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State of the Art Reviews

Oxidative stress, a common molecular pathway for kidney disease: Role of the redox enzyme p66Shc

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Pages 313-320 | Received 03 Jun 2013, Accepted 08 Sep 2013, Published online: 04 Nov 2013

References

  • Vostalova J, Galandakova A, Strebl P, et al. Oxidative stress in kidney disease patients. Vnitr Lek. 2012;58:202–207
  • Menini S, Amadio L, Oddi G, et al. Deletion of p66Shc longevity gene protects against experimental diabetic glomerulopathy by preventing diabetes-induced oxidative stress. Diabetes. 2006;55:1642–1650
  • Luzi L, Confalonieri S, Di Fiore PP, Pelicci PG. Evolution of Shc functions from nematode to human. Curr Opin Genet Dev. 2000;10:668–674
  • Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science. 1997;278:2075–2080
  • Giorgio M, Migliaccio E, Orsini F, et al. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell. 2005;122:221–233
  • Bonfini L, Migliaccio E, Pelicci G, et al. Not all Shc's roads lead to Ras. Trends Biochem Sci. 1996;21:257–261
  • Chakraborti T, Das S, Mondal M, et al. Oxidant, mitochondria and calcium: an overview. Cell Signal. 1999;11:77–85
  • Piantadosi CA, Suliman HB. Redox regulation of mitochondrial biogenesis. Free Radic Biol Med. 2012;53:2043–2053
  • Galimov ER. The role of p66shc in oxidative stress and apoptosis. Acta Naturae. 2010;2:44–51
  • Khanday FA, Santhanam L, Kasuno K, et al. Sos-mediated activation of rac1 by p66shc. J Cell Biol. 2006;172:817–822
  • Wu Z, Rogers B, Kachi S, et al. Reduction of p66Shc suppresses oxidative damage in retinal pigmented epithelial cells and retina. J Cell Physiol. 2006;209:996–1005
  • Koch OR, Fusco S, Ranieri SC, et al. Role of the life span determinant P66(shcA) in ethanol-induced liver damage. Lab Invest. 2008;88:750–760
  • Berniakovich I, Trinei M, Stendardo M, et al. p66Shc-generated oxidative signal promotes fat accumulation. J Biol Chem. 2008;283:34283–34293
  • Pinton P, Rimessi A, Marchi S, et al. Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc. Science. 2007;315:659–663
  • Liesa M, Palacin M, Zorzano A. Mitochondrial dynamics in mammalian health and disease. Physiol Rev. 2009;89:799–845
  • Otera H, Mihara K. Molecular mechanisms and physiologic functions of mitochondrial dynamics. J Biochem. 2011;149:241–251
  • Zhan M, Brooks C, Liu F, et al. Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology. Kidney Int. 2013;83:568–581
  • Small DM, Coombes JS, Bennett N, et al. Oxidative stress, anti-oxidant therapies and chronic kidney disease. Nephrology (Carlton). 2012;17:311–321
  • Raffaello A, Rizzuto R. Mitochondrial longevity pathways. Biochim Biophys Acta. 2011;1813:260–268
  • Su K, Bourdette D, Forte M. Genetic inactivation of mitochondria-targeted redox enzyme p66ShcA preserves neuronal viability and mitochondrial integrity in response to oxidative challenges. Front Physiol. 2012;3:285–293
  • Veeramani S, Chou YW, Lin FC, et al. Reactive oxygen species induced by p66Shc longevity protein mediate nongenomic androgen action via tyrosine phosphorylation signaling to enhance tumorigenicity of prostate cancer cells. Free Radic Biol Med. 2012;53:95–108
  • Natalicchio A, Tortosa F, Perrini S, et al. p66Shc, a multifaceted protein linking Erk signalling, glucose metabolism, and oxidative stress. Arch Physiol Biochem. 2011;117:116–124
  • Alam SM, Rajendran M, Ouyang S, et al. A novel role of Shc adaptor proteins in steroid hormone-regulated cancers. Endocr Relat Cancer. 2009;16:1–16
  • Bashir M, Kirmani D, Bhat HF, et al. P66shc and its downstream Eps8 and Rac1 proteins are upregulated in esophageal cancers. Cell Commun Signal. 2010;8:13–18
  • Carollo C, Lo Presti R, Caimi G. Leukocyte activation markers and oxidative status in chronic kidney disease. Minerva Urol Nefrol. 2013;65:69–76
  • Fassett RG, Venuthurupalli SK, Gobe GC, et al. Biomarkers in chronic kidney disease: a review. Kidney Int. 2011;80:806–821
  • Gill PS, Wilcox CS. NADPH oxidases in the kidney. Antioxid Redox Signal. 2006;8:1597–1607
  • Percy CJ, Brown L, Power DA, et al. Obesity and hypertension have differing oxidant handling molecular pathways in age-related chronic kidney disease. Mech Ageing Dev. 2009;130:129–138
  • Kanwar YS, Sun L, Xie P, et al. A glimpse of various pathogenetic mechanisms of diabetic nephropathy. Annu Rev Pathol. 2011;6:395–423
  • Inoguchi T. Role of oxidative stress in pathogenesis of diabetic nephropathy. Nihon Jinzo Gakkai Shi. 2011;53:1016–1020
  • Sun L, Xiao L, Nie J, et al. p66Shc mediates high-glucose and angiotensin II-induced oxidative stress renal tubular injury via mitochondrial-dependent apoptotic pathway. Am J Physiol Renal Physiol. 2010;299:F1014–F1025
  • Menini S, Iacobini C, Ricci C, et al. Ablation of the gene encoding p66Shc protects mice against AGE-induced glomerulopathy by preventing oxidant-dependent tissue injury and further AGE accumulation. Diabetologia. 2007;50:1997–2007
  • Pagnin E, Fadini G, de Toni R, et al. Diabetes induces p66shc gene expression in human peripheral blood mononuclear cells: relationship to oxidative stress. J Clin Endocrinol Metab. 2005;90:1130–1136
  • Bock F, Shahzad K, Wang H, et al. Activated protein C ameliorates diabetic nephropathy by epigenetically inhibiting the redox enzyme p66Shc. Proc Natl Acad Sci USA. 2013;110:648–653
  • Abuelo JG. Normotensive ischemic acute renal failure. N Engl J Med. 2007;357:797–805
  • Chapman JR, O'Connell PJ, Nankivell BJ. Chronic renal allograft dysfunction. J Am Soc Nephrol. 2005;16:3015–3026
  • Safirstein RL. Lessons learned from ischemic and cisplatin-induced nephrotoxicity in animals. Ren Fail. 1999;21:359–364
  • Arany I, Megyesi JK, Kaneto H, et al. Activation of ERK or inhibition of JNK ameliorates H(2)O(2) cytotoxicity in mouse renal proximal tubule cells. Kidney Int. 2004;65:1231–1239
  • Arany I, Megyesi JK, Reusch JE, Safirstein RL. CREB mediates ERK-induced survival of mouse renal tubular cells after oxidant stress. Kidney Int. 2005;68:1573–1582
  • di Mari JF, Davis R, Safirstein RL. MAPK activation determines renal epithelial cell survival during oxidative injury. Am J Physiol. 1999;277:F195–F203
  • Andreucci M, Michael A, Kramers C, et al. Renal ischemia/reperfusion and ATP depletion/repletion in LLC-PK(1) cells result in phosphorylation of FKHR and FKHRL1. Kidney Int. 2003;64:1189–1198
  • Iordanov MS, Choi RJ, Ryabinina OP, et al. The UV (Ribotoxic) stress response of human keratinocytes involves the unexpected uncoupling of the Ras-extracellular signal-regulated kinase signaling cascade from the activated epidermal growth factor receptor. Mol Cell Biol. 2002;22:5380–5394
  • Wang Z, Chen JK, Wang SW, et al. Importance of functional EGF receptors in recovery from acute nephrotoxic injury. J Am Soc Nephrol. 2003;14:3147–3154
  • Yano T, Yazima S, Hagiwara K, et al. Activation of epidermal growth factor receptor in the early phase after renal ischemia--reperfusion in rat. Nephron. 1999;81:230–233
  • Ravichandran KS. Signaling via Shc family adapter proteins. Oncogene. 2001;20:6322–6330
  • Rao GN. Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases. Oncogene. 1996;13:713–719
  • Pellegrini M, Pacini S, Baldari CT. p66SHC: the apoptotic side of Shc proteins. Apoptosis. 2005;10:13–18
  • Okada S, Kao AW, Ceresa BP, et al. The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway. J Biol Chem. 1997;272:28042–28049
  • Purdom S, Chen QM. Linking oxidative stress and genetics of aging with p66Shc signaling and forkhead transcription factors. Biogerontology. 2003;4:181–191
  • Skulachev VP. The p66shc protein: a mediator of the programmed death of an organism? IUBMB Life. 2000;49:177–180
  • Arany I, Faisal A, Nagamine Y, Safirstein RL. p66shc inhibits pro-survival epidermal growth factor receptor/ERK signaling during severe oxidative stress in mouse renal proximal tubule cells. J Biol Chem. 2008;283:6110–6117
  • Arany I, Faisal A, Clark JS, et al. p66SHC-mediated mitochondrial dysfunction in renal proximal tubule cells during oxidative injury. Am J Physiol Renal Physiol. 2010;298:F1214–1221
  • Barisoni L, Kriz W, Mundel P, D'Agati V. The dysregulated podocyte phenotype: a novel concept in the pathogenesis of collapsing idiopathic focal segmental glomerulosclerosis and HIV-associated nephropathy. J Am Soc Nephrol. 1999;10:51–61
  • Zhong J, Zuo Y, Ma J, et al. Expression of HIV-1 genes in podocytes alone can lead to the full spectrum of HIV-1-associated nephropathy. Kidney Int. 2005;68:1048–1060
  • Hu Y, Wang X, Zeng L, et al. ERK phosphorylates p66shcA on Ser36 and subsequently regulates p27kip1 expression via the Akt-FOXO3a pathway: implication of p27kip1 in cell response to oxidative stress. Mol Biol Cell. 2005;16:3705–3718
  • Husain M, Meggs LG, Vashistha H, et al. Inhibition of p66ShcA longevity gene rescues podocytes from HIV-1-induced oxidative stress and apoptosis. J Biol Chem. 2009;284:16648–16658
  • Orth SR, Ritz E. The renal risks of smoking: an update. Curr Opin Nephrol Hypertens. 2002;11:483–488
  • Orth SR, Hallan SI. Smoking: a risk factor for progression of chronic kidney disease and for cardiovascular morbidity and mortality in renal patients – absence of evidence or evidence of absence? Clin J Am Soc Nephrol. 2008;3:226–236
  • Halimi JM, Giraudeau B, Vol S, et al. Effects of current smoking and smoking discontinuation on renal function and proteinuria in the general population. Kidney Int. 2000;58:1285–1292
  • Rossing P, Hougaard P, Parving HH. Risk factors for development of incipient and overt diabetic nephropathy in type 1 diabetic patients: a 10-year prospective observational study. Diabetes Care. 2002;25:859–864
  • Hallan SI, Orth SR. Smoking is a risk factor in the progression to kidney failure. Kidney Int. 2011;80:516–523
  • Agarwal PK, Hellemons ME, Zelle DM, et al. Smoking is a risk factor for graft failure and mortality after renal transplantation. Am J Nephrol. 2011;34:26–31
  • Husain K, Scott BR, Reddy SK, Somani SM. Chronic ethanol and nicotine interaction on rat tissue antioxidant defense system. Alcohol. 2001;25:89–97
  • Orth SR. Smoking and the kidney. J Am Soc Nephrol. 2002;13:1663–1672
  • Arany I, Clark J, Reed DK, Juncos LA. Chronic nicotine exposure augments renal oxidative stress and injury through transcriptional activation of p66shc. Nephrol Dial Transplant. 2013;28:1417–1425
  • Sigalotti L, Fratta E, Coral S, et al. Epigenetic drugs as pleiotropic agents in cancer treatment: biomolecular aspects and clinical applications. J Cell Physiol. 2007;212:330–344
  • Peterson BA, Collins AJ, Vogelzang NJ, Bloomfield CD. 5-Azacytidine and renal tubular dysfunction. Blood. 1981;57:182–185
  • Kintzel PE. Anticancer drug-induced kidney disorders. Drug Saf. 2001;24:19–38
  • Gao S, Mobley A, Miller C, et al. Potentiation of reactive oxygen species is a marker for synergistic cytotoxicity of MS-275 and 5-azacytidine in leukemic cells. Leuk Res. 2008;32:771–780
  • Nadasi E, Clark JS, Szanyi I, et al. Epigenetic modifiers exacerbate oxidative stress in renal proximal tubule cells. Anticancer Res. 2009;29:2295–2299
  • Ventura A, Luzi L, Pacini S, et al. The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter. J Biol Chem. 2002;277:22370–22376
  • Arany I, Clark JS, Ember I, Juncos LA. Epigenetic modifiers exert renal toxicity through induction of p66shc. Anticancer Res. 2011;31:3267–3271
  • Arany I, Safirstein RL. Cisplatin nephrotoxicity. Semin Nephrol. 2003;23:460–464
  • Hanigan MH, Devarajan P. Cisplatin nephrotoxicity: molecular mechanisms. Cancer Ther. 2003;1:47–61
  • Pabla N, Dong Z. Cisplatin nephrotoxicity: mechanisms and renoprotective strategies. Kidney Int. 2008;73:994–1007
  • Kim YK, Kim HJ, Kwon CH, et al. Role of ERK activation in cisplatin-induced apoptosis in OK renal epithelial cells. J Appl Toxicol. 2005;25:374–382
  • Nowak G. Protein kinase C-alpha and ERK1/2 mediate mitochondrial dysfunction, decreases in active Na+ transport, and cisplatin-induced apoptosis in renal cells. J Biol Chem. 2002;277:43377–43388
  • Jo SK, Cho WY, Sung SA, et al. MEK inhibitor, U0126, attenuates cisplatin-induced renal injury by decreasing inflammation and apoptosis. Kidney Int. 2005;67:458–466
  • Obreztchikova M, Elouardighi H, Ho M, et al. Distinct signaling functions for Shc isoforms in the heart. J Biol Chem. 2006;281:20197–20204
  • Clark JS, Faisal A, Baliga R, et al. Cisplatin induces apoptosis through the ERK-p66shc pathway in renal proximal tubule cells. Cancer Lett. 2010;297:165–170
  • Arany I, Clark JS, Reed DK, et al. Cisplatin enhances interaction between p66Shc and HSP27: its role in reorganization of the actin cytoskeleton in renal proximal tubule cells. Anticancer Res. 2012;32:4759–4763
  • Rattanavich R, Plagov A, Kumar D, et al. Deficit of p66ShcA restores redox-sensitive stress response program in cisplatin-induced acute kidney injury. Exp Mol Pathol. 2013;94:445–452
  • Toussaint ND. Extracellular matrix calcification in chronic kidney disease. Curr Opin Nephrol Hypertens. 2011;20:360–368
  • Acloque H, Adams MS, Fishwick K, et al. Epithelial--mesenchymal transitions: the importance of changing cell state in development and disease. J Clin Invest. 2009;119:1438–1449
  • Liu Y. New insights into epithelial--mesenchymal transition in kidney fibrosis. J Am Soc Nephrol. 2010;21:212–222
  • Zhang A, Jia Z, Guo X, Yang T. Aldosterone induces epithelial-mesenchymal transition via ROS of mitochondrial origin. Am J Physiol Renal Physiol. 2007;293:F723–F731
  • Hock MB, Kralli A. Transcriptional control of mitochondrial biogenesis and function. Annu Rev Physiol. 2009;71:177–203
  • Yuan Y, Chen Y, Zhang P, et al. Mitochondrial dysfunction accounts for aldosterone-induced epithelial-to-mesenchymal transition of renal proximal tubular epithelial cells. Free Radic Biol Med. 2012;53:30–43
  • Sorokin A. Endothelin signaling and actions in the renal mesangium. Contrib Nephrol. 2011;172:50–62
  • Foschi M, Franchi F, Han J, La Villa G, Sorokin A. Endothelin-1 induces serine phosphorylation of the adaptor protein p66Shc and its association with 14-3-3 protein in glomerular mesangial cells. J Biol Chem. 2001;276:26640–26647
  • Chao DT, Korsmeyer SJ. BCL-2 family: regulators of cell death. Annu Rev Immunol. 1998;16:395–419
  • Nissenson AR. Acute renal failure: definition and pathogenesis. Kidney Int Suppl. 1998;66:S7–10
  • Shichiri M, Yokokura M, Marumo F, Hirata Y. Endothelin-1 inhibits apoptosis of vascular smooth muscle cells induced by nitric oxide and serum deprivation via MAP kinase pathway. Arterioscler Thromb Vasc Biol. 2000;20:989–997
  • Nangaku M, Couser WG. Mechanisms of immune-deposit formation and the mediation of immune renal injury. Clin Exp Nephrol. 2005;9:183–191
  • Finetti F, Pellegrini M, Ulivieri C, et al. The proapoptotic and antimitogenic protein p66SHC acts as a negative regulator of lymphocyte activation and autoimmunity. Blood. 2008;111:5017–5027
  • Rajendran R, Garva R, Krstic-Demonacos M, Demonacos C. Sirtuins: molecular traffic lights in the crossroad of oxidative stress, chromatin remodeling, and transcription. J Biomed Biotechnol. 2011;2011:368276–368292
  • Zhou S, Chen HZ, Wan YZ, et al. Repression of P66Shc expression by SIRT1 contributes to the prevention of hyperglycemia-induced endothelial dysfunction. Circ Res. 2011;109:639–648
  • Xu Y, Nie L, Yin YG, et al. Resveratrol protects against hyperglycemia-induced oxidative damage to mitochondria by activating SIRT1 in rat mesangial cells. Toxicol Appl Pharmacol. 2012;259:395–401
  • Yang L, Bailey L, Baltimore D, Wang P. Targeting lentiviral vectors to specific cell types in vivo. Proc Natl Acad Sci USA. 2006;103:11479–11484
  • Wang H, Ghosh A, Baigude H, et al. Therapeutic gene silencing delivered by a chemically modified small interfering RNA against mutant SOD1 slows amyotrophic lateral sclerosis progression. J Biol Chem. 2008;283:15845–15852

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