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Volumn 93, Issue 4, 2015, Pages 440-448

Aldehyde dehydrogenase-independent bioactivation of nitroglycerin in porcine and bovine blood vessels

Author keywords

Aldehyde dehydrogenase 2; Denitration; Nitroglycerin; Protein expression; Vascular relaxation

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALDEHYDE DEHYDROGENASE 3A1; ALDEHYDE DEHYDROGENASE ISOENZYME 2; CYTOCHROME P450; ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; GLYCERYL TRINITRATE; MESSENGER RNA; UNCLASSIFIED DRUG; ALDH2 PROTEIN, HUMAN;

EID: 84961290478     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2014.12.021     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 0019388174 scopus 로고
    • Mechanism of vascular smooth muscle relaxation by organic nitrates, nitrites, nitroprusside and nitric oxide: Evidence for the involvement of S-nitrosothiols as active intermediates
    • L.J. Ignarro, H. Lippton, J.C. Edwards, W.H. Baricos, A.L. Hyman, and P.J. Kadowitz Mechanism of vascular smooth muscle relaxation by organic nitrates, nitrites, nitroprusside and nitric oxide: evidence for the involvement of S-nitrosothiols as active intermediates J Pharmacol Exp Ther 218 1981 739 749
    • (1981) J Pharmacol Exp Ther , vol.218 , pp. 739-749
    • Ignarro, L.J.1    Lippton, H.2    Edwards, J.C.3    Baricos, W.H.4    Hyman, A.L.5    Kadowitz, P.J.6
  • 2
    • 0022380821 scopus 로고
    • The reaction between organic nitrates and sulfhydryl compounds. A possible model system for the activation of organic nitrates
    • R.A. Yeates, H. Laufen, and M. Leitold The reaction between organic nitrates and sulfhydryl compounds. A possible model system for the activation of organic nitrates Mol Pharmacol 28 1985 555 559
    • (1985) Mol Pharmacol , vol.28 , pp. 555-559
    • Yeates, R.A.1    Laufen, H.2    Leitold, M.3
  • 4
    • 0024390285 scopus 로고
    • Antagonism of glycerol trinitrate activity by an inhibitor of glutathione S-transferase
    • R.A. Yeates, M. Schmid, and M. Leitold Antagonism of glycerol trinitrate activity by an inhibitor of glutathione S-transferase Biochem Pharmacol 38 1989 1749 1753
    • (1989) Biochem Pharmacol , vol.38 , pp. 1749-1753
    • Yeates, R.A.1    Schmid, M.2    Leitold, M.3
  • 5
    • 0026595087 scopus 로고
    • Metabolism of nitroglycerin by smooth muscle cells: Involvement of glutathione and glutathione S-transferase
    • K.E. Hill, R.W. Hunt, R. Jones, R.L. Hoover, and R.F. Burke Metabolism of nitroglycerin by smooth muscle cells: involvement of glutathione and glutathione S-transferase Biochem Pharmacol 43 1992 561 566
    • (1992) Biochem Pharmacol , vol.43 , pp. 561-566
    • Hill, K.E.1    Hunt, R.W.2    Jones, R.3    Hoover, R.L.4    Burke, R.F.5
  • 6
    • 0025638838 scopus 로고
    • Cytochrome P-450 mediated biotransformation of organic nitrates
    • B.J. McDonald, and B.M. Bennett Cytochrome P-450 mediated biotransformation of organic nitrates Can J Physiol Pharmacol 68 1990 1552 1557
    • (1990) Can J Physiol Pharmacol , vol.68 , pp. 1552-1557
    • McDonald, B.J.1    Bennett, B.M.2
  • 7
    • 0026680866 scopus 로고
    • Cytochrome-P-450 mediates bioactivation of organic nitrates
    • H. Schröder Cytochrome-P-450 mediates bioactivation of organic nitrates J Pharmacol Exp Ther 262 1992 298 302
    • (1992) J Pharmacol Exp Ther , vol.262 , pp. 298-302
    • Schröder, H.1
  • 8
    • 0028020180 scopus 로고
    • Inhibition of the biotransformation and pharmacological actions of glyceryl trinitrate by the flavoprotein inhibitor, diphenyleneiodonium sulfate
    • J.J. McGuire, D.J. Anderson, and B.M. Bennett Inhibition of the biotransformation and pharmacological actions of glyceryl trinitrate by the flavoprotein inhibitor, diphenyleneiodonium sulfate J Pharmacol Exp Ther 271 1994 708 714
    • (1994) J Pharmacol Exp Ther , vol.271 , pp. 708-714
    • McGuire, J.J.1    Anderson, D.J.2    Bennett, B.M.3
  • 9
    • 0035816582 scopus 로고    scopus 로고
    • Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction. Evaluation of its role in nitric oxide generation in anoxic tissues
    • H.T. Li, A. Samouilov, X.P. Liu, and J.L. Zweier Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction. Evaluation of its role in nitric oxide generation in anoxic tissues J Biol Chem 276 2001 24482 24489
    • (2001) J Biol Chem , vol.276 , pp. 24482-24489
    • Li, H.T.1    Samouilov, A.2    Liu, X.P.3    Zweier, J.L.4
  • 10
    • 0034696803 scopus 로고    scopus 로고
    • Reduction of organic nitrites to nitric oxide catalyzed by xanthine oxidase: Possible role in metabolism of nitrovasodilators
    • J.J. Doel, B.L.J. Godber, T.A. Goult, R. Eisenthal, and R. Harrison Reduction of organic nitrites to nitric oxide catalyzed by xanthine oxidase: possible role in metabolism of nitrovasodilators Biochem Biophys Res Commun 270 2000 880 885
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 880-885
    • Doel, J.J.1    Godber, B.L.J.2    Goult, T.A.3    Eisenthal, R.4    Harrison, R.5
  • 11
    • 77956701107 scopus 로고    scopus 로고
    • Mitochondrial aldehyde dehydrogenase mediates vasodilator responses of glyceryl trinitrate and sodium nitrite in the pulmonary vascular bed of the rat
    • A.M. Badejo Jr., C. Hodnette, J.S. Dhaliwal, D.B. Casey, E. Pankey, and S.N. Murthy Mitochondrial aldehyde dehydrogenase mediates vasodilator responses of glyceryl trinitrate and sodium nitrite in the pulmonary vascular bed of the rat Am J Physiol 299 2010 H819 H826
    • (2010) Am J Physiol , vol.299 , pp. H819-H826
    • Badejo, Jr.A.M.1    Hodnette, C.2    Dhaliwal, J.S.3    Casey, D.B.4    Pankey, E.5    Murthy, S.N.6
  • 12
    • 1342281276 scopus 로고    scopus 로고
    • Biochemical mechanism of nitroglycerin action and tolerance: Is this old mystery solved?
    • H.L. Fung Biochemical mechanism of nitroglycerin action and tolerance: is this old mystery solved? Annu Rev Pharmacol Toxicol 44 2004 67 85
    • (2004) Annu Rev Pharmacol Toxicol , vol.44 , pp. 67-85
    • Fung, H.L.1
  • 13
    • 0037062518 scopus 로고    scopus 로고
    • Identification of the enzymatic mechanism of nitroglycerin bioactivation
    • Z. Chen, J. Zhang, and J.S. Stamler Identification of the enzymatic mechanism of nitroglycerin bioactivation Proc Natl Acad Sci USA 99 2002 8306 8311
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8306-8311
    • Chen, Z.1    Zhang, J.2    Stamler, J.S.3
  • 14
    • 51349126026 scopus 로고    scopus 로고
    • The enigma of nitroglycerin bioactivation and nitrate tolerance: News, views, and troubles
    • B. Mayer, and M. Beretta The enigma of nitroglycerin bioactivation and nitrate tolerance: news, views, and troubles Br J Pharmacol 155 2008 170 184
    • (2008) Br J Pharmacol , vol.155 , pp. 170-184
    • Mayer, B.1    Beretta, M.2
  • 15
    • 24744461677 scopus 로고    scopus 로고
    • An essential role for mitochondrial aldehyde dehydrogenase in nitroglycerin bioactivation
    • Z. Chen, M.W. Foster, J. Zhang, L. Mao, H.A. Rockman, and T. Kawamoto An essential role for mitochondrial aldehyde dehydrogenase in nitroglycerin bioactivation Proc Natl Acad Sci USA 102 2005 12159 12164
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12159-12164
    • Chen, Z.1    Foster, M.W.2    Zhang, J.3    Mao, L.4    Rockman, H.A.5    Kawamoto, T.6
  • 16
    • 79960231900 scopus 로고    scopus 로고
    • Site-directed mutagenesis of aldehyde dehydrogenase-2 suggests three distinct pathways of nitroglycerin biotransformation
    • M.V. Wenzl, M. Beretta, M. Griesberger, M. Russwurm, D. Koesling, and K. Schmidt Site-directed mutagenesis of aldehyde dehydrogenase-2 suggests three distinct pathways of nitroglycerin biotransformation Mol Pharmacol 80 2011 258 266
    • (2011) Mol Pharmacol , vol.80 , pp. 258-266
    • Wenzl, M.V.1    Beretta, M.2    Griesberger, M.3    Russwurm, M.4    Koesling, D.5    Schmidt, K.6
  • 18
    • 13444273181 scopus 로고    scopus 로고
    • Contribution of aldehyde dehydrogenase to mitochondrial bioactivation of nitroglycerin: Evidence for the activation of purified soluble guanylate cyclase through direct formation of nitric oxide
    • A. Kollau, A. Hofer, M. Russwurm, D. Koesling, W.M. Keung, and K. Schmidt Contribution of aldehyde dehydrogenase to mitochondrial bioactivation of nitroglycerin: evidence for the activation of purified soluble guanylate cyclase through direct formation of nitric oxide Biochem J 385 2005 769 777
    • (2005) Biochem J , vol.385 , pp. 769-777
    • Kollau, A.1    Hofer, A.2    Russwurm, M.3    Koesling, D.4    Keung, W.M.5    Schmidt, K.6
  • 19
    • 11144354818 scopus 로고    scopus 로고
    • Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance
    • K. Sydow, A. Daiber, M. Oelze, Z.P. Chen, M. August, and M. Wendt Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance J Clin Invest 113 2004 482 489
    • (2004) J Clin Invest , vol.113 , pp. 482-489
    • Sydow, K.1    Daiber, A.2    Oelze, M.3    Chen, Z.P.4    August, M.5    Wendt, M.6
  • 20
    • 23944518097 scopus 로고    scopus 로고
    • Heterozygous deficiency of manganese superoxide dismutase in mice (Mn-SOD+/-): A novel approach to assess the role of oxidative stress for the development of nitrate tolerance
    • A. Daiber, M. Oelze, S. Sulyok, M. Coldewey, E. Schulz, and N. Treiber Heterozygous deficiency of manganese superoxide dismutase in mice (Mn-SOD+/-): a novel approach to assess the role of oxidative stress for the development of nitrate tolerance Mol Pharmacol 68 2005 579 588
    • (2005) Mol Pharmacol , vol.68 , pp. 579-588
    • Daiber, A.1    Oelze, M.2    Sulyok, S.3    Coldewey, M.4    Schulz, E.5    Treiber, N.6
  • 22
    • 36448970474 scopus 로고    scopus 로고
    • Oxidative inhibition of the mitochondrial aldehyde dehydrogenase promotes nitroglycerin tolerance in human blood vessels
    • U. Hink, A. Daiber, N. Kayhan, J. Trischler, C. Kraatz, and M. Oelze Oxidative inhibition of the mitochondrial aldehyde dehydrogenase promotes nitroglycerin tolerance in human blood vessels J Am Coll Cardiol 50 2007 2226 2232
    • (2007) J Am Coll Cardiol , vol.50 , pp. 2226-2232
    • Hink, U.1    Daiber, A.2    Kayhan, N.3    Trischler, J.4    Kraatz, C.5    Oelze, M.6
  • 23
    • 46749093300 scopus 로고    scopus 로고
    • Inhibition of aldehyde dehydrogenase type 2 attenuates vasodilatory action of nitroglycerin in human veins
    • M.W. Huellner, S. Schrepfer, M. Weyand, H. Weiner, I. Wimplinger, and T. Eschenhagen Inhibition of aldehyde dehydrogenase type 2 attenuates vasodilatory action of nitroglycerin in human veins FASEB J 22 2008 2561 2568
    • (2008) FASEB J , vol.22 , pp. 2561-2568
    • Huellner, M.W.1    Schrepfer, S.2    Weyand, M.3    Weiner, H.4    Wimplinger, I.5    Eschenhagen, T.6
  • 24
    • 84883183849 scopus 로고    scopus 로고
    • Potent inhibition of aldehyde dehydrogenase-2 by diphenyleneiodonium: Focus on nitroglycerin bioactivation
    • R. Neubauer, A. Neubauer, G. Wölkart, C. Schwarzenegger, B. Lang, and K. Schmidt Potent inhibition of aldehyde dehydrogenase-2 by diphenyleneiodonium: focus on nitroglycerin bioactivation Mol Pharmacol 84 2013 407 414
    • (2013) Mol Pharmacol , vol.84 , pp. 407-414
    • Neubauer, R.1    Neubauer, A.2    Wölkart, G.3    Schwarzenegger, C.4    Lang, B.5    Schmidt, K.6
  • 25
    • 0030608336 scopus 로고    scopus 로고
    • Lack of inhibition of glyceryl trinitrate by diphenyleneiodonium in bovine coronary artery
    • I.S. De La Lande, T. Philp, I. Stafford, and J.D. Horowitz Lack of inhibition of glyceryl trinitrate by diphenyleneiodonium in bovine coronary artery Eur J Pharmacol 314 1996 347 350
    • (1996) Eur J Pharmacol , vol.314 , pp. 347-350
    • De La Lande, I.S.1    Philp, T.2    Stafford, I.3    Horowitz, J.D.4
  • 26
    • 0027267937 scopus 로고
    • Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase
    • C.F. Zheng, T.T. Wang, and H. Weiner Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase Alcohol Clin Exp Res 17 1993 828 831
    • (1993) Alcohol Clin Exp Res , vol.17 , pp. 828-831
    • Zheng, C.F.1    Wang, T.T.2    Weiner, H.3
  • 27
    • 49649123367 scopus 로고    scopus 로고
    • Bioactivation of nitroglycerin by purified mitochondrial and cytosolic aldehyde dehydrogenases
    • M. Beretta, K. Gruber, A. Kollau, M. Russwurm, D. Koesling, and W. Goessler Bioactivation of nitroglycerin by purified mitochondrial and cytosolic aldehyde dehydrogenases J Biol Chem 283 2008 17873 17880
    • (2008) J Biol Chem , vol.283 , pp. 17873-17880
    • Beretta, M.1    Gruber, K.2    Kollau, A.3    Russwurm, M.4    Koesling, D.5    Goessler, W.6
  • 29
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • M.W. Pfaffl A new mathematical model for relative quantification in real-time RT-PCR Nucl Acids Res 29 2001 2002 2007
    • (2001) Nucl Acids Res , vol.29 , pp. 2002-2007
    • Pfaffl, M.W.1
  • 30
    • 67749097943 scopus 로고    scopus 로고
    • Role of the general base Glu-268 in nitroglycerin bioactivation and superoxide formation by aldehyde dehydrogenase-2
    • M.V. Wenzl, M. Beretta, A.C.F. Gorren, A. Zeller, P.K. Baral, and K. Gruber Role of the general base Glu-268 in nitroglycerin bioactivation and superoxide formation by aldehyde dehydrogenase-2 J Biol Chem 284 2009 19878 19886
    • (2009) J Biol Chem , vol.284 , pp. 19878-19886
    • Wenzl, M.V.1    Beretta, M.2    Gorren, A.C.F.3    Zeller, A.4    Baral, P.K.5    Gruber, K.6
  • 31
    • 47249141931 scopus 로고    scopus 로고
    • Constitutive nitric oxide synthase activation is a significant route for nitroglycerin-mediated vasodilation
    • M.G. Bonini, K. Stadler, S. Sueli de Oliviera, J. Corbett, M. Dore, and J. Petranka Constitutive nitric oxide synthase activation is a significant route for nitroglycerin-mediated vasodilation Proc Natl Acad Sci USA 105 2008 8569 8574
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8569-8574
    • Bonini, M.G.1    Stadler, K.2    Sueli De Oliviera, S.3    Corbett, J.4    Dore, M.5    Petranka, J.6
  • 32
    • 0029938767 scopus 로고    scopus 로고
    • Characterization of 1H-[1,2,4]oxadiazolo[4,3-A]quinoxalin-1-one as a heme-Site inhibitor of nitric oxide-Sensitive guanylyl cyclase
    • A. Schrammel, S. Behrends, K. Schmidt, D. Koesling, and B. Mayer Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanylyl cyclase Mol Pharmacol 50 1996 1 5
    • (1996) Mol Pharmacol , vol.50 , pp. 1-5
    • Schrammel, A.1    Behrends, S.2    Schmidt, K.3    Koesling, D.4    Mayer, B.5
  • 33
    • 84856740599 scopus 로고    scopus 로고
    • Vascular bioactivation of nitroglycerin is catalyzed by cytosolic aldehyde dehydrogenase-2
    • M. Beretta, G. Wölkart, M. Schernthaner, M. Griesberger, R. Neubauer, and K. Schmidt Vascular bioactivation of nitroglycerin is catalyzed by cytosolic aldehyde dehydrogenase-2 Circ Res 110 2012 385 393
    • (2012) Circ Res , vol.110 , pp. 385-393
    • Beretta, M.1    Wölkart, G.2    Schernthaner, M.3    Griesberger, M.4    Neubauer, R.5    Schmidt, K.6
  • 34
    • 84886176772 scopus 로고    scopus 로고
    • In vitro organic nitrate bioactivation to nitric oxide by recombinant aldehyde dehydrogenase 3A1
    • S. Lin, N.A. Page, S.M. Fung, and H.L. Fung In vitro organic nitrate bioactivation to nitric oxide by recombinant aldehyde dehydrogenase 3A1 Nitric Oxide Biol Chem 35 2013 137 143
    • (2013) Nitric Oxide Biol Chem , vol.35 , pp. 137-143
    • Lin, S.1    Page, N.A.2    Fung, S.M.3    Fung, H.L.4
  • 35
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): Biochemical characterization and immunohistochemical localization in the cornea
    • A. Pappa, T. Estey, R. Manzer, D. Brown, and V. Vasiliou Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea Biochem J 376 2003 615 623
    • (2003) Biochem J , vol.376 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 37
    • 33645130053 scopus 로고    scopus 로고
    • Kv channels contribute to nitric oxide- and atrial natriuretic peptide-induced relaxation of a rat conduit artery
    • Y. Tanaka, G. Tang, K. Takizawa, K. Otsuka, M. Eghbali, and M. Song Kv channels contribute to nitric oxide- and atrial natriuretic peptide-induced relaxation of a rat conduit artery J Pharmacol Exp Ther 317 2006 341 354
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 341-354
    • Tanaka, Y.1    Tang, G.2    Takizawa, K.3    Otsuka, K.4    Eghbali, M.5    Song, M.6
  • 38
    • 9444221430 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial aldehyde dehydrogenase activity: A comparison of pentaerythritol tetranitrate with other organic nitrates
    • A. Daiber, M. Oelze, M. Coldewey, M. Bachschmid, P. Wenzel, and K. Sydow Oxidative stress and mitochondrial aldehyde dehydrogenase activity: a comparison of pentaerythritol tetranitrate with other organic nitrates Mol Pharmacol 66 2004 1372 1382
    • (2004) Mol Pharmacol , vol.66 , pp. 1372-1382
    • Daiber, A.1    Oelze, M.2    Coldewey, M.3    Bachschmid, M.4    Wenzel, P.5    Sydow, K.6
  • 39
    • 26244465889 scopus 로고    scopus 로고
    • Explaining the phenomenon of nitrate tolerance
    • T. Münzel, A. Daiber, and A. Mülsch Explaining the phenomenon of nitrate tolerance Circ Res 97 2005 618 628
    • (2005) Circ Res , vol.97 , pp. 618-628
    • Münzel, T.1    Daiber, A.2    Mülsch, A.3


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