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Volumn 44, Issue 6, 2008, Pages 1062-1071

Oxidoreductase regulation of Kv currents in rat ventricle

Author keywords

Glutaredoxin; K+ channels; Redox; Thioredoxin

Indexed keywords

1,3 BIS (2 CHLOROETHYL) 1 NITROSOUREA; AURANOFIN; DIAMIDE; DICHLOROACETIC ACID; GLUTAREDOXIN; INSULIN; OXIDOREDUCTASE; POTASSIUM CHANNEL; PROTEIN KINASE C INHIBITOR; PROTEIN TYROSINE KINASE; RETINOIC ACID; THIOREDOXIN; UREA DERIVATIVE;

EID: 44649115155     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2008.03.011     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0028824707 scopus 로고
    • Redox signaling and the control of cell growth and death
    • Powis G., Briehl M., and Oblong L. Redox signaling and the control of cell growth and death. Pharmacol Ther 68 1 (1995) 149-173
    • (1995) Pharmacol Ther , vol.68 , Issue.1 , pp. 149-173
    • Powis, G.1    Briehl, M.2    Oblong, L.3
  • 2
    • 0032100603 scopus 로고    scopus 로고
    • Redox signaling and the emerging therapeutic potential of thiol antioxidants
    • Sen C.K. Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem Pharmacol 55 (1998) 1747-1758
    • (1998) Biochem Pharmacol , vol.55 , pp. 1747-1758
    • Sen, C.K.1
  • 3
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget M.S.B., and Buttner M.J. Thiol-based regulatory switches. Annu Rev Genet 37 (2003) 91-121
    • (2003) Annu Rev Genet , vol.37 , pp. 91-121
    • Paget, M.S.B.1    Buttner, M.J.2
  • 4
    • 12844257477 scopus 로고    scopus 로고
    • Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins
    • Bigelow D.J., and Squier T.C. Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochim Biophys Acta 1703 (2005) 121-134
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 121-134
    • Bigelow, D.J.1    Squier, T.C.2
  • 5
    • 0034467411 scopus 로고    scopus 로고
    • Redox regulation by thioredoxin superfamily; protection against oxidative stress and aging
    • Tanaka T., Nakamura H., Nishiyama A., Hosoi F., Masutani H., Wada H., et al. Redox regulation by thioredoxin superfamily; protection against oxidative stress and aging. Free Radic Res 33 (2000) 851-855
    • (2000) Free Radic Res , vol.33 , pp. 851-855
    • Tanaka, T.1    Nakamura, H.2    Nishiyama, A.3    Hosoi, F.4    Masutani, H.5    Wada, H.6
  • 6
    • 0037056109 scopus 로고    scopus 로고
    • Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity
    • Shioji K., Kishimoto C., Nakamura H., Masutani H., Yuan Z., Oka S., et al. Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity. Circulation 106 (2002) 1403-1409
    • (2002) Circulation , vol.106 , pp. 1403-1409
    • Shioji, K.1    Kishimoto, C.2    Nakamura, H.3    Masutani, H.4    Yuan, Z.5    Oka, S.6
  • 7
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin. A key regulator of cardiovascular homeostasis
    • Yamawaki H., Jaendeler J., and Berk B.C. Thioredoxin. A key regulator of cardiovascular homeostasis. Circ Res. 93 (2003) 1029-1033
    • (2003) Circ Res. , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Jaendeler, J.2    Berk, B.C.3
  • 8
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér E.S., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267 (2000) 6102-6109
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arnér, E.S.1    Holmgren, A.2
  • 9
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren A., and Bjornstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol 252 (1995) 199-208
    • (1995) Methods Enzymol , vol.252 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 10
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G., and Montfort W.R. Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol 41 (2001) 261-295
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 11
    • 0036710563 scopus 로고    scopus 로고
    • Cell signaling and the glutathione redox system
    • Filomeni G., Rotilio G., and Ciriolo M.R. Cell signaling and the glutathione redox system. Biochem Pharmacol 64 (2002) 1057-1064
    • (2002) Biochem Pharmacol , vol.64 , pp. 1057-1064
    • Filomeni, G.1    Rotilio, G.2    Ciriolo, M.R.3
  • 12
    • 0036290861 scopus 로고    scopus 로고
    • Thioredoxin superfamily and thioredoxin-inducing agents
    • Hirota K., Nakamura H., Masutani H., and Yodoi J. Thioredoxin superfamily and thioredoxin-inducing agents. Ann N Y Acad Sci 957 (2002) 189-199
    • (2002) Ann N Y Acad Sci , vol.957 , pp. 189-199
    • Hirota, K.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 13
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S., Nanri H., Fernando M.R., and Minakami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J Biochem 116 (1994) 42-46
    • (1994) J Biochem , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 15
    • 1242318832 scopus 로고    scopus 로고
    • Differential regulation of the slow and rapid components of guinea pig cardiac delayed rectifier channels by hypoxia
    • Hool L.C. Differential regulation of the slow and rapid components of guinea pig cardiac delayed rectifier channels by hypoxia. J Physiol 554.3 (2003) 743-754
    • (2003) J Physiol , vol.554 3 , pp. 743-754
    • Hool, L.C.1
  • 16
    • 0036903347 scopus 로고    scopus 로고
    • + channels in rat ventricular myocytes
    • + channels in rat ventricular myocytes. J Mol Cell. Cardiol 34 (2002) 1623-1632
    • (2002) J Mol Cell. Cardiol , vol.34 , pp. 1623-1632
    • Rozanski, G.J.1    Xu, Z.2
  • 17
    • 3242752598 scopus 로고    scopus 로고
    • 2+ channel activity by phenylarsine oxide
    • 2+ channel activity by phenylarsine oxide. Br J Pharmacol 142 (2004) 797-807
    • (2004) Br J Pharmacol , vol.142 , pp. 797-807
    • Sims, C.1    Harvey, R.D.2
  • 19
    • 0042831502 scopus 로고    scopus 로고
    • Regulation of glutathione in cardiac myocytes
    • Li S., Li X., and Rozanski G.J. Regulation of glutathione in cardiac myocytes. J Mol Cell Cardiol 35 (2003) 1145-1152
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 1145-1152
    • Li, S.1    Li, X.2    Rozanski, G.J.3
  • 20
    • 0029006990 scopus 로고
    • Diamide: an oxidant probe for thiols
    • Kosower N.S., and Kosower E.M. Diamide: an oxidant probe for thiols. Methods Enzymol 251 (1995) 123-133
    • (1995) Methods Enzymol , vol.251 , pp. 123-133
    • Kosower, N.S.1    Kosower, E.M.2
  • 22
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J., and Arner E.S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31 11 (2001) 1287-1312
    • (2001) Free Radic Biol Med , vol.31 , Issue.11 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 23
    • 0032401496 scopus 로고    scopus 로고
    • The role of oxidative stress in the genesis of heart disease
    • Singal P.K., Khaper N., Palance V., and Kumar D. The role of oxidative stress in the genesis of heart disease. Cardiovasc Res 40 (1998) 426-432
    • (1998) Cardiovasc Res , vol.40 , pp. 426-432
    • Singal, P.K.1    Khaper, N.2    Palance, V.3    Kumar, D.4
  • 26
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R., and Jaken S. Protein kinase C signaling and oxidative stress. Free Radic Biol Med 28 (2000) 1349-1361
    • (2000) Free Radic Biol Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 27
    • 0347627268 scopus 로고    scopus 로고
    • Protein tyrosine kinase-dependent modulation of voltage-dependent potassium channels by genistein in rat cardiac ventricular myocytes
    • Gao Z., Lau C.P., Wong T.M., and Li G.R. Protein tyrosine kinase-dependent modulation of voltage-dependent potassium channels by genistein in rat cardiac ventricular myocytes. Cell Signal 16 (2004) 333-341
    • (2004) Cell Signal , vol.16 , pp. 333-341
    • Gao, Z.1    Lau, C.P.2    Wong, T.M.3    Li, G.R.4
  • 30
    • 0030807891 scopus 로고    scopus 로고
    • Dichloroacetate as metabolic therapy for myocardial ischemia and failure
    • Bersin R.M., and Stacpoole P.W. Dichloroacetate as metabolic therapy for myocardial ischemia and failure. Am Heart J 134 5 (1997) 841-855
    • (1997) Am Heart J , vol.134 , Issue.5 , pp. 841-855
    • Bersin, R.M.1    Stacpoole, P.W.2
  • 31
    • 0038677200 scopus 로고    scopus 로고
    • Differential modulation of glucose, lactate, and pyruvate oxidation by insulin and dichloroacetate in the rat heart
    • Lloyd S., Brocks C., and Chatham J.C. Differential modulation of glucose, lactate, and pyruvate oxidation by insulin and dichloroacetate in the rat heart. Am J Physiol Heart Circ Physiol 285 (2003) H163-H172
    • (2003) Am J Physiol Heart Circ Physiol , vol.285
    • Lloyd, S.1    Brocks, C.2    Chatham, J.C.3
  • 32
    • 0028136598 scopus 로고
    • Peroxovanadium compounds. A new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics
    • Posner B.J., Faure R., Burgess J.W., Bevan A.P., Lachance D., Zhang-Sun G., et al. Peroxovanadium compounds. A new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics. J Biol Chem 296 6 (1994) 4596-4604
    • (1994) J Biol Chem , vol.296 , Issue.6 , pp. 4596-4604
    • Posner, B.J.1    Faure, R.2    Burgess, J.W.3    Bevan, A.P.4    Lachance, D.5    Zhang-Sun, G.6
  • 33
    • 3042620174 scopus 로고    scopus 로고
    • Auranofin increases apoptosis and ischemia-reperfusion injury in the rat isolated heart
    • Venardos K., Harrison G., Headrick J., and Perkins A. Auranofin increases apoptosis and ischemia-reperfusion injury in the rat isolated heart. Clin Exp Pharmacol. Physiol. 31 (2004) 289-294
    • (2004) Clin Exp Pharmacol. Physiol. , vol.31 , pp. 289-294
    • Venardos, K.1    Harrison, G.2    Headrick, J.3    Perkins, A.4
  • 34
    • 0024314622 scopus 로고
    • The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid
    • Schallreuter K.U., and Wood J.M. The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid. Biochem Biophys Res Comm 160 (1989) 573-579
    • (1989) Biochem Biophys Res Comm , vol.160 , pp. 573-579
    • Schallreuter, K.U.1    Wood, J.M.2
  • 35
    • 0025062053 scopus 로고
    • The mechanism of action of the nitrosourea anti-tumor drugs on thioredoxin reductase, glutathione reductase and ribonucleotide reductase
    • Schallreuter K.U., Gleason F.K., and Wood J.M. The mechanism of action of the nitrosourea anti-tumor drugs on thioredoxin reductase, glutathione reductase and ribonucleotide reductase. Biochim Biophys Acta 1054 (1990) 14-20
    • (1990) Biochim Biophys Acta , vol.1054 , pp. 14-20
    • Schallreuter, K.U.1    Gleason, F.K.2    Wood, J.M.3
  • 36
    • 18844427352 scopus 로고    scopus 로고
    • S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism
    • Dalle-Donne I., Giustarini D., Colombo R., Milzani A., and Rossi R. S-glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism. Free Radic Biol Med 38 (2005) 1501-1510
    • (2005) Free Radic Biol Med , vol.38 , pp. 1501-1510
    • Dalle-Donne, I.1    Giustarini, D.2    Colombo, R.3    Milzani, A.4    Rossi, R.5
  • 37
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin A.T., Neubert H., Brennan J.P., and Eaton P. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc Natl Acad Sci 101 (2004) 17982-17989
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 17982-17989
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 38
    • 0042233494 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase modulates cytosolic redox status and contractile phenotype in adult cardiomyocytes
    • Jain M., Brenner D.A., Cui L., Lim C.C., Wang B., Pimentel D.R., et al. Glucose-6-phosphate dehydrogenase modulates cytosolic redox status and contractile phenotype in adult cardiomyocytes. Circ Res 93 (2003) e9-e16
    • (2003) Circ Res , vol.93
    • Jain, M.1    Brenner, D.A.2    Cui, L.3    Lim, C.C.4    Wang, B.5    Pimentel, D.R.6
  • 39
    • 0037384491 scopus 로고    scopus 로고
    • Radiation response of cells during altered protein thiol redox
    • Biaglow J.E., Ayene I.S., Koch C.J., Donahue J., Stamato T.D., et al. Radiation response of cells during altered protein thiol redox. Radiat Res 159 (2003) 484-494
    • (2003) Radiat Res , vol.159 , pp. 484-494
    • Biaglow, J.E.1    Ayene, I.S.2    Koch, C.J.3    Donahue, J.4    Stamato, T.D.5
  • 40
    • 1342267125 scopus 로고    scopus 로고
    • Increased myocardial dysfunction after ischemia-reperfusion in mice lacking glucose-6-phosphate dehydrogenase
    • Jain M., Cui L., Brenner D.A., Wang B., Handy D.E., Leopold J.A., et al. Increased myocardial dysfunction after ischemia-reperfusion in mice lacking glucose-6-phosphate dehydrogenase. Circulation 109 (2004) 898-903
    • (2004) Circulation , vol.109 , pp. 898-903
    • Jain, M.1    Cui, L.2    Brenner, D.A.3    Wang, B.4    Handy, D.E.5    Leopold, J.A.6
  • 42
    • 0142243372 scopus 로고    scopus 로고
    • Antioxidant properties of myocardial fuels
    • Mallet R.T., and Sun J. Antioxidant properties of myocardial fuels. Mol Cell Biochem 253 (2003) 103-111
    • (2003) Mol Cell Biochem , vol.253 , pp. 103-111
    • Mallet, R.T.1    Sun, J.2
  • 43
    • 25444529765 scopus 로고    scopus 로고
    • Molecular physiology of cardiac repolarization
    • Nerbonne J.M., and Kass R.S. Molecular physiology of cardiac repolarization. Physiol Rev 85 (2005) 1205-1253
    • (2005) Physiol Rev , vol.85 , pp. 1205-1253
    • Nerbonne, J.M.1    Kass, R.S.2
  • 44
    • 0036742183 scopus 로고    scopus 로고
    • Regulation of transient outward current in human atrial myocytes by protein tyrosine kinase pathway
    • Wang Y., Kumar R., Wagner M.B., Cheng J., Mishra M., and Joyner R.W. Regulation of transient outward current in human atrial myocytes by protein tyrosine kinase pathway. J Cardiovasc Electrophysiol 13 (2002) 927-935
    • (2002) J Cardiovasc Electrophysiol , vol.13 , pp. 927-935
    • Wang, Y.1    Kumar, R.2    Wagner, M.B.3    Cheng, J.4    Mishra, M.5    Joyner, R.W.6
  • 45
    • 0037107183 scopus 로고    scopus 로고
    • Phosphorylation-dependent and phosphorylation-independent modes of modulation of shaker family voltage-gated potassium channels by SRC family protein tyrosine kinases
    • Nitabach M.N., Llamas D.A., Thompson I.J., Collins K.A., and Holmes T.C. Phosphorylation-dependent and phosphorylation-independent modes of modulation of shaker family voltage-gated potassium channels by SRC family protein tyrosine kinases. J Neurosci 22 (2002) 7913-7922
    • (2002) J Neurosci , vol.22 , pp. 7913-7922
    • Nitabach, M.N.1    Llamas, D.A.2    Thompson, I.J.3    Collins, K.A.4    Holmes, T.C.5
  • 46
    • 0030473947 scopus 로고    scopus 로고
    • Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain
    • Holmes T.C., Fadool D.A., Ren R., and Levitan I.B. Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science 274 (1996) 2089-2091
    • (1996) Science , vol.274 , pp. 2089-2091
    • Holmes, T.C.1    Fadool, D.A.2    Ren, R.3    Levitan, I.B.4
  • 47
    • 33749485651 scopus 로고    scopus 로고
    • Tyrosine phosphatases epsilon and alpha perform specific and overlapping functions in regulation of voltage-gated potassium channels in Schwann cells
    • Tiran Z., Peretz A., Sines T., Shinder V., Sap J., Attali B., et al. Tyrosine phosphatases epsilon and alpha perform specific and overlapping functions in regulation of voltage-gated potassium channels in Schwann cells. Mol Biol Cell 17 (2006) 4330-4342
    • (2006) Mol Biol Cell , vol.17 , pp. 4330-4342
    • Tiran, Z.1    Peretz, A.2    Sines, T.3    Shinder, V.4    Sap, J.5    Attali, B.6
  • 48
    • 33645460750 scopus 로고    scopus 로고
    • ERK/MAPK regulates Kv4.2 potassium current by direct phosphorylation of the pore-forming subunit
    • Schrader L.A., Birnbaum S.G., Nadin B.M., Ren Y., Bui D., et al. ERK/MAPK regulates Kv4.2 potassium current by direct phosphorylation of the pore-forming subunit. Am J Physiol Cell Physiol 290 (2006) C852-C861
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Schrader, L.A.1    Birnbaum, S.G.2    Nadin, B.M.3    Ren, Y.4    Bui, D.5
  • 49
    • 18144383207 scopus 로고    scopus 로고
    • PTPs versus PTKs: the redox side of the coin
    • Chiarugi P. PTPs versus PTKs: the redox side of the coin. Free Radic Res 39 (2005) 353-364
    • (2005) Free Radic Res , vol.39 , pp. 353-364
    • Chiarugi, P.1


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