全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

ROS and RNS Signaling in Heart Disorders: Could Antioxidant Treatment Be Successful?

DOI: 10.1155/2011/293769

Full-Text   Cite this paper   Add to My Lib

Abstract:

There is not too much success in the antioxidant treatment of heart deceases in humans. However a new approach is now developed that suggests that depending on their structures and concentrations antioxidants can exhibit much more complicated functions in many pathological disorders. It is now well established that physiological free radicals superoxide and nitric oxide together with their derivatives hydrogen peroxide and peroxynitrite (all are named reactive oxygen species (ROS) and reactive nitrogen species (RNS)) play a more important role in heart diseases through their signaling functions. Correspondingly this work is dedicated to the consideration of damaging signaling by ROS and RNS in various heart and vascular disorders: heart failure (congestive heart failure or CHF), left ventricular hypertrophy (LVH), coronary heart disease, cardiac arrhythmias, and so forth. It will be demonstrated that ROS overproduction (oxidative stress) is a main origin of the transformation of normal physiological signaling processes into the damaging ones. Furthermore the favorable effects of low/moderate oxidative stress through preconditioning mechanisms in ischemia/reperfusion will be considered. And in the last part we will discuss the possibility of efficient application of antioxidants and enzyme/gene inhibitors for the regulation of damaging ROS signaling in heart disorders. 1. Introduction Heart disease (cardiopathy) and cardiovascular diseases are a group of numerous pathological disorders such as heart failure (congestive heart failure or CHF), left ventricular hypertrophy (LVH), coronary heart disease, cardiac arrhythmias, and so forth, in which signaling processes of reactive oxygen and reactive nitrogen species (ROS and RNS) play an important (probably critical) role. Contemporary studies identified major sources of ROS and RNS productions: NADPH oxidases (Nox), xanthine oxidase, mitochondria, and nitric oxide synthases (NOS). As a rule, heart and cardiovascular diseases are characterized by ROS overproduction whereas the formation of major RNSs nitric oxide (a free radical) and peroxynitrite (diamagnetic molecule) can decrease or increase depending on the nature of heart injury. Free radicals are usually considered to be the damaging factors in various pathologies, but on the other hand ROS and RNS are important signaling species in many physiological and pathophysiological processes. For example the critical role of these species has been shown in preconditioning and other survival processes (see below). A major aim of this work is to consider the role

References

[1]  K. K. Griendling, D. Sorescu, and M. Ushio-Fukai, “NAD(P)H oxidase: role in cardiovascular biology and disease,” Circulation Research, vol. 86, no. 5, pp. 494–501, 2000.
[2]  B. Lassègue and R. E. Clempus, “Vascular NAD(P)H oxidases: specific features, expression, and regulation,” American Journal of Physiology, vol. 285, no. 2, pp. R277–R297, 2003.
[3]  C. E. Murdoch, M. Zhang, A. C. Cave, and A. M. Shah, “NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure,” Cardiovascular Research, vol. 71, no. 2, pp. 208–215, 2006.
[4]  J. K. Bendall, A. C. Cave, C. Heymes, N. Gall, and A. M. Shah, “Pivotal role of a gp91phox-containing NADPH oxidase in angiotensin II-induced cardiac hypertrophy in mice,” Circulation, vol. 105, no. 3, pp. 293–296, 2002.
[5]  H. Nakagami, M. Takemoto, and J. K. Liao, “NADPH oxidase-derived superoxide anion mediates angiotensin II-induced cardiac hypertrophy,” Journal of Molecular and Cellular Cardiology, vol. 35, no. 7, pp. 851–859, 2003.
[6]  J. M. Li, N. P. Gall, D. J. Grieve, M. Chen, and A. M. Shah, “Activation of NADPH oxidase during progression of cardiac hypertrophy to failure,” Hypertension, vol. 40, no. 4, pp. 477–484, 2002.
[7]  Y. L. Li, L. Gao, I. H. Zucker, and H. D. Schultz, “NADPH oxidase-derived superoxide anion mediates angiotensin II-enhanced carotid body chemoreceptor sensitivity in heart failure rabbits,” Cardiovascular Research, vol. 75, no. 3, pp. 546–554, 2007.
[8]  C. Doerries, K. Grote, D. Hilfiker-Kleiner et al., “Critical role of the NAD(P)H oxidase subunit p47phox for left ventricular remodeling/dysfunction and survival after myocardial infarction,” Circulation Research, vol. 100, no. 6, pp. 894–903, 2007.
[9]  J. A. Byrne, D. J. Grieve, J. K. Bendall et al., “Contrasting roles of NADPH oxidase isoforms in pressure-overload versus angiotensin II-induced cardiac hypertrophy,” Circulation Research, vol. 93, no. 9, pp. 802–804, 2003.
[10]  M. Satoh, H. Ogita, K. Takeshita, Y. Mukai, D. J. Kwiatkowski, and J. K. Liao, “Requirement of Rac1 in the development of cardiac hypertrophy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 19, pp. 7432–7437, 2006.
[11]  S. D. Hingtgen, X. Tian, J. Yang et al., “Nox2-containing NADPH oxidase and Akt activation play a key role in angiotensin II-induced cardiomyocyte hypertrophy,” Physiological Genomics, vol. 26, no. 3, pp. 180–191, 2006.
[12]  C. P. Judkins, H. Diep, B. R. S. Broughton et al., “Direct evidence of a role for Nox2 in superoxide production, reduced nitric oxide bioavailability, and early atherosclerotic plaque formation in ApoE-/- mice,” American Journal of Physiology, vol. 298, no. 1, pp. H24–H32, 2010.
[13]  A. Buday, P. Orsy, M. Godó et al., “Elevated systemic TGF-β impairs aortic vasomotor function through activation of NADPH oxidase-driven superoxide production and leads to hypertension, myocardial remodeling, and increased plaque formation in apoE-/- mice,” American Journal of Physiology, vol. 299, no. 2, pp. H386–H395, 2010.
[14]  K. D. Martyn, L. M. Frederick, K. Von Loehneysen, M. C. Dinauer, and U. G. Knaus, “Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases,” Cellular Signalling, vol. 18, no. 1, pp. 69–82, 2006.
[15]  L. Serrander, L. Cartier, K. Bedard et al., “NOX4 activity is determined by mRNA levels and reveals a unique pattern of ROS generation,” Biochemical Journal, vol. 406, no. 1, pp. 105–114, 2007.
[16]  E. T. Denisov and I. B. Afanas’ev, Oxidation and Antioxidants in Organic Chemistry and Biology, CRC Press/Taylor & Francis Group, Boca Raton, Fla, USA, 2005.
[17]  I. Afanasev, “Detection of superoxide in cells, tissues and whole organisms,” Frontiers in Bioscience (Elite Edition), vol. 1, pp. 153–160, 2009.
[18]  T. J. Guzik, J. Sadowski, B. Guzik et al., “Coronary artery superoxide production and nox isoform expression in human coronary artery disease,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 26, no. 2, pp. 333–339, 2006.
[19]  J. Kuroda, T. Ago, S. Matsushima, P. Zhai, M. D. Schneider, and J. Sadoshima, “NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 35, pp. 15565–15570, 2010.
[20]  T. Ago, J. Kuroda, J. Pain, C. Fu, H. Li, and J. Sadoshima, “Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myocytes,” Circulation Research, vol. 106, no. 7, pp. 1253–1264, 2010.
[21]  M. Zhang, A. C. Brewer, K. Schr?der et al., “NADPH oxidase-4 mediates protection against chronic load-induced stress in mouse hearts by enhancing angiogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 42, pp. 18121–18126, 2010.
[22]  G. Zhang, F. Zhang, R. Muh et al., “Autocrine/paracrine pattern of superoxide production through NAD(P)H oxidase in coronary arterial myocytes,” American Journal of Physiology, vol. 292, no. 1, pp. H483–H495, 2007.
[23]  J. M. McCord, R. S. Roy, and S. W. Schaffer, “Free radicals and myocardial ischemia. The role of xanthine oxidase,” Advances in myocardiology, vol. 5, pp. 183–189, 1985.
[24]  D. E. Chambers, D. A. Parks, and G. Patterson, “Xanthine oxidase as a source of free radical damage in myocardial ischemia,” Journal of Molecular and Cellular Cardiology, vol. 17, no. 2, pp. 145–152, 1985.
[25]  J. M. McCord and I. Fridovich, “The utility of superoxide dismutase in studying free radical reactions. II. The mechanism of the mediation of cytochrome c reduction by a variety of electron carriers,” Journal of Biological Chemistry, vol. 245, no. 6, pp. 1374–1377, 1970.
[26]  J. M. Downey, T. Miura, L. J. Eddy et al., “Xanthine oxidase is not a source of free radicals in the ischemic rabbit heart,” Journal of Molecular and Cellular Cardiology, vol. 19, no. 11, pp. 1053–1060, 1987.
[27]  C. M. Grum, K. P. Gallagher, M. M. Kirsh, and M. Shlafer, “Absence of detectable xanthine oxidase in human myocardium,” Journal of Molecular and Cellular Cardiology, vol. 21, no. 3, pp. 263–267, 1989.
[28]  S. L. Thompson-Gorman and J. L. Zweier, “Evaluation of the role of xanthine oxidase in myocardial reperfusion injury,” Journal of Biological Chemistry, vol. 265, no. 12, pp. 6656–6663, 1990.
[29]  Y. Xia and J. L. Zweier, “Substrate control of free radical generation from xanthine oxidase in the postischemic heart,” Journal of Biological Chemistry, vol. 270, no. 32, pp. 18797–18803, 1995.
[30]  M. Ashraf and Z. Q. Samra, “Subcellular distribution of xanthine oxidase during cardiac ischemia and reperfusion: an immunocytochemical study,” Journal of submicroscopic cytology and pathology, vol. 25, no. 2, pp. 193–201, 1993.
[31]  J. W. De Jong, R. G. Schoemaker, R. De Jonge et al., “Enhanced expression and activity of xanthine oxidoreductase in the failing heart,” Journal of Molecular and Cellular Cardiology, vol. 32, no. 11, pp. 2083–2089, 2000.
[32]  U. Landmesser, S. Spiekermann, S. Dikalov et al., “Vascular oxidative stress and endothelial dysfunction in patients with chronic heart failure: role of xanthine-oxidase and extracellular superoxide dismutase,” Circulation, vol. 106, no. 24, pp. 3073–3078, 2002.
[33]  U. Landmesser, S. Spiekermann, C. Preuss et al., “Angiotensin II induces endothelial xanthine oxidase activation: role for endothelial dysfunction in patients with coronary disease,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 4, pp. 943–948, 2007.
[34]  J. G. Duncan, R. Ravi, L. B. Stull, and A. M. Murphy, “Chronic xanthine oxidase inhibition prevents myofibrillar protein oxidation and preserves cardiac function in a transgenic mouse model of cardiomyopathy,” American Journal of Physiology, vol. 289, no. 4, pp. H1512–H1518, 2005.
[35]  S. Baldus, R. K?ster, P. Chumley et al., “Oxypurinol improves coronary and peripheral endothelial function in patients with coronary artery disease,” Free Radical Biology and Medicine, vol. 39, no. 9, pp. 1184–1190, 2005.
[36]  K. M. Minhas, R. M. Saraiva, K. H. Schuleri et al., “Xanthine oxidoreductase inhibition causes reverse remodeling in rats with dilated cardiomyopathy,” Circulation Research, vol. 98, no. 2, pp. 271–279, 2006.
[37]  C. Zhang, X. Xu, B. J. Potter et al., “TNF-α contributes to endothelial dysfunction in ischemia/reperfusion injury,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 26, no. 3, pp. 475–480, 2006.
[38]  E. Yamamoto, K. Kataoka, T. Yamashita et al., “Role of xanthine oxidoreductase in the reversal of diastolic heart failure by candesartan in the salt-sensitive hypertensive rat,” Hypertension, vol. 50, no. 4, pp. 657–662, 2007.
[39]  D. R. Gonzalez, A. V. Treuer, J. Castellanos, R. A. Dulce, and J. M. Hare, “Impaired S-nitrosylation of the ryanodine receptor caused by xanthine oxidase activity contributes to calcium leak in heart failure,” Journal of Biological Chemistry, vol. 285, no. 37, pp. 28938–28945, 2010.
[40]  I. B. Afanas’ev, Signaling Mechanisms of Oxygen and Nitrogen Free Radicals, CRC Press/Taylor & Francis, Boca Raton, Fla, USA, 2009.
[41]  T. Ide, H. Tsutsui, S. Kinugawa et al., “Mitochondrial electron transport complex I is a potential source of oxygen free radicals in the failing myocardium,” Circulation Research, vol. 85, no. 4, pp. 357–363, 1999.
[42]  Q. Chen, S. Moghaddas, C. L. Hoppel, and E. J. Lesnefsky, “Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria,” American Journal of Physiology, vol. 294, no. 2, pp. C460–C466, 2008.
[43]  A. Carpi, R. Menabò, N. Kaludercic, P. Pelicci, F. Di Lisa, and M. Giorgio, “The cardioprotective effects elicited by ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury,” Biochimica et Biophysica Acta, vol. 1787, no. 7, pp. 774–780, 2009.
[44]  Y. Chen, M. Hou, Y. Li et al., “Increased superoxide production causes coronary endothelial dysfunction and depressed oxygen consumption in the failing heart,” American Journal of Physiology, vol. 288, no. 1, pp. H133–H141, 2005.
[45]  E. M. Redout, M. J. Wagner, M. J. Zuidwijk et al., “Right-ventricular failure is associated with increased mitochondrial complex II activity and production of reactive oxygen species,” Cardiovascular Research, vol. 75, no. 4, pp. 770–781, 2007.
[46]  N. Mariappan, C. M. Elks, B. Fink, and J. Francis, “TNF-induced mitochondrial damage: a link between mitochondrial complex I activity and left ventricular dysfunction,” Free Radical Biology and Medicine, vol. 46, no. 4, pp. 462–470, 2009.
[47]  R. A. Haworth, K. T. Potter, and D. C. Russell, “Role of arachidonic acid, lipoxygenase, and mitochondrial depolarization in reperfusion arrhythmias,” American Journal of Physiology, vol. 299, no. 1, pp. H165–H174, 2010.
[48]  Y. R. Chen, C. L. Chen, D. R. Pfeiffer, and J. L. Zweier, “Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation,” Journal of Biological Chemistry, vol. 282, no. 45, pp. 32640–32654, 2007.
[49]  S. Umar and A. Van Der Laarse, “Nitric oxide and nitric oxide synthase isoforms in the normal, hypertrophic, and failing heart,” Molecular and Cellular Biochemistry, vol. 333, no. 1-2, pp. 191–201, 2010.
[50]  D. A. I. Lijun, P. S. Brookes, V. M. Darley-Usmar, and P. G. Anderson, “Bioenergetics in cardiac hypertrophy: mitochondrial respiration as a pathological target of NO?,” American Journal of Physiology, vol. 281, no. 6, pp. H2261–H2269, 2001.
[51]  X. Chen, F. Niroomand, Z. Liu et al., “Expression of nitric oxide related enzymes in coronary heart disease,” Basic Research in Cardiology, vol. 101, no. 4, pp. 346–353, 2006.
[52]  F. H. Khadour, D. Panas, P. Ferdinandy et al., “Enhanced NO and superoxide generation in dysfunctional hearts from endotoxemic rats,” American Journal of Physiology, vol. 283, no. 3, pp. H1108–H1115, 2002.
[53]  E. Takimoto, H. C. Champion, M. Li et al., “Oxidant stress from nitric oxide synthase-3 uncoupling stimulates cardiac pathologic remodeling from chronic pressure load,” Journal of Clinical Investigation, vol. 115, no. 5, pp. 1221–1231, 2005.
[54]  Y. H. Liu, O. A. Carretero, O. H. Cingolani et al., “Role of inducible nitric oxide synthase in cardiac function and remodeling in mice with heart failure due to myocardial infarction,” American Journal of Physiology, vol. 289, no. 6, pp. H2616–H2623, 2005.
[55]  W. F. Saavedra, N. Paolocci, M. E. S. John et al., “Imbalance between xanthine oxidase and nitric oxide synthase signaling pathways underlies mechanoenergetic uncoupling in the failing heart,” Circulation Research, vol. 90, no. 3, pp. 297–304, 2002.
[56]  S. A. Khan, K. Lee, K. M. Minhas et al., “Neuronal nitric oxide synthase negatively regulates xanthine oxidoreductase inhibition of cardiac excitation-contraction coupling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 45, pp. 15944–15948, 2004.
[57]  R. M. Saraiva, K. M. Minhas, M. Zheng et al., “Reduced neuronal nitric oxide synthase expression contributes to cardiac oxidative stress and nitroso-redox imbalance in ob/ob mice,” Nitric Oxide, vol. 16, no. 3, pp. 331–338, 2007.
[58]  N. Suematsu, C. Ojaimi, F. A. Recchia et al., “Potential mechanisms of low sodium diet-induced cardiac disease: superoxide-NO in the heart,” Circulation Research, vol. 106, no. 3, pp. 593–600, 2010.
[59]  S. Philipp, S. D. Critz, L. Cui, V. Solodushko, M. V. Cohen, and J. M. Downey, “Localizing extracellular signal-regulated kinase (ERK) in pharmacological preconditioning's trigger pathway,” Basic Research in Cardiology, vol. 101, no. 2, pp. 159–167, 2006.
[60]  S. Kimura, G. X. Zhang, A. Nishiyama et al., “Role of NAD(P)H oxidase- and mitochondria-derived reactive oxygen species in cardioprotection of ischemic reperfusion injury by angiotensin II,” Hypertension, vol. 45, no. 5, pp. 860–866, 2005.
[61]  M. Duda, A. Konior, E. Klemenska, and A. Beresewicz, “Preconditioning protects endothelium by preventing ET-1-induced activation of NADPH oxidase and xanthine oxidase in post-ischemic heart,” Journal of Molecular and Cellular Cardiology, vol. 42, no. 2, pp. 400–410, 2007.
[62]  Y. Yue, Q. Qin, M. V. Cohen, J. M. Downey, and S. D. Critz, “The relative order of channels, free radicals and p38 MAPK in preconditioning's protective pathway in rat heart,” Cardiovascular Research, vol. 55, no. 3, pp. 681–689, 2002.
[63]  J. P. Brennan, R. Southworth, R. A. Medina, S. M. Davidson, M. R. Duchen, and M. J. Shattock, “Mitochondrial uncoupling, with low concentration FCCP, induces ROS-dependent cardioprotection independent of KATP channel activation,” Cardiovascular Research, vol. 72, no. 2, pp. 313–321, 2006.
[64]  D. Van Cuong, M. Warda, N. Kim et al., “Dynamic changes in nitric oxide and mitochondrial oxidative stress with site-dependent differential tissue response during anoxic preconditioning in rat heart,” American Journal of Physiology, vol. 293, no. 3, pp. H1457–H1465, 2007.
[65]  S. Koneru, S. V. Penumathsa, M. Thirunavukkarasu et al., “Redox regulation of ischemic preconditioning is mediated by the differential activation of caveolins and their association with eNOS and GLUT-4,” American Journal of Physiology, vol. 292, no. 5, pp. H2060–H2072, 2007.
[66]  M. Juhaszova, D. B. Zorov, Y. Yaniv, H. B. Nuss, S. Wang, and S. J. Sollott, “Role of glycogen synthase kinase-3β in cardioprotection,” Circulation Research, vol. 104, no. 11, pp. 1240–1252, 2009.
[67]  M. V. Cohen, X. M. Yang, and J. M. Downey, “Nitric oxide is a preconditioning mimetic and cardioprotectant and is the basis of many available infarct-sparing strategies,” Cardiovascular Research, vol. 70, no. 2, pp. 231–239, 2006.
[68]  F. Vigneron, P. Dos Santos, S. Lemoine et al., “GSK-3β at the crossroads in the signalling of heart preconditioning: implication of mTOR and Wnt pathways,” Cardiovascular Research, vol. 90, no. 1, pp. 49–56, 2011.
[69]  J. X. Chen, H. Zeng, Q. H. Tuo, H. Yu, B. Meyrick, and J. L. Aschner, “NADPH oxidase modulates myocardial Akt, ERK1/2 activation, and angiogenesis after hypoxia-reoxygenation,” American Journal of Physiology, vol. 292, no. 4, pp. H1664–H1674, 2007.
[70]  J. Feng, S. M. Damrauer, M. Lee, F. W. Sellke, C. Ferran, and M. R. Abid, “Endothelium-dependent coronary vasodilatation requires NADPH oxidase-derived reactive oxygen species,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 30, no. 9, pp. 1703–1710, 2010.
[71]  M. Monti, S. Donnini, A. Giachetti, D. Mochly-Rosen, and M. Ziche, “δPKC inhibition or ?PKC activation repairs endothelial vascular dysfunction by regulating eNOS post-translational modification,” Journal of Molecular and Cellular Cardiology, vol. 48, no. 4, pp. 746–756, 2010.
[72]  J. Widder, T. Behr, D. Fraccarollo et al., “Vascular endothelial dysfunction and superoxide anion production in heart failure are p38 MAP kinase-dependent,” Cardiovascular Research, vol. 63, no. 1, pp. 161–167, 2004.
[73]  C. Gaitanaki, M. Mastri, I. K. S. Aggeli, and I. Beis, “Differential roles of p38-MAPK and JNKs in mediating early protection or apoptosis in the hyperthermic perfused amphibian heart,” Journal of Experimental Biology, vol. 211, no. 15, pp. 2524–2532, 2008.
[74]  P. Heusch, M. Canton, S. Aker et al., “The contribution of reactive oxygen species and p38 mitogen-activated protein kinase to myofilament oxidation and progression of heart failure in rabbits,” British Journal of Pharmacology, vol. 160, no. 6, pp. 1408–1416, 2010.
[75]  M. Satoh, C. M. Matter, H. Ogita et al., “Inhibition of apoptosis-regulated signaling kinase-1 and prevention of congestive heart failure by estrogen,” Circulation, vol. 115, no. 25, pp. 3197–3204, 2007.
[76]  J. Cai, F. F. Yi, Z. Y. Bian et al., “Crocetin protects against cardiac hypertrophy by blocking MEK-ERK1-2 signalling pathway,” Journal of Cellular and Molecular Medicine, vol. 13, no. 5, pp. 909–925, 2009.
[77]  C. W. Younce and P. E. Kolattukudy, “MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP,” Biochemical Journal, vol. 426, no. 1, pp. 43–53, 2010.
[78]  S. Hikoso, O. Yamaguchi, Y. Nakano et al., “The IκB Kinase β/nuclear factor κb signaling pathway protects the heart from hemodynamic stress mediated by the regulation of manganese superoxide dismutase expression,” Circulation Research, vol. 105, no. 1, pp. 70–79, 2009.
[79]  A. E. Awad, V. Kandalam, S. Chakrabarti et al., “Tumor necrosis factor induces matrix metalloproteinases in cardiomyocytes and cardiofibroblasts differentially via superoxide production in a PI3Kγ-dependent manner,” American Journal of Physiology, vol. 298, no. 3, pp. C679–C692, 2010.
[80]  Z. Lu, X. Xu, X. Hu et al., “Oxidative stress regulates left ventricular PDE5 expression in the failing heart,” Circulation, vol. 121, no. 13, pp. 1474–1483, 2010.
[81]  Z. Zhao, N. Fefelova, M. Shanmugam, P. Bishara, G. J. Babu, and L. H. Xie, “Angiotensin II induces afterdepolarizations via reactive oxygen species and calmodulin kinase II signaling,” Journal of Molecular and Cellular Cardiology, vol. 50, no. 1, pp. 128–136, 2011.
[82]  R. R. Alcendor, S. Gao, P. Zhai et al., “Sirt1 regulates aging and resistance to oxidative stress in the heart,” Circulation Research, vol. 100, no. 10, pp. 1512–1521, 2007.
[83]  N. R. Sundaresan, M. Gupta, G. Kim, S. B. Rajamohan, A. Isbatan, and M. P. Gupta, “Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice,” Journal of Clinical Investigation, vol. 119, no. 9, pp. 2758–2771, 2009.
[84]  J. Guo, Z. Gertsberg, N. Ozgen, and S. F. Steinberg, “P66Shc links α1-adrenergic receptors to a reactive oxygen species-dependent AKT-FOXO3A phosphorylation pathway in cardiomyocytes,” Circulation Research, vol. 104, no. 5, pp. 660–669, 2009.
[85]  A. Sengupta, J. D. Molkentin, J. -H. Paik, R. A. DePinho, and K. E. Yutzey, “FoxO transcription factors promote cardiomyocyte survival upon induction of oxidative stress,” Journal of Biological Chemistry, vol. 286, no. 9, pp. 7468–7478, 2011.
[86]  S. D. Hingtgen, Z. Li, W. Kutschke, X. Tian, R. V. Sharma, and R. L. Davisson, “Superoxide scavenging and Akt inhibition in myocardium ameliorate pressure overload-induced NF-κB activation and cardiac hypertrophy,” Physiological Genomics, vol. 41, no. 2, pp. 127–136, 2010.
[87]  C. N. White, C. C. Liu, A. Garcia et al., “Activation of cAMP-dependent signaling induces oxidative modification of the cardiac Na+-K+ pump and inhibits its activity,” Journal of Biological Chemistry, vol. 285, no. 18, pp. 13712–13720, 2010.
[88]  Z. Xu, X. Ji, and P. G. Boysen, “Exogenous nitric oxide generates ROS and induces cardioprotection: involvement of PKG, mitochondrial KATP channels, and ERK,” American Journal of Physiology, vol. 286, no. 4, pp. H1433–H1440, 2004.
[89]  A. Das, F. N. Salloum, L. Xi, Y. J. Rao, and R. C. Kukreja, “ERK phosphorylation mediates sildenafil-induced myocardial protection against ischemia-reperfusion injury in mice,” American Journal of Physiology, vol. 296, no. 5, pp. H1236–H1243, 2009.
[90]  C. Zhang, T. W. Hein, W. Wang, Y. Ren, R. D. Shipley, and L. Kuo, “Activation of JNK and xanthine oxidase by TNF-α impairs nitric oxide-mediated dilation of coronary arterioles,” Journal of Molecular and Cellular Cardiology, vol. 40, no. 2, pp. 247–257, 2006.
[91]  L. Shan, J. Li, M. Wei et al., “Disruption of Rac1 signaling reduces ischemia-reperfusion injury in the diabetic heart by inhibiting calpain,” Free Radical Biology and Medicine, vol. 49, no. 11, pp. 1804–1814, 2010.
[92]  I. Afanas'ev, “Reactive oxygen species and age-related genes p66shc, Sirtuin, FOX03 and Klotho in senescence,” Oxidative medicine and cellular longevity, vol. 3, no. 2, pp. 77–85, 2010.
[93]  J. M. Wu and T.-C. Hsieh, “Resveratrol: a cardioprotective substance,” Annals of the New York Academy of Sciences, vol. 1215, no. 1, pp. 16–21, 2011.
[94]  Y. A. Asiri, “Probucol attenuates cyclophosphamideinduced oxidative apoptosis, p53 and Bax signal expression in rat cardiac tissues,” Oxidative Medicine and Cellular Longevity, vol. 3, no. 5, pp. 308–316, 2010.
[95]  P. Tripathi, M. Chandra, and M. K. Misra, “Oral administration of l-arginine in patients with angina or following myocardial infarction may be protective by increasing plasma superoxide dismutase and total thiols with reduction in serum cholesterol and xanthine oxidase,” Oxidative Medicine and Cellular Longevity, vol. 2, no. 4, pp. 231–237, 2009.
[96]  E. D. van Deel, Z. Lu, X. Xu et al., “Extracellular superoxide dismutase protects the heart against oxidative stress and hypertrophy after myocardial infarction,” Free Radical Biology and Medicine, vol. 44, no. 7, pp. 1305–1313, 2008.
[97]  C. Gaitanaki, M. Papatriantafyllou, K. Stathopoulou, and I. Beis, “Effects of various oxidants and antioxidants on the p38-MAPK signalling pathway in the perfused amphibian heart,” Molecular and Cellular Biochemistry, vol. 291, no. 1-2, pp. 107–117, 2006.
[98]  Y. Ding, Y. L. Li, M. C. Zimmerman, R. L. Davisson, and H. D. Schultz, “Role of CuZn superoxide dismutase on carotid body function in heart failure rabbits,” Cardiovascular Research, vol. 81, no. 4, pp. 678–685, 2009.
[99]  C. A. Piantadosi, M. S. Carraway, A. Babiker, and H. B. Suliman, “Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via nrf2-mediated transcriptional control of nuclear respiratory factor-1,” Circulation Research, vol. 103, no. 11, pp. 1232–1240, 2008.
[100]  J. Chen, G. C. Shearer, Q. Chen et al., “Omega-3 fatty acids prevent pressure overload-induced cardiac fibrosis through activation of cyclic GMP/protein kinase g signaling in cardiac fibroblasts,” Circulation, vol. 123, no. 6, pp. 584–593, 2011.
[101]  A. Das, F. N. Salloum, L. Xi, Y. J. Rao, and R. C. Kukreja, “ERK phosphorylation mediates sildenafil-induced myocardial protection against ischemia-reperfusion injury in mice,” American Journal of Physiology, vol. 296, no. 5, pp. H1236–H1243, 2009.
[102]  Z. Ungvari, A. Csiszar, A. Huang, P. M. Kaminski, M. S. Wolin, and A. Koller, “High pressure induces superoxide production in isolated arteries via protein kinase C-dependent activation of NAD(P)H oxidase,” Circulation, vol. 108, no. 10, pp. 1253–1258, 2003.
[103]  A. Fortu?o, J. Bidegain, A. Baltanás et al., “Is leptin involved in phagocytic NADPH oxidase overactivity in obesity? Potential clinical implications,” Journal of Hypertension, vol. 28, no. 9, pp. 1944–1950, 2010.
[104]  E. V. Vykhovanets, E. Shankar, O. V. Vykhovanets, S. Shukla, and S. Gupta, “High-fat diet increases NF-κB signaling in the prostate of reporter mice,” Prostate, vol. 71, no. 2, pp. 147–156, 2011.
[105]  L. Chen, B. Xu, L. Liu et al., “Cadmium induction of reactive oxygen species activates the mTOR pathway, leading to neuronal cell death,” Free Radical Biology and Medicine, vol. 50, no. 5, pp. 624–632, 2011.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133