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Volumn 77, Issue 1, 2008, Pages 107-117

Pro-oxidant effect of transforming growth factor-β1 mediates contractile dysfunction in rat ventricular myocytes

Author keywords

Glutathione; NAD(P)H oxidase; Oxidative stress; Redox; TGF

Indexed keywords

ACETYLCYSTEINE; CELL PROTEIN; GLUTATHIONE; GLUTATHIONE REDUCTASE; REACTIVE OXYGEN METABOLITE; SCAVENGER; TRANSFORMING GROWTH FACTOR BETA1;

EID: 38849104982     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvm022     Document Type: Article
Times cited : (30)

References (43)
  • 2
    • 0034083227 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiovascular diseases
    • Dhalla NS, Temsah RM, Netticadan T. Role of oxidative stress in cardiovascular diseases. J Hypertens 2000;18:655-673.
    • (2000) J Hypertens , vol.18 , pp. 655-673
    • Dhalla, N.S.1    Temsah, R.M.2    Netticadan, T.3
  • 3
    • 0034733807 scopus 로고    scopus 로고
    • Redox-dependent signal transduction
    • Finkel T. Redox-dependent signal transduction. FEBS Lett 2000;476:52-54.
    • (2000) FEBS Lett , vol.476 , pp. 52-54
    • Finkel, T.1
  • 4
    • 0037204990 scopus 로고    scopus 로고
    • Signal transduction by the TGF-β1 superfamily
    • Attisano L, Wrana JL. Signal transduction by the TGF-β1 superfamily. Science 2002;296:1646-1647.
    • (2002) Science , vol.296 , pp. 1646-1647
    • Attisano, L.1    Wrana, J.L.2
  • 5
    • 0026841119 scopus 로고
    • Reduction of glutathione is associated with growth restriction and enlargement of bovine pulmonary artery endothelial cells produced by transforming growth factorβ1
    • White AC, Das SK, Fanburg BL. Reduction of glutathione is associated with growth restriction and enlargement of bovine pulmonary artery endothelial cells produced by transforming growth factorβ1. Am J Respir Cell Mol Biol 1992;6:364-368.
    • (1992) Am J Respir Cell Mol Biol , vol.6 , pp. 364-368
    • White, A.C.1    Das, S.K.2    Fanburg, B.L.3
  • 6
    • 0031280268 scopus 로고    scopus 로고
    • Transforming growth factor-β1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: Transcriptional effect on the GSH rate-limiting enzyme γ-glutamylcysteine synthetase
    • Arsalane K, Dubois CM, Muanza T, Begin R, Boudreau F, Asselin C et al. Transforming growth factor-β1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: transcriptional effect on the GSH rate-limiting enzyme γ-glutamylcysteine synthetase. Am J Respir Cell Mol Biol 1997;17:599-607.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 599-607
    • Arsalane, K.1    Dubois, C.M.2    Muanza, T.3    Begin, R.4    Boudreau, F.5    Asselin, C.6
  • 7
    • 0030817668 scopus 로고    scopus 로고
    • Cycloheximide prevents apoptosis, reactive oxygen species production, and glutathione depletion induced by transforming growth factor β in fetal rat hepatocytes in primary culture
    • Sanchez A, Alvarez AM, Benito M, Fabregat I. Cycloheximide prevents apoptosis, reactive oxygen species production, and glutathione depletion induced by transforming growth factor β in fetal rat hepatocytes in primary culture. Hepatology 1997;26:935-943.
    • (1997) Hepatology , vol.26 , pp. 935-943
    • Sanchez, A.1    Alvarez, A.M.2    Benito, M.3    Fabregat, I.4
  • 8
    • 27644456575 scopus 로고    scopus 로고
    • NAD(P)H oxidase 4 mediates transforming growth factor-β1-induced differentiation of cardiac fibroblasts into myofibroblasts
    • Cucoranu I, Clempus R, Dikalova A, Phelan PJ, Ariyan S, Dikalov S et al. NAD(P)H oxidase 4 mediates transforming growth factor-β1-induced differentiation of cardiac fibroblasts into myofibroblasts. Circ Res 2005;97:900-907.
    • (2005) Circ Res , vol.97 , pp. 900-907
    • Cucoranu, I.1    Clempus, R.2    Dikalova, A.3    Phelan, P.J.4    Ariyan, S.5    Dikalov, S.6
  • 9
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology disease
    • Griendling KK, Sorescu D, Ushio-Fukai M. NAD(P)H oxidase: role in cardiovascular biology disease. Circ Res 2000;86:494-501.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 11
    • 0035058207 scopus 로고    scopus 로고
    • Alteration of antioxidants during the progression of heart disease in streptozotocin-induced diabetic rats
    • Doi K, Sawada F, Toda G, Yamachika S, Seto S, Urata Y et al. Alteration of antioxidants during the progression of heart disease in streptozotocin-induced diabetic rats. Free Radic Res 2001;34:251- 261.
    • (2001) Free Radic Res , vol.34 , pp. 251-261
    • Doi, K.1    Sawada, F.2    Toda, G.3    Yamachika, S.4    Seto, S.5    Urata, Y.6
  • 12
    • 0036645337 scopus 로고    scopus 로고
    • Transforming growth factor function blocking prevents myocardial fibrosis and diastolic dysfunction in pressure-overloaded rats
    • Kuwahara F, Kai H, Tokuda K, Kai M, Takeshita A, Egashira K et al. Transforming growth factor function blocking prevents myocardial fibrosis and diastolic dysfunction in pressure-overloaded rats. Circulation 2002;106:130-135.
    • (2002) Circulation , vol.106 , pp. 130-135
    • Kuwahara, F.1    Kai, H.2    Tokuda, K.3    Kai, M.4    Takeshita, A.5    Egashira, K.6
  • 13
    • 21044435626 scopus 로고    scopus 로고
    • Postinfarction gene therapy against transforming growth factor-β signal modulates infarct tissue dynamics and attenuates left ventricular remodeling and heart failure
    • Okada H, Takemura G, Kosai K, Li Y, Takahashi T, Esaki M et al. Postinfarction gene therapy against transforming growth factor-β signal modulates infarct tissue dynamics and attenuates left ventricular remodeling and heart failure. Circulation 2005;111:2430-2437.
    • (2005) Circulation , vol.111 , pp. 2430-2437
    • Okada, H.1    Takemura, G.2    Kosai, K.3    Li, Y.4    Takahashi, T.5    Esaki, M.6
  • 14
    • 0042831502 scopus 로고    scopus 로고
    • Regulation of glutathione in cardiac myocytes
    • Li S, Li X, Rozanski GJ. Regulation of glutathione in cardiac myocytes. J Mol Cell Cardiol 2003;35:1145-1152.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 1145-1152
    • Li, S.1    Li, X.2    Rozanski, G.J.3
  • 16
    • 18644370826 scopus 로고    scopus 로고
    • Intimal plaque development and oxidative stress in cholesterol-induced atherosclerosis in New Zealand rabbits
    • Heinle H, Brehme U, Friedemann G, Frey JC, Wolf AT, Kelber O et al. Intimal plaque development and oxidative stress in cholesterol-induced atherosclerosis in New Zealand rabbits. Acta Physiol Scand 2002;76:101-107.
    • (2002) Acta Physiol Scand , vol.76 , pp. 101-107
    • Heinle, H.1    Brehme, U.2    Friedemann, G.3    Frey, J.C.4    Wolf, A.T.5    Kelber, O.6
  • 18
    • 0022300420 scopus 로고
    • Glutathione synthesis: γ-glutamylcysteine synthetase from rat kidney
    • Seelig GF, Meister A. Glutathione synthesis: γ-glutamylcysteine synthetase from rat kidney. Methods Enzymol 1985;113:379-390.
    • (1985) Methods Enzymol , vol.113 , pp. 379-390
    • Seelig, G.F.1    Meister, A.2
  • 19
    • 0029417335 scopus 로고
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor-β1
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor-β1. J Biol Chem 1995;270:30334-30338.
    • (1995) J Biol Chem , vol.270 , pp. 30334-30338
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 22
    • 11844263366 scopus 로고    scopus 로고
    • Transforming growth factor-beta, cell signaling and cardiovascular disorders
    • Agrotis A, Kalinina N, Bobik A. Transforming growth factor-beta, cell signaling and cardiovascular disorders. Curr Vasc Pharmacol 2005;3:55-61.
    • (2005) Curr Vasc Pharmacol , vol.3 , pp. 55-61
    • Agrotis, A.1    Kalinina, N.2    Bobik, A.3
  • 23
    • 34047148354 scopus 로고    scopus 로고
    • The role of TGF-β signaling in myocardial infarction and cardiac remodeling
    • Bujak M, Frangogiannis NG. The role of TGF-β signaling in myocardial infarction and cardiac remodeling. Cardiovasc Res 2007;74:184- 195.
    • (2007) Cardiovasc Res , vol.74 , pp. 184-195
    • Bujak, M.1    Frangogiannis, N.G.2
  • 24
    • 8644268825 scopus 로고    scopus 로고
    • Inhibition of TGF-β signaling exacerbates early cardiac dysfunction but prevents late remodeling after infarction
    • Ikeuchi M, Tsutsui H, Shiomi T, Matsusaka H, Matsushima S, Wen J et al. Inhibition of TGF-β signaling exacerbates early cardiac dysfunction but prevents late remodeling after infarction. Cardiovasc Res 2004;64:526-535.
    • (2004) Cardiovasc Res , vol.64 , pp. 526-535
    • Ikeuchi, M.1    Tsutsui, H.2    Shiomi, T.3    Matsusaka, H.4    Matsushima, S.5    Wen, J.6
  • 25
    • 14844349754 scopus 로고    scopus 로고
    • Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: Role of p47phox phosphorylation and binding to TRAF4
    • Li JM, Fan LM, Christie MR, Shah AM. Acute tumor necrosis factor alpha signaling via NADPH oxidase in microvascular endothelial cells: role of p47phox phosphorylation and binding to TRAF4. Mol Cell Biol 2005;25:2320- 2330.
    • (2005) Mol Cell Biol , vol.25 , pp. 2320-2330
    • Li, J.M.1    Fan, L.M.2    Christie, M.R.3    Shah, A.M.4
  • 26
    • 14644404356 scopus 로고    scopus 로고
    • p47phox associates with the cytoskeleton through cortactin in human vascular smooth muscle cells: Role in NAD(P)H oxidase regulation by angiotensin II
    • Touyz RM, Yao G, Quinn MT, Pagano PJ, Schiffrin EL. p47phox associates with the cytoskeleton through cortactin in human vascular smooth muscle cells: role in NAD(P)H oxidase regulation by angiotensin II. Arterioscler Thromb Vasc Biol 2005;25:512-518.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 512-518
    • Touyz, R.M.1    Yao, G.2    Quinn, M.T.3    Pagano, P.J.4    Schiffrin, E.L.5
  • 27
    • 0032007564 scopus 로고    scopus 로고
    • Tumor necrosis factor-α activates a p22phox-based NADH oxidase in vascurlar smooth muscle cells
    • De Keulenaer GW, Alexander RW, Ushio-Fukai M, Ishizaka N, Griendling KK. Tumor necrosis factor-α activates a p22phox-based NADH oxidase in vascurlar smooth muscle cells. Biochem J 329:653-657. 198.
    • Biochem J , vol.329 , Issue.653-657 , pp. 198
    • De Keulenaer, G.W.1    Alexander, R.W.2    Ushio-Fukai, M.3    Ishizaka, N.4    Griendling, K.K.5
  • 28
    • 0031848577 scopus 로고    scopus 로고
    • Angiotensin II induces p67phox mRNA expression and NADPH oxidase superoxide generation in rabbit aortic adventitial fibroblasts
    • Pagano PJ, Chanock SJ, Siwik DA, Colucci WS, Clark JK. Angiotensin II induces p67phox mRNA expression and NADPH oxidase superoxide generation in rabbit aortic adventitial fibroblasts. Hypertension 1998;32:331- 337.
    • (1998) Hypertension , vol.32 , pp. 331-337
    • Pagano, P.J.1    Chanock, S.J.2    Siwik, D.A.3    Colucci, W.S.4    Clark, J.K.5
  • 30
    • 0033806242 scopus 로고    scopus 로고
    • Oxidative stress and regulation of glutathione in lung inflammation
    • Rahman I, MacNee W. Oxidative stress and regulation of glutathione in lung inflammation. Eur Respir J 2000;16:534-554.
    • (2000) Eur Respir J , vol.16 , pp. 534-554
    • Rahman, I.1    MacNee, W.2
  • 32
    • 0017876204 scopus 로고
    • The fate of extracellular glutathione in the rat
    • Hahn R, Wendel A, Flohe L. The fate of extracellular glutathione in the rat. Biochim Biophys Acta 1978;539:324-337.
    • (1978) Biochim Biophys Acta , vol.539 , pp. 324-337
    • Hahn, R.1    Wendel, A.2    Flohe, L.3
  • 33
    • 0000636206 scopus 로고
    • Glutathione (GSH) repletion by N-acetylcysteine (NAC) in patients with the adult respiratory distress syndrome (ARDS)
    • Bernard GR, Swindell BB, Meredith MJ, Carroll FE, Higgins SB. Glutathione (GSH) repletion by N-acetylcysteine (NAC) in patients with the adult respiratory distress syndrome (ARDS). Am Rev Respir Dis 1989;139:A221.
    • (1989) Am Rev Respir Dis , vol.139
    • Bernard, G.R.1    Swindell, B.B.2    Meredith, M.J.3    Carroll, F.E.4    Higgins, S.B.5
  • 34
    • 24344490793 scopus 로고    scopus 로고
    • N-Acetyl-L-cysteine suppresses TGF-β signaling at distinct molecular steps: The biochemical and biological efficacy of a multifunctional, antifibrotic drug
    • Meurer SK, Lahme B, Tihaa L, Weiskirchen R, Gressner AM. N-Acetyl-L-cysteine suppresses TGF-β signaling at distinct molecular steps: the biochemical and biological efficacy of a multifunctional, antifibrotic drug. Biochem Pharmacol 2005;70:1026-1034.
    • (2005) Biochem Pharmacol , vol.70 , pp. 1026-1034
    • Meurer, S.K.1    Lahme, B.2    Tihaa, L.3    Weiskirchen, R.4    Gressner, A.M.5
  • 35
    • 0034076416 scopus 로고    scopus 로고
    • Oxygen free radicals and excitation-contraction coupling
    • Goldhaber JI, Qayyum MS. Oxygen free radicals and excitation-contraction coupling. Antioxid Redox Signal 2000;2:55-64.
    • (2000) Antioxid Redox Signal , vol.2 , pp. 55-64
    • Goldhaber, J.I.1    Qayyum, M.S.2
  • 36
    • 33745198418 scopus 로고    scopus 로고
    • Redox regulation of cardiac calcium channels and transporters
    • Zima AV, Blatter LA. Redox regulation of cardiac calcium channels and transporters. Cardiovasc Res 2006;71:310-321.
    • (2006) Cardiovasc Res , vol.71 , pp. 310-321
    • Zima, A.V.1    Blatter, L.A.2
  • 38
    • 0031857290 scopus 로고    scopus 로고
    • Interaction of reactive oxygen species with ion transport mechanisms
    • Kourie JI. Interaction of reactive oxygen species with ion transport mechanisms. Am J Physiol 1998;275:C1-C24.
    • (1998) Am J Physiol , vol.275
    • Kourie, J.I.1
  • 39
    • 33749505491 scopus 로고    scopus 로고
    • Biphasic modulation of ryanodine receptors by sulfhydryl oxidation in rat ventricular myocytes
    • Xie H, Zhu PH. Biphasic modulation of ryanodine receptors by sulfhydryl oxidation in rat ventricular myocytes. Biophys J 2006;91:2882- 2891.
    • (2006) Biophys J , vol.91 , pp. 2882-2891
    • Xie, H.1    Zhu, P.H.2
  • 40
    • 11144227270 scopus 로고    scopus 로고
    • Lysosome-sarcoplasmic reticulum junctions. A trigger zone for calcium signaling by nicotinic acid adenine dinucleotide phosphate and endothelin-1
    • Kinnear NP, Boittin F-X, Thomas JM, Galione A, Evans AM. Lysosome-sarcoplasmic reticulum junctions. A trigger zone for calcium signaling by nicotinic acid adenine dinucleotide phosphate and endothelin-1. J Biol Chem 2004;279:54319-54326.
    • (2004) J Biol Chem , vol.279 , pp. 54319-54326
    • Kinnear, N.P.1    Boittin, F.-X.2    Thomas, J.M.3    Galione, A.4    Evans, A.M.5
  • 41
    • 0031015476 scopus 로고    scopus 로고
    • 2+-ATPase function by direct attack on the ATP binding site
    • 2+-ATPase function by direct attack on the ATP binding site. Circ Res 1997;80:76-81.
    • (1997) Circ Res , vol.80 , pp. 76-81
    • Xu, K.Y.1    Zweier, J.L.2    Becher, L.C.3
  • 43
    • 3442896500 scopus 로고    scopus 로고
    • Increased inhibition of SERCA2 by phospholamban in the type I diabetic heart
    • Vasanji Z, Dhalla NS, Netticadan T. Increased inhibition of SERCA2 by phospholamban in the type I diabetic heart. Mol Cell Biochem 2004;261:245-249.
    • (2004) Mol Cell Biochem , vol.261 , pp. 245-249
    • Vasanji, Z.1    Dhalla, N.S.2    Netticadan, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.