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Volumn 288, Issue 51, 2013, Pages 36636-36647

Potent reversible inhibition of myeloperoxidase by aromatic hydroxamates

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING AFFINITIES; HEME POCKETS; INFLAMMATORY DISEASE; MYELOPEROXIDASE; OXIDATIVE DAMAGE; REVERSIBLE INHIBITIONS; SUBSTITUTED AROMATIC;

EID: 84890909211     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.507756     Document Type: Article
Times cited : (91)

References (52)
  • 2
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies, M. J., Hawkins, C. L., Pattison, D. I., and Rees, M. D. (2008) Mammalian heme peroxidases: From molecular mechanisms to health implications. Antioxid. Redox. Signal. 10, 1199-1234
    • (2008) Antioxid. Redox. Signal , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 3
    • 73449143528 scopus 로고    scopus 로고
    • Myeloperoxidase: Molecular mechanisms of action and their relevance to human health and disease
    • van der Veen, B. S., de Winther, M. P., and Heeringa, P. (2009) Myeloperoxidase: Molecular mechanisms of action and their relevance to human health and disease. Antioxid. Redox. Signal. 11, 2899-2937
    • (2009) Antioxid. Redox. Signal. , vol.11 , pp. 2899-2937
    • Van Der Veen, B.S.1    De Winther, M.P.2    Heeringa, P.3
  • 5
    • 0026079216 scopus 로고
    • Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs
    • Kettle, A. J., and Winterbourn, C. C. (1991) Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs. Biochem. Pharmacol. 41, 1485-1492
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1485-1492
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 7
    • 69249244191 scopus 로고    scopus 로고
    • Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase
    • Sliskovic, I., Abdulhamid, I., Sharma, M., and Abu-Soud, H. M. (2009) Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase. Free Radic. Biol. Med. 47, 1005-1013
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1005-1013
    • Sliskovic, I.1    Abdulhamid, I.2    Sharma, M.3    Abu-Soud, H.M.4
  • 9
    • 80054014857 scopus 로고    scopus 로고
    • Inhibition of the chlorinating activity of myeloperoxidase by Tempol: Revisiting the kinetics and mechanisms
    • Queiroz, R. F., Vaz, S. M., and Augusto, O. (2011) Inhibition of the chlorinating activity of myeloperoxidase by Tempol: Revisiting the kinetics and mechanisms. Biochem. J. 439, 423-431
    • (2011) Biochem. J. , vol.439 , pp. 423-431
    • Queiroz, R.F.1    Vaz, S.M.2    Augusto, O.3
  • 10
    • 0033567245 scopus 로고    scopus 로고
    • Oxidation of clozapine and ascorbate by myeloperoxidase
    • Hsuanyu, Y., and Dunford, H. B. (1999) Oxidation of clozapine and ascorbate by myeloperoxidase. Arch. Biochem. Biophys. 368, 413-420
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 413-420
    • Hsuanyu, Y.1    Dunford, H.B.2
  • 13
    • 0031029267 scopus 로고    scopus 로고
    • The mechanism of inactivation of myeloperoxidase by 4-Aminobenzoic acid hydrazide
    • Kettle, A. J., Gedye, C. A., and Winterbourn, C. C. (1997) The mechanism of inactivation of myeloperoxidase by 4-Aminobenzoic acid hydrazide. Biochem. J. 321, 503-508
    • (1997) Biochem. J. , vol.321 , pp. 503-508
    • Kettle, A.J.1    Gedye, C.A.2    Winterbourn, C.C.3
  • 16
    • 84865469048 scopus 로고    scopus 로고
    • Isoniazid as a substrate and inhibitor of myeloperoxidase: Identification of amine adducts and the influence of superoxide dismutase on their formation
    • Forbes, L. V., Furtmüller, P. G., Khalilova, I., Turner, R., Obinger, C., and Kettle, A. J. (2012) Isoniazid as a substrate and inhibitor of myeloperoxidase: Identification of amine adducts and the influence of superoxide dismutase on their formation. Biochem. Pharmacol. 84, 949-960
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 949-960
    • Forbes, L.V.1    Furtmüller, P.G.2    Khalilova, I.3    Turner, R.4    Obinger, C.5    Kettle, A.J.6
  • 17
    • 0034792757 scopus 로고    scopus 로고
    • Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase
    • Arnhold, J., Furtmüller, P. G., Regelsberger, G., and Obinger, C. (2001) Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase. Eur. J. Biochem. 268, 5142-5148
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5142-5148
    • Arnhold, J.1    Furtmüller, P.G.2    Regelsberger, G.3    Obinger, C.4
  • 18
    • 0037423684 scopus 로고    scopus 로고
    • Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase
    • Furtmüler, P. G., Arnhold, J., Jantschko, W., Pichler, H., and Obinger, C. (2003) Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase. Biochem. Biophys. Res. Commun. 301, 551-557
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 551-557
    • Furtmüler, P.G.1    Arnhold, J.2    Jantschko, W.3    Pichler, H.4    Obinger, C.5
  • 19
    • 0026645711 scopus 로고
    • The role of leukocyte-generated reactive metabolites in the pathogenesis of idiosyncratic drug reactions
    • Uetrecht, J. P. (1992) The role of leukocyte-generated reactive metabolites in the pathogenesis of idiosyncratic drug reactions. Drug Metab. Rev. 24, 299-366
    • (1992) Drug Metab. Rev. , vol.24 , pp. 299-366
    • Uetrecht, J.P.1
  • 20
    • 0028063436 scopus 로고
    • Transformation of lupusinducing drugs to cytotoxic products by activated neutrophils
    • Jiang, X., Khursigara, G., and Rubin, R. L. (1994) Transformation of lupusinducing drugs to cytotoxic products by activated neutrophils. Science 266, 810-813
    • (1994) Science , vol.266 , pp. 810-813
    • Jiang, X.1    Khursigara, G.2    Rubin, R.L.3
  • 21
    • 0024536827 scopus 로고
    • Inhibition of myeloperoxidase by salicylhydroxamic acid
    • Davies, B., and Edwards, S. W. (1989) Inhibition of myeloperoxidase by salicylhydroxamic acid. Biochem. J. 258, 801-806
    • (1989) Biochem. J. , vol.258 , pp. 801-806
    • Davies, B.1    Edwards, S.W.2
  • 22
    • 0017828675 scopus 로고
    • Studies on mechanism of inhibition of redox enzymes by substituted hydroxamic acids
    • Rich, P. R., Wiegand, N. K., Blum, H., Moore, A. L., and Bonner, W. D. (1978) Studies on mechanism of inhibition of redox enzymes by substituted hydroxamic acids. Biochim. Biophys. Acta 525, 325-337
    • (1978) Biochim. Biophys. Acta , vol.525 , pp. 325-337
    • Rich, P.R.1    Wiegand, N.K.2    Blum, H.3    Moore, A.L.4    Bonner, W.D.5
  • 23
    • 0029003475 scopus 로고
    • Inhibition of myeloperoxidase by benzoic acid hydrazides
    • Kettle, A. J., Gedye, C. A., Hampton, M. B., and Winterbourn, C. C. (1995) Inhibition of myeloperoxidase by benzoic acid hydrazides. Biochem. J. 308, 559-563
    • (1995) Biochem. J. , vol.308 , pp. 559-563
    • Kettle, A.J.1    Gedye, C.A.2    Hampton, M.B.3    Winterbourn, C.C.4
  • 25
    • 0029664747 scopus 로고    scopus 로고
    • 2.3 Å resolution x-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: A model for a prereaction complex with hydrogen peroxide
    • Davey, C. A., and Fenna, R. E. (1996) 2.3 Å resolution x-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: A model for a prereaction complex with hydrogen peroxide. Biochemistry 35, 10967-10973
    • (1996) Biochemistry , vol.35 , pp. 10967-10973
    • Davey, C.A.1    Fenna, R.E.2
  • 26
    • 0034006566 scopus 로고    scopus 로고
    • Large-scale purification of myeloperoxidasefrom HL60 promyelocytic cells: Ccharacterization and comparison to human neutrophil myeloperoxidase
    • Hope, H. R., Remsen, E. E., Lewis, C., Jr., Heuvelman, D. M., Walker, M. C., Jennings, M., and Connolly, D. T. (2000) Large-scale purification of myeloperoxidasefrom HL60 promyelocytic cells: Characterization and comparison to human neutrophil myeloperoxidase. Protein Expr. Purif. 18, 269-276
    • (2000) Protein Expr. Purif. , vol.18 , pp. 269-276
    • Hope, H.R.1    Remsen, E.E.2    Lewis, Jr.C.3    Heuvelman, D.M.4    Walker, M.C.5    Jennings, M.6    Connolly, D.T.7
  • 28
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff, S. P. (1994) Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Methods Enzymol. 233, 182-189
    • (1994) Methods Enzymol , vol.233 , pp. 182-189
    • Wolff, S.P.1
  • 29
    • 2442743845 scopus 로고    scopus 로고
    • Nadph as a co-substrate for studies of the chlorinating activity of myeloperoxidase
    • Auchère, F., and Capeillère-Blandin, C. (1999) NADPH as a co-substrate for studies of the chlorinating activity of myeloperoxidase. Biochem. J. 343, 603-613
    • (1999) Biochem. J. , vol.343 , pp. 603-613
    • Auchère, F.1    Capeillère-Blandin, C.2
  • 30
    • 0034254665 scopus 로고    scopus 로고
    • On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids
    • Prütz, W. A., Kissner, R., Koppenol, W. H., and Rüegger, H. (2000) On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids. Arch. Biochem. Biophys. 380, 181-191
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 181-191
    • Prütz, W.A.1    Kissner, R.2    Koppenol, W.H.3    Rüegger, H.4
  • 31
    • 0030880690 scopus 로고    scopus 로고
    • Tyrosinase- catecholic substrates in vitro model: Kinetic studies on the o-quinone/ o-semiquinone radical formation
    • Ferrari, R. P., Laurenti, E., Ghibaudi, E. M., and Casella, L. (1997) Tyrosinase- catecholic substrates in vitro model: kinetic studies on the o-quinone/ o-semiquinone radical formation. J. Inorg. Biochem. 68, 61-69
    • (1997) J. Inorg. Biochem. , vol.68 , pp. 61-69
    • Ferrari, R.P.1    Laurenti, E.2    Ghibaudi, E.M.3    Casella, L.4
  • 33
    • 0037974571 scopus 로고    scopus 로고
    • Cytochrome P450 inhibition using recombinant proteins and mass spectrometry/multiple reaction monitoring technology in a cassette incubation
    • Weaver, R., Graham, K. S., Beattie, I. G., and Riley, R. J. (2003) Cytochrome P450 inhibition using recombinant proteins and mass spectrometry/multiple reaction monitoring technology in a cassette incubation. Drug Metab. Dispos. 31, 955-966
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 955-966
    • Weaver, R.1    Graham, K.S.2    Beattie, I.G.3    Riley, R.J.4
  • 35
    • 0026538766 scopus 로고
    • A spectrophotometric microtiter-based assay for the detection of hydroperoxy derivatives of linoleic-Acid
    • Auerbach, B. J., Kiely, J. S., and Cornicelli, J. A. (1992) A spectrophotometric microtiter-based assay for the detection of hydroperoxy derivatives of linoleic-Acid. Anal. Biochem. 201, 375-380
    • (1992) Anal. Biochem. , vol.201 , pp. 375-380
    • Auerbach, B.J.1    Kiely, J.S.2    Cornicelli, J.A.3
  • 36
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood. Isolation of mononuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g
    • Böum, A. (1968) Isolation of mononuclear cells and granulocytes from human blood. Isolation of mononuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand. J. Clin. Lab. Invest. Suppl. 97, 77-89
    • (1968) Scand. J. Clin. Lab. Invest. Suppl. , vol.97 , pp. 77-89
    • Böum, A.1
  • 37
    • 0033396672 scopus 로고    scopus 로고
    • Respiratory burst in human neutrophils
    • Dahlgren, C., and Karlsson, A. (1999) Respiratory burst in human neutrophils. J. Immunol. Methods 232, 3-14
    • (1999) J. Immunol. Methods , vol.232 , pp. 3-14
    • Dahlgren, C.1    Karlsson, A.2
  • 38
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry
    • Thornalley, P. J., Battah, S., Ahmed, N., Karachalias, N., Agalou, S., Babaei- Jadidi, R., and Dawnay, A. (2003) Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. Biochem. J. 375, 581-592
    • (2003) Biochem. J. , vol.375 , pp. 581-592
    • Thornalley, P.J.1    Battah, S.2    Ahmed, N.3    Karachalias, N.4    Agalou, S.5    Babaei-Jadidi, R.6    Dawnay, A.7
  • 39
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie, A. G. (1999) Integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 55, 1696-1702
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 40
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 41
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • Fiedler, T. J., Davey, C. A., and Fenna, R. E. (2000) X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem. 275, 11964-11971
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110 -119
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 0029557684 scopus 로고
    • Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications for lipoprotein peroxidation studies
    • Marquez, L. A., and Dunford, H. B. (1995) Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications for lipoprotein peroxidation studies. J. Biol. Chem. 270, 30434-30440
    • (1995) J. Biol. Chem. , vol.270 , pp. 30434-30440
    • Marquez, L.A.1    Dunford, H.B.2
  • 44
    • 0030046117 scopus 로고    scopus 로고
    • Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
    • Kettle, A. J. (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett. 379, 103-106
    • (1996) FEBS Lett , vol.379 , pp. 103-106
    • Kettle, A.J.1
  • 45
    • 0006145015 scopus 로고    scopus 로고
    • Understanding enzyme inhibition
    • Ochs, R. S. (2000) Understanding enzyme inhibition. J. Chem. Educ. 77, 1453-1456
    • (2000) J. Chem. Educ. , vol.77 , pp. 1453-1456
    • Ochs, R.S.1
  • 46
    • 0034102068 scopus 로고    scopus 로고
    • Nitric oxide modulates the catalytic activity of myeloperoxidase
    • Abu-Soud, H. M., and Hazen, S. L. (2000) Nitric oxide modulates the catalytic activity of myeloperoxidase. J. Biol. Chem. 275, 5425-5430
    • (2000) J. Biol. Chem. , vol.275 , pp. 5425-5430
    • Abu-Soud, H.M.1    Hazen, S.L.2
  • 48
    • 0021105386 scopus 로고
    • Stimulation of peroxidase reactions by hydroxamates
    • Brooks, J. L. (1983) Stimulation of peroxidase reactions by hydroxamates. Biochem. Biophys. Res. Commun. 116, 916-921
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 916-921
    • Brooks, J.L.1
  • 49
    • 84863453838 scopus 로고    scopus 로고
    • The mechanism underlying nitroxyl and nitric oxide formation from hydroxamic acids
    • Samuni, Y., Samuni, U., and Goldstein, S. (2012) The mechanism underlying nitroxyl and nitric oxide formation from hydroxamic acids. Biochim. Biophys. Acta 1820, 1560-1566
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1560-1566
    • Samuni, Y.1    Samuni, U.2    Goldstein, S.3
  • 50
    • 0029092658 scopus 로고
    • Neuronal nitric-oxide synthase self-inactivates byforming a ferrous-nitrosyl complex during aerobic catalysis
    • Abu-Soud, H. M., Wang, J., Rousseau, D. L., Fukuto, J. M., Ignarro, L. J., and Stuehr, D. J. (1995) Neuronal nitric-oxide synthase self-inactivates byforming a ferrous-nitrosyl complex during aerobic catalysis. J. Biol. Chem. 270, 22997-23006
    • (1995) J. Biol. Chem. , vol.270 , pp. 22997-23006
    • Abu-Soud, H.M.1    Wang, J.2    Rousseau, D.L.3    Fukuto, J.M.4    Ignarro, L.J.5    Stuehr, D.J.6
  • 51
    • 77953514816 scopus 로고    scopus 로고
    • Oxidative heme proteinmediated nitroxyl (HNO) generation
    • Reisz, J. A., Bechtold, E., and King, S. B. (2010) Oxidative heme proteinmediated nitroxyl (HNO) generation. Dalton Trans. 39, 5203-5212
    • (2010) Dalton Trans. , vol.39 , pp. 5203-5212
    • Reisz, J.A.1    Bechtold, E.2    King, S.B.3
  • 52
    • 10644245185 scopus 로고    scopus 로고
    • Coordination chemistry of the HNO ligand with hemes and synthetic coordination complexes
    • Farmer, P. J., and Sulc, F. (2005) Coordination chemistry of the HNO ligand with hemes and synthetic coordination complexes. J. Inorg. Biochem. 99, 166-184
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 166-184
    • Farmer, P.J.1    Sulc, F.2


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