J. Biol. Chem. 101 1933 603 621
    • (1933) J. Biol. Chem. , vol.101 , pp. 603-621
    • Greenstein, J.P.1
  • 32
    • 0001491319 scopus 로고
    • Thermodynamic properties of solutions of amino acids and related substances. III. The ionization of aliphatic amino acids in aqueous solution from one to fifty degrees
    • P.K. Smith, A.C. Taylor, and E.R.B. Smith Thermodynamic properties of solutions of amino acids and related substances. III. The ionization of aliphatic amino acids in aqueous solution from one to fifty degrees J. Biol. Chem. 122 1937 109 123
    • (1937) J. Biol. Chem. , vol.122 , pp. 109-123
    • Smith, P.K.1    Taylor, A.C.2    Smith, E.R.B.3
  • 33
    • 0003171306 scopus 로고
    • A kinetic study of the reactions on some disulphides with sodium sulphite
    • R. Cecil, and J.R. McPhee A kinetic study of the reactions on some disulphides with sodium sulphite Biochem. J. 60 1955 496 506
    • (1955) Biochem. J. , vol.60 , pp. 496-506
    • Cecil, R.1    McPhee, J.R.2
  • 34
    • 0013906090 scopus 로고
    • Kinetic studies on gluc-amylase. III. The influence of pH on the rates of hydrolysis of maltose and panose
    • K. Hiromi, K. Takahashi, Z. Hamauzu, and S. Ono Kinetic studies on gluc-amylase. III. The influence of pH on the rates of hydrolysis of maltose and panose J. Biochem. 59 1966 469 475
    • (1966) J. Biochem. , vol.59 , pp. 469-475
    • Hiromi, K.1    Takahashi, K.2    Hamauzu, Z.3    Ono, S.4
  • 35
    • 35348868207 scopus 로고    scopus 로고
    • Chemical modification studies on arginine kinase: Essential cysteine and arginine residues at the active site
    • DOI 10.1016/j.ijbiomac.2007.07.007, PII S0141813007001766
    • W.J. Zhu, M. Li, and X.Y. Wang Chemical modification studies on arginine kinase: essential cysteine and arginine residues at the active site Int. J. Biol. Macromol. 41 2007 564 571 (Pubitemid 47575751)
    • (2007) International Journal of Biological Macromolecules , vol.41 , Issue.5 , pp. 564-571
    • Zhu, W.-J.1    Li, M.2    Wang, X.-Y.3
  • 37
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinase
    • C.G. Knight, F. Willenbrock, and G. Murphy A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinase FEBS Lett. 296 1992 263 266
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 38
    • 78650644852 scopus 로고    scopus 로고
    • Expression in Escherichia coli, refolding, and purification of the recombinant mature form of human matrix metalloproteinase 7 (MMP-7)
    • Y. Muta, N. Yasui, Y. Matsumiya, M. Kubo, and K. Inouye Expression in Escherichia coli, refolding, and purification of the recombinant mature form of human matrix metalloproteinase 7 (MMP-7) Biosci. Biotechnol. Biochem. 74 2010 2151 2517
    • (2010) Biosci. Biotechnol. Biochem. , vol.74 , pp. 2151-2517
    • Muta, Y.1    Yasui, N.2    Matsumiya, Y.3    Kubo, M.4    Inouye, K.5
  • 39
    • 0032731203 scopus 로고    scopus 로고
    • Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli
    • H. Oneda, and K. Inouye Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli J. Biochem. 126 1999 905 911
    • (1999) J. Biochem. , vol.126 , pp. 905-911
    • Oneda, H.1    Inouye, K.2
  • 40
    • 0030609810 scopus 로고    scopus 로고
    • 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile
    • M. Betz, P. Huxley, S.J. Davies, Y. Mushtaq, M. Pieper, H. Tschesche, W. Bode, and F.X. Gomis-Rüth 1.8-Å crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile Eur. J. Biochem. 247 1997 356 363 (Pubitemid 27319524)
    • (1997) European Journal of Biochemistry , vol.247 , Issue.1 , pp. 356-363
    • Betz, M.1    Huxley, P.2    Davies, S.J.3    Mushtaq, Y.4    Pieper, M.5    Tschesche, H.6    Bode, W.7    Gomis-Ruth, E.X.8
  • 41
    • 0028063371 scopus 로고
    • Mutational analysis of residues in and around the active site of human fibroblast-type collagenase
    • L.J. Windsor, M.K. Bodden, B. Birkedal-Hansen, J.A. Engler, and H. Birkedal-Hansen Mutational analysis of residues in and around the active site of human fibroblast-type collagenase J. Biol. Chem. 269 1994 4033 4040
    • (1994) J. Biol. Chem. , vol.269 , pp. 4033-4040
    • Windsor, L.J.1    Bodden, M.K.2    Birkedal-Hansen, B.3    Engler, J.A.4    Birkedal-Hansen, H.5
  • 42
    • 0034818299 scopus 로고    scopus 로고
    • Critical role of glutamic acid 202 in the enzymatic activity of stromelysin-1 (MMP-3)
    • DOI 10.1046/j.1432-1327.2001.01943.x
    • B. Arza, M. de Maeyer, J. Félez, D. Collen, and H.R. Lijnen Critical role of glutamic acid 202 in the enzyme activity of stromelysin-1 (MMP-3) Eur. J. Biochem. 268 2001 826 831 (Pubitemid 32862643)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.3 , pp. 826-831
    • Arza, B.1    De Maeyer, M.2    Felez, J.3    Collen, D.4    Roger Lijnen, H.5
  • 44
    • 0037020639 scopus 로고    scopus 로고
    • Catalytic mechanism of matrix metalloproteinases: Two-layered ONIOM study
    • V. Pelmenschikov, and P.E. Siegbahn Catalytic mechanism of matrix metalloproteinases: two-layered ONIOM study Inorg. Chem. 41 2002 5659 5666
    • (2002) Inorg. Chem. , vol.41 , pp. 5659-5666
    • Pelmenschikov, V.1    Siegbahn, P.E.2
  • 45
    • 0029590007 scopus 로고
    • Structure of binary and ternary complexes of zinc and cobalt carboxypeptidase A as determined by X-ray absorption fine structure
    • DOI 10.1021/bi00050a010
    • K. Zhang, and D.S. Auld Structure of binary and ternary complexes of zinc and cobalt carboxypeptidase A as determined by X-ray absorption fine structure Biochemistry 34 1995 16306 16312 (Pubitemid 26006473)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16306-16312
    • Zhang, K.1    Auld, D.S.2
  • 46
    • 0034716940 scopus 로고    scopus 로고
    • Hydrogen bonding and catalysis: A novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
    • M.D. Joshi, G. Sidhu, I. Pot, G.D. Brayer, S.G. Withers, and L.P. Mclntosh Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase J. Mol. Biol. 299 2000 255 279
    • (2000) J. Mol. Biol. , vol.299 , pp. 255-279
    • Joshi, M.D.1    Sidhu, G.2    Pot, I.3    Brayer, G.D.4    Withers, S.G.5    McLntosh, L.P.6


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