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Volumn 55, Issue 1, 2013, Pages 58-63

Mitochondrial aldehyde dehydrogenase 2 activation and cardioprotection

Author keywords

Arrhythmia; Autophagy; Cardiac hypertrophy; Cardiac ischemia and reperfusion; Cardioprotective effects; Mitochondrial aldehyde dehydrogenase 2

Indexed keywords

1,3 BENZODIOXOLE DERIVATIVE; 4 HYDROXYNONENAL; ADENOSINE A2B RECEPTOR AGONIST; ADENOSINE A3 RECEPTOR AGONIST; ADENOSINE RECEPTOR STIMULATING AGENT; ALDEHYDE; ALDEHYDE DEHYDROGENASE ISOENZYME 2; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; N (1,3 BENZODIOXOL 5 YLMETHYL) 2,6 DICHLOROBENZAMIDE; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; SIRTUIN 3; UNCLASSIFIED DRUG;

EID: 84872725111     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2012.03.017     Document Type: Review
Times cited : (27)

References (83)
  • 1
    • 36849015926 scopus 로고    scopus 로고
    • Childhood body-mass index and the risk of coronary heart disease in adulthood
    • Baker J.L., Olsen L.W., Sorensen T.I. Childhood body-mass index and the risk of coronary heart disease in adulthood. N Engl J Med 2007, 357(23):2329-2337.
    • (2007) N Engl J Med , vol.357 , Issue.23 , pp. 2329-2337
    • Baker, J.L.1    Olsen, L.W.2    Sorensen, T.I.3
  • 2
    • 79960245269 scopus 로고    scopus 로고
    • Effect of early intensive multifactorial therapy on 5-year cardiovascular outcomes in individuals with type 2 diabetes detected by screening (ADDITION-Europe): a cluster-randomised trial
    • Griffin S.J., Borch-Johnsen K., Davies M.J., Khunti K., Rutten G.E., Sandbaek A., et al. Effect of early intensive multifactorial therapy on 5-year cardiovascular outcomes in individuals with type 2 diabetes detected by screening (ADDITION-Europe): a cluster-randomised trial. Lancet 2011, 378(9786):156-167.
    • (2011) Lancet , vol.378 , Issue.9786 , pp. 156-167
    • Griffin, S.J.1    Borch-Johnsen, K.2    Davies, M.J.3    Khunti, K.4    Rutten, G.E.5    Sandbaek, A.6
  • 3
    • 79751531393 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2011 update: a report from the American Heart Association
    • Roger V.L., Go A.S., Lloyd-Jones D.M., Adams R.J., Berry J.D., Brown T.M., et al. Heart disease and stroke statistics-2011 update: a report from the American Heart Association. Circulation 2011, 123(4):e18-e209.
    • (2011) Circulation , vol.123 , Issue.4
    • Roger, V.L.1    Go, A.S.2    Lloyd-Jones, D.M.3    Adams, R.J.4    Berry, J.D.5    Brown, T.M.6
  • 5
    • 58149302706 scopus 로고    scopus 로고
    • Time-dependent and ethanol-induced cardiac protection from ischemia mediated by mitochondrial translocation of εPKC and activation of aldehyde dehydrogenase 2
    • Churchill E.N., Disatnik M.H., Mochly-Rosen D. Time-dependent and ethanol-induced cardiac protection from ischemia mediated by mitochondrial translocation of εPKC and activation of aldehyde dehydrogenase 2. J Mol Cell Cardiol 2009, 46(2):278-284.
    • (2009) J Mol Cell Cardiol , vol.46 , Issue.2 , pp. 278-284
    • Churchill, E.N.1    Disatnik, M.H.2    Mochly-Rosen, D.3
  • 6
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion
    • Steinmetz C.G., Xie P., Weiner H., Hurley T.D. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 1997, 5(5):701-711.
    • (1997) Structure , vol.5 , Issue.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 7
    • 34247518100 scopus 로고    scopus 로고
    • Role of reactive oxygen species in myocardial remodeling
    • Zhang M., Shah A.M. Role of reactive oxygen species in myocardial remodeling. Curr Heart Fail Rep 2007, 4(1):26-30.
    • (2007) Curr Heart Fail Rep , vol.4 , Issue.1 , pp. 26-30
    • Zhang, M.1    Shah, A.M.2
  • 8
    • 73349085271 scopus 로고    scopus 로고
    • Beyond reactive oxygen species: aldehydes as arbitrators of alarm and adaptation
    • Hill B.G., Bhatnagar A. Beyond reactive oxygen species: aldehydes as arbitrators of alarm and adaptation. Circ Res 2009, 105(11):1044-1046.
    • (2009) Circ Res , vol.105 , Issue.11 , pp. 1044-1046
    • Hill, B.G.1    Bhatnagar, A.2
  • 9
    • 33846471592 scopus 로고    scopus 로고
    • Aldehyde metabolism in the cardiovascular system
    • Conklin D., Prough R., Bhatanagar A. Aldehyde metabolism in the cardiovascular system. Mol Biosyst 2007, 3(2):136-150.
    • (2007) Mol Biosyst , vol.3 , Issue.2 , pp. 136-150
    • Conklin, D.1    Prough, R.2    Bhatanagar, A.3
  • 10
    • 0019193338 scopus 로고
    • Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
    • Benedetti A., Comporti M., Esterbauer H. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim Biophys Acta 1980, 620(2):281-296.
    • (1980) Biochim Biophys Acta , vol.620 , Issue.2 , pp. 281-296
    • Benedetti, A.1    Comporti, M.2    Esterbauer, H.3
  • 11
    • 0035196175 scopus 로고    scopus 로고
    • Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart
    • Chen J., Henderson G.I., Freeman G.L. Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart. J Mol Cell Cardiol 2001, 33(11):1919-1927.
    • (2001) J Mol Cell Cardiol , vol.33 , Issue.11 , pp. 1919-1927
    • Chen, J.1    Henderson, G.I.2    Freeman, G.L.3
  • 12
    • 18044385349 scopus 로고    scopus 로고
    • Lipid peroxidation during ischemia depends on ischemia time in warm ischemia and reperfusion of rat liver
    • Fukai M., Hayashi T., Yokota R., Shimamura T., Suzuki T., Taniguchi M., et al. Lipid peroxidation during ischemia depends on ischemia time in warm ischemia and reperfusion of rat liver. Free Radic Biol Med 2005, 38(10):1372-1381.
    • (2005) Free Radic Biol Med , vol.38 , Issue.10 , pp. 1372-1381
    • Fukai, M.1    Hayashi, T.2    Yokota, R.3    Shimamura, T.4    Suzuki, T.5    Taniguchi, M.6
  • 13
    • 33747770049 scopus 로고    scopus 로고
    • Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes
    • Farout L., Mary J., Vinh J., Szweda L.I., Friguet B. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes. Arch Biochem Biophys 2006, 453(1):135-142.
    • (2006) Arch Biochem Biophys , vol.453 , Issue.1 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3    Szweda, L.I.4    Friguet, B.5
  • 14
    • 0033535948 scopus 로고    scopus 로고
    • Declines in mitochondrial respiration during cardiac reperfusion: age-dependent inactivation of alpha-ketoglutarate dehydrogenase
    • Lucas D.T., Szweda L.I. Declines in mitochondrial respiration during cardiac reperfusion: age-dependent inactivation of alpha-ketoglutarate dehydrogenase. Proc Natl Acad Sci U S A 1999, 96(12):6689-6693.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.12 , pp. 6689-6693
    • Lucas, D.T.1    Szweda, L.I.2
  • 15
    • 33749347262 scopus 로고    scopus 로고
    • Environmental cardiology: studying mechanistic links between pollution and heart disease
    • Bhatnagar A. Environmental cardiology: studying mechanistic links between pollution and heart disease. Circ Res 2006, 99(7):692-705.
    • (2006) Circ Res , vol.99 , Issue.7 , pp. 692-705
    • Bhatnagar, A.1
  • 16
    • 0020544348 scopus 로고
    • Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity
    • Goedde H.W., Agarwal D.P., Harada S., Meier-Tackmann D., Ruofu D., Bienzle U., et al. Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity. Am J Hum Genet 1983, 35(4):769-772.
    • (1983) Am J Hum Genet , vol.35 , Issue.4 , pp. 769-772
    • Goedde, H.W.1    Agarwal, D.P.2    Harada, S.3    Meier-Tackmann, D.4    Ruofu, D.5    Bienzle, U.6
  • 18
    • 24044510433 scopus 로고    scopus 로고
    • Disruption of the coenzyme binding site and dimer interface revealed in the crystal structure of mitochondrial aldehyde dehydrogenase "Asian" variant
    • Larson H.N., Weiner H., Hurley T.D. Disruption of the coenzyme binding site and dimer interface revealed in the crystal structure of mitochondrial aldehyde dehydrogenase "Asian" variant. J Biol Chem 2005, 280(34):30550-30556.
    • (2005) J Biol Chem , vol.280 , Issue.34 , pp. 30550-30556
    • Larson, H.N.1    Weiner, H.2    Hurley, T.D.3
  • 19
    • 34250333468 scopus 로고    scopus 로고
    • Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487
    • Larson H.N., Zhou J., Chen Z., Stamler J.S., Weiner H., Hurley T.D. Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487. J Biol Chem 2007, 282(17):12940-12950.
    • (2007) J Biol Chem , vol.282 , Issue.17 , pp. 12940-12950
    • Larson, H.N.1    Zhou, J.2    Chen, Z.3    Stamler, J.S.4    Weiner, H.5    Hurley, T.D.6
  • 20
    • 67649949078 scopus 로고    scopus 로고
    • Products of oxidative stress inhibit aldehyde oxidation and reduction pathways in dopamine catabolism yielding elevated levels of a reactive intermediate
    • Jinsmaa Y., Florang V.R., Rees J.N., Anderson D.G., Strack S., Doorn J.A. Products of oxidative stress inhibit aldehyde oxidation and reduction pathways in dopamine catabolism yielding elevated levels of a reactive intermediate. Chem Res Toxicol 2009, 22(5):835-841.
    • (2009) Chem Res Toxicol , vol.22 , Issue.5 , pp. 835-841
    • Jinsmaa, Y.1    Florang, V.R.2    Rees, J.N.3    Anderson, D.G.4    Strack, S.5    Doorn, J.A.6
  • 21
    • 32444448861 scopus 로고    scopus 로고
    • Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family
    • Vasiliou V., Nebert D.W. Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family. Hum Genomics 2005, 2(2):138-143.
    • (2005) Hum Genomics , vol.2 , Issue.2 , pp. 138-143
    • Vasiliou, V.1    Nebert, D.W.2
  • 22
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • Petersen D.R., Doorn J.A. Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic Biol Med 2004, 37(7):937-945.
    • (2004) Free Radic Biol Med , vol.37 , Issue.7 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 23
    • 38049088299 scopus 로고    scopus 로고
    • ALDH-2 deficiency increases cardiovascular oxidative stress-evidence for indirect antioxidative properties
    • Wenzel P., Muller J., Zurmeyer S., Schuhmacher S., Schulz E., Oelze M., et al. ALDH-2 deficiency increases cardiovascular oxidative stress-evidence for indirect antioxidative properties. Biochem Biophys Res Commun 2008, 367(1):137-143.
    • (2008) Biochem Biophys Res Commun , vol.367 , Issue.1 , pp. 137-143
    • Wenzel, P.1    Muller, J.2    Zurmeyer, S.3    Schuhmacher, S.4    Schulz, E.5    Oelze, M.6
  • 25
    • 0030077380 scopus 로고    scopus 로고
    • Distribution of messenger RNAs for aldehyde dehydrogenase 1, aldehyde dehydrogenase 2, and aldehyde dehydrogenase 5 in human tissues
    • Stewart M.J., Malek K., Crabb D.W. Distribution of messenger RNAs for aldehyde dehydrogenase 1, aldehyde dehydrogenase 2, and aldehyde dehydrogenase 5 in human tissues. J Investig Med 1996, 44(2):42-46.
    • (1996) J Investig Med , vol.44 , Issue.2 , pp. 42-46
    • Stewart, M.J.1    Malek, K.2    Crabb, D.W.3
  • 26
    • 84856740599 scopus 로고    scopus 로고
    • Vascular bioactivation of nitroglycerin is catalyzed by cytosolic aldehyde dehydrogenase-2
    • Beretta M., Wolkart G., Schernthaner M., Griesberger M., Neubauer R., Schmidt K., et al. Vascular bioactivation of nitroglycerin is catalyzed by cytosolic aldehyde dehydrogenase-2. Circ Res 2012, 110(3):385-393.
    • (2012) Circ Res , vol.110 , Issue.3 , pp. 385-393
    • Beretta, M.1    Wolkart, G.2    Schernthaner, M.3    Griesberger, M.4    Neubauer, R.5    Schmidt, K.6
  • 27
    • 76349110761 scopus 로고    scopus 로고
    • Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant
    • Perez-Miller S., Younus H., Vanam R., Chen C.H., Mochly-Rosen D., Hurley T.D. Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant. Nat Struct Mol Biol 2010, 17(2):159-164.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.2 , pp. 159-164
    • Perez-Miller, S.1    Younus, H.2    Vanam, R.3    Chen, C.H.4    Mochly-Rosen, D.5    Hurley, T.D.6
  • 28
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., Reimer K.A. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 1986, 74(5):1124-1136.
    • (1986) Circulation , vol.74 , Issue.5 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 29
    • 0026047960 scopus 로고
    • Protection against infarction afforded by preconditioning is mediated by A1 adenosine receptors in rabbit heart
    • Liu G.S., Thornton J., Van Winkle D.M., Stanley A.W., Olsson R.A., Downey J.M. Protection against infarction afforded by preconditioning is mediated by A1 adenosine receptors in rabbit heart. Circulation 1991, 84(1):350-356.
    • (1991) Circulation , vol.84 , Issue.1 , pp. 350-356
    • Liu, G.S.1    Thornton, J.2    Van Winkle, D.M.3    Stanley, A.W.4    Olsson, R.A.5    Downey, J.M.6
  • 30
    • 22144492968 scopus 로고    scopus 로고
    • Reperfusion-induced translocation of deltaPKC to cardiac mitochondria prevents pyruvate dehydrogenase reactivation
    • Churchill E.N., Murriel C.L., Chen C.H., Mochly-Rosen D., Szweda L.I. Reperfusion-induced translocation of deltaPKC to cardiac mitochondria prevents pyruvate dehydrogenase reactivation. Circ Res 2005, 97(1):78-85.
    • (2005) Circ Res , vol.97 , Issue.1 , pp. 78-85
    • Churchill, E.N.1    Murriel, C.L.2    Chen, C.H.3    Mochly-Rosen, D.4    Szweda, L.I.5
  • 31
    • 9144256765 scopus 로고    scopus 로고
    • Protein kinase Cdelta activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving BAD and the mitochondria
    • Murriel C.L., Churchill E., Inagaki K., Szweda L.I., Mochly-Rosen D. Protein kinase Cdelta activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving BAD and the mitochondria. J Biol Chem 2004, 279(46):47985-47991.
    • (2004) J Biol Chem , vol.279 , Issue.46 , pp. 47985-47991
    • Murriel, C.L.1    Churchill, E.2    Inagaki, K.3    Szweda, L.I.4    Mochly-Rosen, D.5
  • 32
    • 0141751749 scopus 로고    scopus 로고
    • Preconditioning the myocardium: from cellular physiology to clinical cardiology
    • Yellon D.M., Downey J.M. Preconditioning the myocardium: from cellular physiology to clinical cardiology. Physiol Rev 2003, 83(4):1113-1151.
    • (2003) Physiol Rev , vol.83 , Issue.4 , pp. 1113-1151
    • Yellon, D.M.1    Downey, J.M.2
  • 33
    • 0033607301 scopus 로고    scopus 로고
    • Cardioprotection from ischemia by a brief exposure to physiological levels of ethanol: role of epsilon protein kinase C
    • Chen C.H., Gray M.O., Mochly-Rosen D. Cardioprotection from ischemia by a brief exposure to physiological levels of ethanol: role of epsilon protein kinase C. Proc Natl Acad Sci U S A 1999, 96(22):12784-12789.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.22 , pp. 12784-12789
    • Chen, C.H.1    Gray, M.O.2    Mochly-Rosen, D.3
  • 34
    • 77956864883 scopus 로고    scopus 로고
    • Mitochondrial import of PKCepsilon is mediated by HSP90: a role in cardioprotection from ischaemia and reperfusion injury
    • Budas G.R., Churchill E.N., Disatnik M.H., Sun L., Mochly-Rosen D. Mitochondrial import of PKCepsilon is mediated by HSP90: a role in cardioprotection from ischaemia and reperfusion injury. Cardiovasc Res 2010, 88(1):83-92.
    • (2010) Cardiovasc Res , vol.88 , Issue.1 , pp. 83-92
    • Budas, G.R.1    Churchill, E.N.2    Disatnik, M.H.3    Sun, L.4    Mochly-Rosen, D.5
  • 35
    • 77649273950 scopus 로고    scopus 로고
    • Activation of aldehyde dehydrogenase 2 (ALDH2) confers cardioprotection in protein kinase C epsilon (PKCvarepsilon) knockout mice
    • Budas G.R., Disatnik M.H., Chen C.H., Mochly-Rosen D. Activation of aldehyde dehydrogenase 2 (ALDH2) confers cardioprotection in protein kinase C epsilon (PKCvarepsilon) knockout mice. J Mol Cell Cardiol 2010, 48(4):757-764.
    • (2010) J Mol Cell Cardiol , vol.48 , Issue.4 , pp. 757-764
    • Budas, G.R.1    Disatnik, M.H.2    Chen, C.H.3    Mochly-Rosen, D.4
  • 36
    • 84857628087 scopus 로고    scopus 로고
    • The role of SIRT3 in mitochondrial homeostasis and cardiac adaptation to hypertrophy and aging
    • Sack M.N. The role of SIRT3 in mitochondrial homeostasis and cardiac adaptation to hypertrophy and aging. J Mol Cell Cardiol 2012, 52(3):520-525.
    • (2012) J Mol Cell Cardiol , vol.52 , Issue.3 , pp. 520-525
    • Sack, M.N.1
  • 37
    • 79961032436 scopus 로고    scopus 로고
    • SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity
    • Lu Z., Bourdi M., Li J.H., Aponte A.M., Chen Y., Lombard D.B., et al. SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity. EMBO Rep 2011, 12(8):840-846.
    • (2011) EMBO Rep , vol.12 , Issue.8 , pp. 840-846
    • Lu, Z.1    Bourdi, M.2    Li, J.H.3    Aponte, A.M.4    Chen, Y.5    Lombard, D.B.6
  • 38
    • 84855757015 scopus 로고    scopus 로고
    • Acetylation-dependent regulation of mitochondrial ALDH2 activation by SIRT3 mediates acute ethanol-induced eNOS activation
    • Xue L., Xu F., Meng L., Wei S., Wang J., Hao P., et al. Acetylation-dependent regulation of mitochondrial ALDH2 activation by SIRT3 mediates acute ethanol-induced eNOS activation. FEBS Lett 2012, 586(2):137-142.
    • (2012) FEBS Lett , vol.586 , Issue.2 , pp. 137-142
    • Xue, L.1    Xu, F.2    Meng, L.3    Wei, S.4    Wang, J.5    Hao, P.6
  • 39
    • 77956173286 scopus 로고    scopus 로고
    • SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
    • Bao J., Scott I., Lu Z., Pang L., Dimond C.C., Gius D., et al. SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity. Free Radic Biol Med 2010, 49(7):1230-1237.
    • (2010) Free Radic Biol Med , vol.49 , Issue.7 , pp. 1230-1237
    • Bao, J.1    Scott, I.2    Lu, Z.3    Pang, L.4    Dimond, C.C.5    Gius, D.6
  • 40
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: therapeutic targets to treat diseases of aging
    • Milne J.C., Denu J.M. The Sirtuin family: therapeutic targets to treat diseases of aging. Curr Opin Chem Biol 2008, 12(1):11-17.
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.1 , pp. 11-17
    • Milne, J.C.1    Denu, J.M.2
  • 41
    • 3543029270 scopus 로고    scopus 로고
    • Ethanol and acetaldehyde in alcoholic cardiomyopathy: from bad to ugly en route to oxidative stress
    • Zhang X., Li S.Y., Brown R.A., Ren J. Ethanol and acetaldehyde in alcoholic cardiomyopathy: from bad to ugly en route to oxidative stress. Alcohol 2004, 32(3):175-186.
    • (2004) Alcohol , vol.32 , Issue.3 , pp. 175-186
    • Zhang, X.1    Li, S.Y.2    Brown, R.A.3    Ren, J.4
  • 42
    • 79956133768 scopus 로고    scopus 로고
    • Changes in heart rate variability associated with acute alcohol consumption: current knowledge and implications for practice and research
    • Romanowicz M., Schmidt J.E., Bostwick J.M., Mrazek D.A., Karpyak V.M. Changes in heart rate variability associated with acute alcohol consumption: current knowledge and implications for practice and research. Alcohol Clin Exp Res 2011, 35(6):1092-1105.
    • (2011) Alcohol Clin Exp Res , vol.35 , Issue.6 , pp. 1092-1105
    • Romanowicz, M.1    Schmidt, J.E.2    Bostwick, J.M.3    Mrazek, D.A.4    Karpyak, V.M.5
  • 43
    • 67649119660 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase-2 (ALDH2) ameliorates chronic alcohol ingestion-induced myocardial insulin resistance and endoplasmic reticulum stress
    • Li S.Y., Gilbert S.A., Li Q., Ren J. Aldehyde dehydrogenase-2 (ALDH2) ameliorates chronic alcohol ingestion-induced myocardial insulin resistance and endoplasmic reticulum stress. J Mol Cell Cardiol 2009, 47(2):247-255.
    • (2009) J Mol Cell Cardiol , vol.47 , Issue.2 , pp. 247-255
    • Li, S.Y.1    Gilbert, S.A.2    Li, Q.3    Ren, J.4
  • 44
    • 64249100372 scopus 로고    scopus 로고
    • Transgenic overexpression of aldehyde dehydrogenase-2 rescues chronic alcohol intake-induced myocardial hypertrophy and contractile dysfunction
    • Doser T.A., Turdi S., Thomas D.P., Epstein P.N., Li S.Y., Ren J. Transgenic overexpression of aldehyde dehydrogenase-2 rescues chronic alcohol intake-induced myocardial hypertrophy and contractile dysfunction. Circulation 2009, 119(14):1941-1949.
    • (2009) Circulation , vol.119 , Issue.14 , pp. 1941-1949
    • Doser, T.A.1    Turdi, S.2    Thomas, D.P.3    Epstein, P.N.4    Li, S.Y.5    Ren, J.6
  • 45
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132(1):27-42.
    • (2008) Cell , vol.132 , Issue.1 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 46
    • 41149116150 scopus 로고    scopus 로고
    • Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells
    • Hill B.G., Haberzettl P., Ahmed Y., Srivastava S., Bhatnagar A. Unsaturated lipid peroxidation-derived aldehydes activate autophagy in vascular smooth-muscle cells. Biochem J 2008, 410(3):525-534.
    • (2008) Biochem J , vol.410 , Issue.3 , pp. 525-534
    • Hill, B.G.1    Haberzettl, P.2    Ahmed, Y.3    Srivastava, S.4    Bhatnagar, A.5
  • 47
    • 84855371108 scopus 로고    scopus 로고
    • Inflammation, endoplasmic reticulum stress, autophagy, and the monocyte chemoattractant protein-1/CCR2 pathway
    • Kolattukudy P.E., Niu J. Inflammation, endoplasmic reticulum stress, autophagy, and the monocyte chemoattractant protein-1/CCR2 pathway. Circ Res 2012, 110(1):174-189.
    • (2012) Circ Res , vol.110 , Issue.1 , pp. 174-189
    • Kolattukudy, P.E.1    Niu, J.2
  • 48
    • 43949114864 scopus 로고    scopus 로고
    • Molecular mechanisms and physiological significance of autophagy during myocardial ischemia and reperfusion
    • Matsui Y., Kyoi S., Takagi H., Hsu C.P., Hariharan N., Ago T., et al. Molecular mechanisms and physiological significance of autophagy during myocardial ischemia and reperfusion. Autophagy 2008, 4(4):409-415.
    • (2008) Autophagy , vol.4 , Issue.4 , pp. 409-415
    • Matsui, Y.1    Kyoi, S.2    Takagi, H.3    Hsu, C.P.4    Hariharan, N.5    Ago, T.6
  • 49
    • 34147168105 scopus 로고    scopus 로고
    • Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy
    • Matsui Y., Takagi H., Qu X., Abdellatif M., Sakoda H., Asano T., et al. Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy. Circ Res 2007, 100(6):914-922.
    • (2007) Circ Res , vol.100 , Issue.6 , pp. 914-922
    • Matsui, Y.1    Takagi, H.2    Qu, X.3    Abdellatif, M.4    Sakoda, H.5    Asano, T.6
  • 51
    • 77951920370 scopus 로고    scopus 로고
    • The cardiac mitochondrion: nexus of stress
    • Baines C.P. The cardiac mitochondrion: nexus of stress. Annu Rev Physiol 2010, 72:61-80.
    • (2010) Annu Rev Physiol , vol.72 , pp. 61-80
    • Baines, C.P.1
  • 52
    • 70450180180 scopus 로고    scopus 로고
    • Inhibition of mitochondrial membrane permeability as a putative pharmacological target for cardioprotection
    • Morin D., Assaly R., Paradis S., Berdeaux A. Inhibition of mitochondrial membrane permeability as a putative pharmacological target for cardioprotection. Curr Med Chem 2009, 16(33):4382-4398.
    • (2009) Curr Med Chem , vol.16 , Issue.33 , pp. 4382-4398
    • Morin, D.1    Assaly, R.2    Paradis, S.3    Berdeaux, A.4
  • 53
    • 84859110698 scopus 로고    scopus 로고
    • The MPTP Status During Early Reoxygenation is Critical for Cardioprotection
    • Husainy M.A., Dickenson J.M., Galinanes M. The MPTP Status During Early Reoxygenation is Critical for Cardioprotection. J Surg Res 2010, 174(1):62-72.
    • (2010) J Surg Res , vol.174 , Issue.1 , pp. 62-72
    • Husainy, M.A.1    Dickenson, J.M.2    Galinanes, M.3
  • 54
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • Hunter D.R., Haworth R.A., Southard J.H. Relationship between configuration, function, and permeability in calcium-treated mitochondria. J Biol Chem 1976, 251(16):5069-5077.
    • (1976) J Biol Chem , vol.251 , Issue.16 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 55
    • 0036088518 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by the nonimmunosuppressive cyclosporin derivative NIM811
    • Waldmeier P.C., Feldtrauer J.J., Qian T., Lemasters J.J. Inhibition of the mitochondrial permeability transition by the nonimmunosuppressive cyclosporin derivative NIM811. Mol Pharmacol 2002, 62(1):22-29.
    • (2002) Mol Pharmacol , vol.62 , Issue.1 , pp. 22-29
    • Waldmeier, P.C.1    Feldtrauer, J.J.2    Qian, T.3    Lemasters, J.J.4
  • 56
    • 77955955395 scopus 로고    scopus 로고
    • A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection
    • Halestrap A.P. A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection. Biochem Soc Trans 2010, 38(4):841-860.
    • (2010) Biochem Soc Trans , vol.38 , Issue.4 , pp. 841-860
    • Halestrap, A.P.1
  • 57
    • 0037144409 scopus 로고    scopus 로고
    • Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A
    • Clarke S.J., McStay G.P., Halestrap A.P. Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A. J Biol Chem 2002, 277(38):34793-34799.
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 34793-34799
    • Clarke, S.J.1    McStay, G.P.2    Halestrap, A.P.3
  • 58
    • 0027381281 scopus 로고
    • On the involvement of a cyclosporin A sensitive mitochondrial pore in myocardial reperfusion injury
    • Duchen M.R., McGuinness O., Brown L.A., Crompton M. On the involvement of a cyclosporin A sensitive mitochondrial pore in myocardial reperfusion injury. Cardiovasc Res 1993, 27(10):1790-1794.
    • (1993) Cardiovasc Res , vol.27 , Issue.10 , pp. 1790-1794
    • Duchen, M.R.1    McGuinness, O.2    Brown, L.A.3    Crompton, M.4
  • 59
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • Griffiths E.J., Halestrap A.P. Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion. Biochem J 1995, 307(Pt. 1):93-98.
    • (1995) Biochem J , vol.307 , Issue.PART 1 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 60
    • 0035951823 scopus 로고    scopus 로고
    • + and is a causative event in the death of myocytes in postischemic reperfusion of the heart
    • + and is a causative event in the death of myocytes in postischemic reperfusion of the heart. J Biol Chem 2001, 276(4):2571-2575.
    • (2001) J Biol Chem , vol.276 , Issue.4 , pp. 2571-2575
    • Di Lisa, F.1    Menabo, R.2    Canton, M.3    Barile, M.4    Bernardi, P.5
  • 61
    • 0032988868 scopus 로고    scopus 로고
    • Reversal of permeability transition during recovery of hearts from ischemia and its enhancement by pyruvate
    • Kerr P.M., Suleiman M.S., Halestrap A.P. Reversal of permeability transition during recovery of hearts from ischemia and its enhancement by pyruvate. Am J Physiol 1999, 276(2 Pt. 2):H496-H502.
    • (1999) Am J Physiol , vol.276 , Issue.2 PART 2
    • Kerr, P.M.1    Suleiman, M.S.2    Halestrap, A.P.3
  • 62
    • 79955644151 scopus 로고    scopus 로고
    • Activation of mitochondrial aldehyde dehydrogenase 2 and inhibition of mitochondrial permeability transition pore involved in cardioprotection of ethanol postconditioning
    • Li Z.H., Jiang C.R., Xia M.L., Ye H.W., Guan S.D., Gao Q. Activation of mitochondrial aldehyde dehydrogenase 2 and inhibition of mitochondrial permeability transition pore involved in cardioprotection of ethanol postconditioning. Zhejiang Da Xue Xue Bao Yi Xue Ban 2010, 39(6):566-571.
    • (2010) Zhejiang Da Xue Xue Bao Yi Xue Ban , vol.39 , Issue.6 , pp. 566-571
    • Li, Z.H.1    Jiang, C.R.2    Xia, M.L.3    Ye, H.W.4    Guan, S.D.5    Gao, Q.6
  • 63
    • 48249109117 scopus 로고    scopus 로고
    • Effect of cyclosporine on reperfusion injury in acute myocardial infarction
    • Piot C., Croisille P., Staat P., Thibault H., Rioufol G., Mewton N., et al. Effect of cyclosporine on reperfusion injury in acute myocardial infarction. N Engl J Med 2008, 359(5):473-481.
    • (2008) N Engl J Med , vol.359 , Issue.5 , pp. 473-481
    • Piot, C.1    Croisille, P.2    Staat, P.3    Thibault, H.4    Rioufol, G.5    Mewton, N.6
  • 65
    • 0029866196 scopus 로고    scopus 로고
    • 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition
    • Kristal B.S., Park B.K., Yu B.P. 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition. J Biol Chem 1996, 271(11):6033-6038.
    • (1996) J Biol Chem , vol.271 , Issue.11 , pp. 6033-6038
    • Kristal, B.S.1    Park, B.K.2    Yu, B.P.3
  • 66
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines C.P., Kaiser R.A., Purcell N.H., Blair N.S., Osinska H., Hambleton M.A., et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005, 434(7033):658-662.
    • (2005) Nature , vol.434 , Issue.7033 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4    Osinska, H.5    Hambleton, M.A.6
  • 67
    • 15844404722 scopus 로고    scopus 로고
    • Biochemistry: a pore way to die
    • Halestrap A. Biochemistry: a pore way to die. Nature 2005, 434(7033):578-579.
    • (2005) Nature , vol.434 , Issue.7033 , pp. 578-579
    • Halestrap, A.1
  • 68
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T., Shimizu S., Watanabe T., Yamaguchi O., Otsu K., Yamagata H., et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005, 434(7033):652-658.
    • (2005) Nature , vol.434 , Issue.7033 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6
  • 69
    • 0032921371 scopus 로고    scopus 로고
    • Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart
    • Eaton P., Li J.M., Hearse D.J., Shattock M.J. Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart. Am J Physiol 1999, 276(3 Pt. 2):H935-H943.
    • (1999) Am J Physiol , vol.276 , Issue.3 PART 2
    • Eaton, P.1    Li, J.M.2    Hearse, D.J.3    Shattock, M.J.4
  • 70
    • 77957701709 scopus 로고    scopus 로고
    • The reduction of infarct size-forty years of research
    • Ferreira R. The reduction of infarct size-forty years of research. Rev Port Cardiol 2010, 29(6):1037-1053.
    • (2010) Rev Port Cardiol , vol.29 , Issue.6 , pp. 1037-1053
    • Ferreira, R.1
  • 72
    • 0031440184 scopus 로고    scopus 로고
    • Enzymology of ethanol and acetaldehyde metabolism in mammals
    • Riveros-Rosas H., Julian-Sanchez A., Pina E. Enzymology of ethanol and acetaldehyde metabolism in mammals. Arch Med Res 1997, 28(4):453-471.
    • (1997) Arch Med Res , vol.28 , Issue.4 , pp. 453-471
    • Riveros-Rosas, H.1    Julian-Sanchez, A.2    Pina, E.3
  • 73
    • 2442533169 scopus 로고    scopus 로고
    • Ischemic postconditioning: brief ischemia during reperfusion converts persistent ventricular fibrillation into regular rhythm
    • Galagudza M., Kurapeev D., Minasian S., Valen G., Vaage J. Ischemic postconditioning: brief ischemia during reperfusion converts persistent ventricular fibrillation into regular rhythm. Eur J Cardiothorac Surg 2004, 25(6):1006-1010.
    • (2004) Eur J Cardiothorac Surg , vol.25 , Issue.6 , pp. 1006-1010
    • Galagudza, M.1    Kurapeev, D.2    Minasian, S.3    Valen, G.4    Vaage, J.5
  • 74
    • 0030013497 scopus 로고    scopus 로고
    • Ventricular premature beat-driven intermittent restoration of coronary blood flow reduces the incidence of reperfusion-induced ventricular fibrillation in a cat model of regional ischemia
    • Na H.S., Kim Y.I., Yoon Y.W., Han H.C., Nahm S.H., Hong S.K. Ventricular premature beat-driven intermittent restoration of coronary blood flow reduces the incidence of reperfusion-induced ventricular fibrillation in a cat model of regional ischemia. Am Heart J 1996, 132(1 Pt. 1):78-83.
    • (1996) Am Heart J , vol.132 , Issue.1 PART 1 , pp. 78-83
    • Na, H.S.1    Kim, Y.I.2    Yoon, Y.W.3    Han, H.C.4    Nahm, S.H.5    Hong, S.K.6
  • 75
    • 21644460350 scopus 로고    scopus 로고
    • Myocardial ischemic postconditioning: a brief ischemia causes conversion of resistent reperfusion-induced ventricular fibrillation into the normal rhythm
    • Petrishchev N.N., Vlasov T.D., Galagudza M.M., Kurapeev D.I., Minasian S.M. Myocardial ischemic postconditioning: a brief ischemia causes conversion of resistent reperfusion-induced ventricular fibrillation into the normal rhythm. Ross Fiziol Zh Im I M Sechenova 2004, 90(9):1138-1144.
    • (2004) Ross Fiziol Zh Im I M Sechenova , vol.90 , Issue.9 , pp. 1138-1144
    • Petrishchev, N.N.1    Vlasov, T.D.2    Galagudza, M.M.3    Kurapeev, D.I.4    Minasian, S.M.5
  • 76
    • 35348995408 scopus 로고    scopus 로고
    • Preconditioning and postconditioning: innate cardioprotection from ischemia-reperfusion injury
    • Vinten-Johansen J., Zhao Z.Q., Jiang R., Zatta A.J., Dobson G.P. Preconditioning and postconditioning: innate cardioprotection from ischemia-reperfusion injury. J Appl Physiol 2007, 103(4):1441-1448.
    • (2007) J Appl Physiol , vol.103 , Issue.4 , pp. 1441-1448
    • Vinten-Johansen, J.1    Zhao, Z.Q.2    Jiang, R.3    Zatta, A.J.4    Dobson, G.P.5
  • 77
    • 0025939931 scopus 로고
    • Cellular electrophysiological basis for oxygen radical-induced arrhythmias. A patch-clamp study in guinea pig ventricular myocytes
    • Cerbai E., Ambrosio G., Porciatti F., Chiariello M., Giotti A., Mugelli A. Cellular electrophysiological basis for oxygen radical-induced arrhythmias. A patch-clamp study in guinea pig ventricular myocytes. Circulation 1991, 84(4):1773-1782.
    • (1991) Circulation , vol.84 , Issue.4 , pp. 1773-1782
    • Cerbai, E.1    Ambrosio, G.2    Porciatti, F.3    Chiariello, M.4    Giotti, A.5    Mugelli, A.6
  • 78
    • 77956631792 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase activation prevents reperfusion arrhythmias by inhibiting local renin release from cardiac mast cells
    • Koda K., Salazar-Rodriguez M., Corti F., Chan N.Y., Estephan R., Silver R.B., et al. Aldehyde dehydrogenase activation prevents reperfusion arrhythmias by inhibiting local renin release from cardiac mast cells. Circulation 2010, 122(8):771-781.
    • (2010) Circulation , vol.122 , Issue.8 , pp. 771-781
    • Koda, K.1    Salazar-Rodriguez, M.2    Corti, F.3    Chan, N.Y.4    Estephan, R.5    Silver, R.B.6
  • 79
    • 3042526150 scopus 로고    scopus 로고
    • Acetaldehyde induces histamine release from human airway mast cells to cause bronchoconstriction
    • Kawano T., Matsuse H., Kondo Y., Machida I., Saeki S., Tomari S., et al. Acetaldehyde induces histamine release from human airway mast cells to cause bronchoconstriction. Int Arch Allergy Immunol 2004, 134(3):233-239.
    • (2004) Int Arch Allergy Immunol , vol.134 , Issue.3 , pp. 233-239
    • Kawano, T.1    Matsuse, H.2    Kondo, Y.3    Machida, I.4    Saeki, S.5    Tomari, S.6
  • 80
    • 77957240605 scopus 로고    scopus 로고
    • Interaction between sensory C-fibers and cardiac mast cells in ischemia/reperfusion: activation of a local renin-angiotensin system culminating in severe arrhythmic dysfunction
    • Morrey C., Brazin J., Seyedi N., Corti F., Silver R.B., Levi R. Interaction between sensory C-fibers and cardiac mast cells in ischemia/reperfusion: activation of a local renin-angiotensin system culminating in severe arrhythmic dysfunction. J Pharmacol Exp Ther 2010, 335(1):76-84.
    • (2010) J Pharmacol Exp Ther , vol.335 , Issue.1 , pp. 76-84
    • Morrey, C.1    Brazin, J.2    Seyedi, N.3    Corti, F.4    Silver, R.B.5    Levi, R.6
  • 81
    • 0026034835 scopus 로고
    • Acetaldehyde metabolism in different aldehyde dehydrogenase-2 genotypes
    • Enomoto N., Takase S., Yasuhara M., Takada A. Acetaldehyde metabolism in different aldehyde dehydrogenase-2 genotypes. Alcohol Clin Exp Res 1991, 15(1):141-144.
    • (1991) Alcohol Clin Exp Res , vol.15 , Issue.1 , pp. 141-144
    • Enomoto, N.1    Takase, S.2    Yasuhara, M.3    Takada, A.4
  • 82
    • 32444440593 scopus 로고    scopus 로고
    • Mitochondrial aldehyde dehydrogenase-2 (ALDH2) Glu504Lys polymorphism contributes to the variation in efficacy of sublingual nitroglycerin
    • Li Y., Zhang D., Jin W., Shao C., Yan P., Xu C., et al. Mitochondrial aldehyde dehydrogenase-2 (ALDH2) Glu504Lys polymorphism contributes to the variation in efficacy of sublingual nitroglycerin. J Clin Invest 2006, 116(2):506-511.
    • (2006) J Clin Invest , vol.116 , Issue.2 , pp. 506-511
    • Li, Y.1    Zhang, D.2    Jin, W.3    Shao, C.4    Yan, P.5    Xu, C.6
  • 83
    • 9444221430 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial aldehyde dehydrogenase activity: a comparison of pentaerythritol tetranitrate with other organic nitrates
    • Daiber A., Oelze M., Coldewey M., Bachschmid M., Wenzel P., Sydow K., et al. Oxidative stress and mitochondrial aldehyde dehydrogenase activity: a comparison of pentaerythritol tetranitrate with other organic nitrates. Mol Pharmacol 2004, 66(6):1372-1382.
    • (2004) Mol Pharmacol , vol.66 , Issue.6 , pp. 1372-1382
    • Daiber, A.1    Oelze, M.2    Coldewey, M.3    Bachschmid, M.4    Wenzel, P.5    Sydow, K.6


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