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Volumn 19, Issue 5, 2009, Pages 158-164

Aldehyde Dehydrogenase 2 in Cardiac Protection: A New Therapeutic Target?

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; ACETALDEHYDE; ALDA 1; ALDEHYDE; ALDEHYDE DEHYDROGENASE INHIBITOR; ALDEHYDE DEHYDROGENASE ISOENZYME 2; DISULFIRAM; GLYCERYL TRINITRATE; N (1,3 BENZODIOXOL 5 YLMETHYL) 2,6 DICHLOROBENZAMIDE; NITRATE; NITRIC OXIDE; NITROPRUSSIDE SODIUM; ORGANIC NITRATE; PROTEIN KINASE C EPSILON; UNCLASSIFIED DRUG;

EID: 71249147300     PISSN: 10501738     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcm.2009.09.003     Document Type: Review
Times cited : (108)

References (59)
  • 1
    • 85047680361 scopus 로고
    • Preconditioning of isolated rabbit cardiomyocytes: induction by metabolic stress and blockade by the adenosine antagonist SPT and calphostin C, a protein kinase C inhibitor
    • Armstrong S., Downey J.M., and Ganote C.E. Preconditioning of isolated rabbit cardiomyocytes: induction by metabolic stress and blockade by the adenosine antagonist SPT and calphostin C, a protein kinase C inhibitor. Cardiovasc Res 28 (1994) 72-77
    • (1994) Cardiovasc Res , vol.28 , pp. 72-77
    • Armstrong, S.1    Downey, J.M.2    Ganote, C.E.3
  • 2
    • 0000707453 scopus 로고
    • Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations
    • Arnold W.P., Mittal C.K., Katsuki S., and Murad F. Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations. Proc Natl Acad Sci U S A 74 (1977) 3203-3207
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 3203-3207
    • Arnold, W.P.1    Mittal, C.K.2    Katsuki, S.3    Murad, F.4
  • 3
    • 0037968275 scopus 로고    scopus 로고
    • Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria
    • Baines C.P., Song C.X., Zheng Y.T., et al. Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria. Circ Res 92 (2003) 873-880
    • (2003) Circ Res , vol.92 , pp. 873-880
    • Baines, C.P.1    Song, C.X.2    Zheng, Y.T.3
  • 4
    • 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., et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434 (2005) 658-662
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 5
    • 57649171121 scopus 로고    scopus 로고
    • Partially irreversible inactivation of mitochondrial aldehyde dehydrogenase by nitroglycerin
    • Beretta M., Sottler A., Schmidt K., et al. Partially irreversible inactivation of mitochondrial aldehyde dehydrogenase by nitroglycerin. J Biol Chem 283 (2008) 30735-30744
    • (2008) J Biol Chem , vol.283 , pp. 30735-30744
    • Beretta, M.1    Sottler, A.2    Schmidt, K.3
  • 6
    • 0029092913 scopus 로고
    • 4-Hydroxynonenal, a novel indicator of lipid peroxidation for reperfusion injury of the myocardium
    • Blasig I.E., Grune T., Schonheit K., et al. 4-Hydroxynonenal, a novel indicator of lipid peroxidation for reperfusion injury of the myocardium. Am J Physiol 269 (1995) H14-H22
    • (1995) Am J Physiol , vol.269
    • Blasig, I.E.1    Grune, T.2    Schonheit, K.3
  • 7
    • 33846244291 scopus 로고    scopus 로고
    • Preconditioning: a paradigm shift in the biology of myocardial ischemia
    • Bolli R. Preconditioning: a paradigm shift in the biology of myocardial ischemia. Am J Physiol Heart Circ Physiol 292 (2007) H19-H27
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Bolli, R.1
  • 8
    • 0001371023 scopus 로고
    • Direct evidence that oxygen-derived free radicals contribute to postischemic myocardial dysfunction in the intact dog
    • Bolli R., Jeroudi M.O., Patel B.S., et al. Direct evidence that oxygen-derived free radicals contribute to postischemic myocardial dysfunction in the intact dog. Proc Natl Acad Sci U S A 86 (1989) 4695-4699
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 4695-4699
    • Bolli, R.1    Jeroudi, M.O.2    Patel, B.S.3
  • 9
    • 0034965843 scopus 로고    scopus 로고
    • Protein kinase C-alpha and -epsilon modulate connexin-43 phosphorylation in human heart
    • Bowling N., Huang X., Sandusky G.E., et al. Protein kinase C-alpha and -epsilon modulate connexin-43 phosphorylation in human heart. J Mol Cell Cardiol 33 (2001) 789-798
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 789-798
    • Bowling, N.1    Huang, X.2    Sandusky, G.E.3
  • 10
    • 0023928805 scopus 로고
    • Mechanism of glyceryl trinitrate-induced vasodilation. I. Relationship between drug biotransformation, tissue cyclic GMP elevation and relaxation of rabbit aorta
    • Brien J.F., McLaughlin B.E., Kobus S.M., et al. Mechanism of glyceryl trinitrate-induced vasodilation. I. Relationship between drug biotransformation, tissue cyclic GMP elevation and relaxation of rabbit aorta. J Pharmacol Exp Ther 244 (1988) 322-327
    • (1988) J Pharmacol Exp Ther , vol.244 , pp. 322-327
    • Brien, J.F.1    McLaughlin, B.E.2    Kobus, S.M.3
  • 11
    • 33750024221 scopus 로고    scopus 로고
    • Bioactivation of nitroglycerin by the mitochondrial aldehyde dehydrogenase
    • Chen Z., and Stamler J.S. Bioactivation of nitroglycerin by the mitochondrial aldehyde dehydrogenase. Trends Cardiovasc Med 16 (2006) 259-265
    • (2006) Trends Cardiovasc Med , vol.16 , pp. 259-265
    • Chen, Z.1    Stamler, J.S.2
  • 12
    • 0035542854 scopus 로고    scopus 로고
    • Molecular transporters for peptides: delivery of a cardioprotective epsilonPKC agonist peptide into cells and intact ischemic heart using a transport system, R(7)
    • Chen L., Wright L.R., Chen C.H., et al. Molecular transporters for peptides: delivery of a cardioprotective epsilonPKC agonist peptide into cells and intact ischemic heart using a transport system, R(7). Chem Biol 8 (2001) 1123-1129
    • (2001) Chem Biol , vol.8 , pp. 1123-1129
    • Chen, L.1    Wright, L.R.2    Chen, C.H.3
  • 13
    • 0037062518 scopus 로고    scopus 로고
    • Identification of the enzymatic mechanism of nitroglycerin bioactivation
    • Chen Z., Zhang J., and Stamler J.S. Identification of the enzymatic mechanism of nitroglycerin bioactivation. Proc Natl Acad Sci U S A 99 (2002) 8306-8311
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 8306-8311
    • Chen, Z.1    Zhang, J.2    Stamler, J.S.3
  • 14
    • 24744461677 scopus 로고    scopus 로고
    • An essential role for mitochondrial aldehyde dehydrogenase in nitroglycerin bioactivation
    • Chen Z., Foster M.W., Zhang J., et al. An essential role for mitochondrial aldehyde dehydrogenase in nitroglycerin bioactivation. Proc Natl Acad Sci U S A 102 (2005) 12159-12164
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12159-12164
    • Chen, Z.1    Foster, M.W.2    Zhang, J.3
  • 15
    • 51749104191 scopus 로고    scopus 로고
    • Activation of aldehyde dehydrogenase-2 reduces ischemic damage to the heart
    • Chen C.H., Budas G.R., Churchill E.N., et al. Activation of aldehyde dehydrogenase-2 reduces ischemic damage to the heart. Science 321 (2008) 1493-1495
    • (2008) Science , vol.321 , pp. 1493-1495
    • Chen, C.H.1    Budas, G.R.2    Churchill, E.N.3
  • 16
    • 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., et al. Reperfusion-induced translocation of deltaPKC to cardiac mitochondria prevents pyruvate dehydrogenase reactivation. Circ Res 97 (2005) 78-85
    • (2005) Circ Res , vol.97 , pp. 78-85
    • Churchill, E.N.1    Murriel, C.L.2    Chen, C.H.3
  • 17
    • 58149302706 scopus 로고    scopus 로고
    • Time-dependent and ethanol-induced cardiac protection from ischemia mediated by mitochondrial translocation of varepsilonPKC and activation of aldehyde dehydrogenase 2
    • Churchill E.N., Disatnik M.H., and Mochly-Rosen D. Time-dependent and ethanol-induced cardiac protection from ischemia mediated by mitochondrial translocation of varepsilonPKC and activation of aldehyde dehydrogenase 2. J Mol Cell Cardiol 46 (2009) 278-284
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 278-284
    • Churchill, E.N.1    Disatnik, M.H.2    Mochly-Rosen, D.3
  • 18
    • 0027500478 scopus 로고
    • Estimation of the extent of lipid peroxidation in the ischemic and reperfused heart by monitoring lipid metabolic products with the aid of high-performance liquid chromatography
    • Cordis G.A., Maulik N., Bagchi D., et al. Estimation of the extent of lipid peroxidation in the ischemic and reperfused heart by monitoring lipid metabolic products with the aid of high-performance liquid chromatography. J Chromatogr 632 (1993) 97-103
    • (1993) J Chromatogr , vol.632 , pp. 97-103
    • Cordis, G.A.1    Maulik, N.2    Bagchi, D.3
  • 19
    • 31844443064 scopus 로고    scopus 로고
    • Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal
    • Doorn J.A., Hurley T.D., and Petersen D.R. Inhibition of human mitochondrial aldehyde dehydrogenase by 4-hydroxynon-2-enal and 4-oxonon-2-enal. Chem Res Toxicol 19 (2006) 102-110
    • (2006) Chem Res Toxicol , vol.19 , pp. 102-110
    • Doorn, J.A.1    Hurley, T.D.2    Petersen, D.R.3
  • 20
    • 13044274187 scopus 로고    scopus 로고
    • Sustained in vivo cardiac protection by a rationally designed peptide that causes epsilon protein kinase C translocation
    • Dorn Jr. G.W., Souroujon M.C., Liron T., et al. Sustained in vivo cardiac protection by a rationally designed peptide that causes epsilon protein kinase C translocation. Proc Natl Acad Sci U S A 96 (1999) 12798-12803
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 12798-12803
    • Dorn Jr., G.W.1    Souroujon, M.C.2    Liron, T.3
  • 21
    • 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., et al. Transgenic overexpression of aldehyde dehydrogenase-2 rescues chronic alcohol intake-induced myocardial hypertrophy and contractile dysfunction. Circulation 119 (2009) 1941-1949
    • (2009) Circulation , vol.119 , pp. 1941-1949
    • Doser, T.A.1    Turdi, S.2    Thomas, D.P.3
  • 22
    • 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., and Shattock M.J. Formation of 4-hydroxy-2-nonenal-modified proteins in ischemic rat heart. Am J Physiol 276 (1999) H935-H943
    • (1999) Am J Physiol , vol.276
    • Eaton, P.1    Li, J.M.2    Hearse, D.J.3    Shattock, M.J.4
  • 23
    • 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., et al. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes. Arch Biochem Biophys 453 (2006) 135-142
    • (2006) Arch Biochem Biophys , vol.453 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3
  • 24
    • 0020544348 scopus 로고
    • Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity
    • Goedde H.W., Agarwal D.P., Harada S., et al. Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity. Am J Hum Genet 35 (1983) 769-772
    • (1983) Am J Hum Genet , vol.35 , pp. 769-772
    • Goedde, H.W.1    Agarwal, D.P.2    Harada, S.3
  • 25
    • 46849092968 scopus 로고    scopus 로고
    • Nitrate-induced toxicity and preconditioning: a rationale for reconsidering the use of these drugs
    • Gori T., and Parker J.D. Nitrate-induced toxicity and preconditioning: a rationale for reconsidering the use of these drugs. J Am Coll Cardiol 52 (2008) 251-254
    • (2008) J Am Coll Cardiol , vol.52 , pp. 251-254
    • Gori, T.1    Parker, J.D.2
  • 26
    • 47849116981 scopus 로고    scopus 로고
    • The mechanism of nitrate-induced preconditioning
    • Gori T., Di Stolfo G., Dragoni S., et al. The mechanism of nitrate-induced preconditioning. Clin Hemorheol Microcirc 39 (2008) 191-196
    • (2008) Clin Hemorheol Microcirc , vol.39 , pp. 191-196
    • Gori, T.1    Di Stolfo, G.2    Dragoni, S.3
  • 27
    • 0030609162 scopus 로고    scopus 로고
    • A selective epsilon-protein kinase C antagonist inhibits protection of cardiac myocytes from hypoxia-induced cell death
    • Gray M.O., Karliner J.S., and Mochly-Rosen D. A selective epsilon-protein kinase C antagonist inhibits protection of cardiac myocytes from hypoxia-induced cell death. J Biol Chem 272 (1997) 30945-30951
    • (1997) J Biol Chem , vol.272 , pp. 30945-30951
    • Gray, M.O.1    Karliner, J.S.2    Mochly-Rosen, D.3
  • 28
    • 0019443140 scopus 로고
    • Relationship between cyclic guanosine 3′:5′-monophosphate formation and relaxation of coronary arterial smooth muscle by glyceryl trinitrate, nitroprusside, nitrite and nitric oxide: effects of methylene blue and methemoglobin
    • Gruetter C.A., Gruetter D.Y., Lyon J.E., et al. Relationship between cyclic guanosine 3′:5′-monophosphate formation and relaxation of coronary arterial smooth muscle by glyceryl trinitrate, nitroprusside, nitrite and nitric oxide: effects of methylene blue and methemoglobin. J Pharmacol Exp Ther 219 (1981) 181-186
    • (1981) J Pharmacol Exp Ther , vol.219 , pp. 181-186
    • Gruetter, C.A.1    Gruetter, D.Y.2    Lyon, J.E.3
  • 29
    • 0037698600 scopus 로고    scopus 로고
    • Cardiac overexpression of alcohol dehydrogenase exacerbates cardiac contractile dysfunction, lipid peroxidation, and protein damage after chronic ethanol ingestion
    • Hintz K.K., Relling D.P., Saari J.T., et al. Cardiac overexpression of alcohol dehydrogenase exacerbates cardiac contractile dysfunction, lipid peroxidation, and protein damage after chronic ethanol ingestion. Alcohol Clin Exp Res 27 (2003) 1090-1098
    • (2003) Alcohol Clin Exp Res , vol.27 , pp. 1090-1098
    • Hintz, K.K.1    Relling, D.P.2    Saari, J.T.3
  • 30
    • 0242442127 scopus 로고    scopus 로고
    • Inhibition of delta-protein kinase C protects against reperfusion injury of the ischemic heart in vivo
    • Inagaki K., Chen L., Ikeno F., et al. Inhibition of delta-protein kinase C protects against reperfusion injury of the ischemic heart in vivo. Circulation 108 (2003) 2304-2307
    • (2003) Circulation , vol.108 , pp. 2304-2307
    • Inagaki, K.1    Chen, L.2    Ikeno, F.3
  • 31
    • 33749670149 scopus 로고    scopus 로고
    • Mitochondrial PKC epsilon and mitochondrial ATP-sensitive K+ channel copurify and coreconstitute to form a functioning signaling module in proteoliposomes
    • Jaburek M., Costa A.D., Burton J.R., et al. Mitochondrial PKC epsilon and mitochondrial ATP-sensitive K+ channel copurify and coreconstitute to form a functioning signaling module in proteoliposomes. Circ Res 99 (2006) 878-883
    • (2006) Circ Res , vol.99 , pp. 878-883
    • Jaburek, M.1    Costa, A.D.2    Burton, J.R.3
  • 32
    • 0029866196 scopus 로고    scopus 로고
    • 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition
    • Kristal B.S., Park B.K., and Yu B.P. 4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition. J Biol Chem 271 (1996) 6033-6038
    • (1996) J Biol Chem , vol.271 , pp. 6033-6038
    • Kristal, B.S.1    Park, B.K.2    Yu, B.P.3
  • 33
    • 71249142058 scopus 로고    scopus 로고
    • Male-female differences in post translational modifications of mitochondrial proteins
    • Lagranha C.J., Steenbergen C., and Murphy E. Male-female differences in post translational modifications of mitochondrial proteins. FASEB J 23 (2009) 508.1
    • (2009) FASEB J , vol.23
    • Lagranha, C.J.1    Steenbergen, C.2    Murphy, E.3
  • 34
    • 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., et al. Mitochondrial aldehyde dehydrogenase-2 (ALDH2) Glu504Lys polymorphism contributes to the variation in efficacy of sublingual nitroglycerin. J Clin Invest 116 (2006) 506-511
    • (2006) J Clin Invest , vol.116 , pp. 506-511
    • Li, Y.1    Zhang, D.2    Jin, W.3
  • 35
    • 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., et al. Protection against infarction afforded by preconditioning is mediated by A1 adenosine receptors in rabbit heart. Circulation 84 (1991) 350-356
    • (1991) Circulation , vol.84 , pp. 350-356
    • Liu, G.S.1    Thornton, J.2    Van Winkle, D.M.3
  • 36
    • 0032884872 scopus 로고    scopus 로고
    • Protein kinase C-epsilon is responsible for the protection of preconditioning in rabbit cardiomyocytes
    • Liu G.S., Cohen M.V., Mochly-Rosen D., and Downey J.M. Protein kinase C-epsilon is responsible for the protection of preconditioning in rabbit cardiomyocytes. J Mol Cell Cardiol 31 (1999) 1937-1948
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1937-1948
    • Liu, G.S.1    Cohen, M.V.2    Mochly-Rosen, D.3    Downey, J.M.4
  • 37
    • 24144454139 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 2 plays a role in the bioactivation of nitroglycerin in humans
    • Mackenzie I.S., Maki-Petaja K.M., McEniery C.M., et al. Aldehyde dehydrogenase 2 plays a role in the bioactivation of nitroglycerin in humans. Arterioscler Thromb Vasc Biol 25 (2005) 1891-1895
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 1891-1895
    • Mackenzie, I.S.1    Maki-Petaja, K.M.2    McEniery, C.M.3
  • 38
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: a theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 268 (1995) 247-251
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 39
    • 0025883342 scopus 로고
    • Nitric oxide: physiology, pathophysiology, and pharmacology
    • Moncada S., Palmer R.M., and Higgs E.A. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 43 (1991) 109-142
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 40
    • 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., et al. Protein kinase Cdelta activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving BAD and the mitochondria. J Biol Chem 279 (2004) 47985-47991
    • (2004) J Biol Chem , vol.279 , pp. 47985-47991
    • Murriel, C.L.1    Churchill, E.2    Inagaki, K.3
  • 41
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., and Reimer K.A. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74 (1986) 1124-1136
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 42
    • 0032861874 scopus 로고    scopus 로고
    • Long-term nitrate use may be deleterious in ischemic heart disease: a study using the databases from two large-scale postinfarction studies. Multicenter Myocardial Ischemia Research Group
    • Nakamura Y., Moss A.J., Brown M.W., et al. Long-term nitrate use may be deleterious in ischemic heart disease: a study using the databases from two large-scale postinfarction studies. Multicenter Myocardial Ischemia Research Group. Am Heart J 138 (1999) 577-585
    • (1999) Am Heart J , vol.138 , pp. 577-585
    • Nakamura, Y.1    Moss, A.J.2    Brown, M.W.3
  • 43
    • 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., et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434 (2005) 652-658
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3
  • 44
    • 4744359912 scopus 로고    scopus 로고
    • Cytochrome c oxidase subunit IV as a marker of protein kinase Cepsilon function in neonatal cardiac myocytes: implications for cytochrome c oxidase activity
    • Ogbi M., Chew C.S., Pohl J., et al. Cytochrome c oxidase subunit IV as a marker of protein kinase Cepsilon function in neonatal cardiac myocytes: implications for cytochrome c oxidase activity. Biochem J 382 (2004) 923-932
    • (2004) Biochem J , vol.382 , pp. 923-932
    • Ogbi, M.1    Chew, C.S.2    Pohl, J.3
  • 45
    • 64249093838 scopus 로고    scopus 로고
    • Mechanistic insights into nitrite-induced cardioprotection using an integrated metabolomic/proteomic approach
    • Perlman D.H., Bauer S.M., Ashrafian H., et al. Mechanistic insights into nitrite-induced cardioprotection using an integrated metabolomic/proteomic approach. Circ Res 104 (2009) 796-804
    • (2009) Circ Res , vol.104 , pp. 796-804
    • Perlman, D.H.1    Bauer, S.M.2    Ashrafian, H.3
  • 46
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • Petersen D.R., and Doorn J.A. Reactions of 4-hydroxynonenal with proteins and cellular targets. Free Radic Biol Med 37 (2004) 937-945
    • (2004) Free Radic Biol Med , vol.37 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 47
    • 0030872474 scopus 로고    scopus 로고
    • Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity
    • Ping P., Zhang J., Qiu Y., et al. Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity. Circ Res 81 (1997) 404-414
    • (1997) Circ Res , vol.81 , pp. 404-414
    • Ping, P.1    Zhang, J.2    Qiu, Y.3
  • 48
    • 0034141455 scopus 로고    scopus 로고
    • Activation of mitochondrial ATP-dependent potassium channels by nitric oxide
    • Sasaki N., Sato T., Ohler A., et al. Activation of mitochondrial ATP-dependent potassium channels by nitric oxide. Circulation 101 (2000) 439-445
    • (2000) Circulation , vol.101 , pp. 439-445
    • Sasaki, N.1    Sato, T.2    Ohler, A.3
  • 49
    • 0036023643 scopus 로고    scopus 로고
    • Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts
    • Saurin A.T., Pennington D.J., Raat N.J., et al. Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts. Cardiovasc Res 55 (2002) 672-680
    • (2002) Cardiovasc Res , vol.55 , pp. 672-680
    • Saurin, A.T.1    Pennington, D.J.2    Raat, N.J.3
  • 51
    • 0031761325 scopus 로고    scopus 로고
    • Peptide modulators of protein-protein interactions in intracellular signaling
    • Souroujon M.C., and Mochly-Rosen D. Peptide modulators of protein-protein interactions in intracellular signaling. Nat Biotechnol 16 (1998) 919-924
    • (1998) Nat Biotechnol , vol.16 , pp. 919-924
    • Souroujon, M.C.1    Mochly-Rosen, D.2
  • 52
    • 11144354818 scopus 로고    scopus 로고
    • Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance and cross-tolerance
    • Sydow K., Daiber A., Oelze M., et al. Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance and cross-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
  • 53
    • 0022353721 scopus 로고
    • Erythrocyte aldehyde dehydrogenase and disulfiram-like side effects of hypoglycemics and antianginals
    • Towell J., Garthwaite T., and Wang R. Erythrocyte aldehyde dehydrogenase and disulfiram-like side effects of hypoglycemics and antianginals. Alcohol Clin Exp Res 9 (1985) 438-442
    • (1985) Alcohol Clin Exp Res , vol.9 , pp. 438-442
    • Towell, J.1    Garthwaite, T.2    Wang, R.3
  • 54
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K., and Stadtman E.R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc Natl Acad Sci U S A 89 (1992) 4544-4548
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 55
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction
    • Uchida K., and Stadtman E.R. Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction. J Biol Chem 268 (1993) 6388-6393
    • (1993) J Biol Chem , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 56
    • 32444448861 scopus 로고    scopus 로고
    • Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family
    • Vasiliou V., and Nebert D.W. Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family. Hum Genomics 2 (2005) 138-143
    • (2005) Hum Genomics , vol.2 , pp. 138-143
    • Vasiliou, V.1    Nebert, D.W.2
  • 57
    • 0034534311 scopus 로고    scopus 로고
    • Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism
    • Vasiliou V., Pappa A., and Petersen D.R. Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chem Biol Interact 129 (2000) 1-19
    • (2000) Chem Biol Interact , vol.129 , pp. 1-19
    • Vasiliou, V.1    Pappa, A.2    Petersen, D.R.3
  • 58
    • 0035933389 scopus 로고    scopus 로고
    • Protein kinase C epsilon-Src modules direct signal transduction in nitric oxide-induced cardioprotection: complex formation as a means for cardioprotective signaling
    • Vondriska T.M., Zhang J., Song C., et al. Protein kinase C epsilon-Src modules direct signal transduction in nitric oxide-induced cardioprotection: complex formation as a means for cardioprotective signaling. Circ Res 88 (2001) 1306-1313
    • (2001) Circ Res , vol.88 , pp. 1306-1313
    • Vondriska, T.M.1    Zhang, J.2    Song, C.3
  • 59
    • 0028348870 scopus 로고
    • Preconditioning protects ischemic rabbit heart by protein kinase C activation
    • Ytrehus K., Liu Y., and Downey J.M. Preconditioning protects ischemic rabbit heart by protein kinase C activation. Am J Physiol 266 (1994) H1145-H1152
    • (1994) Am J Physiol , vol.266
    • Ytrehus, K.1    Liu, Y.2    Downey, J.M.3


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