The NAD ratio redox paradox: why does too much reductive power cause oxidative stress?

References

• Avogaro A, Crepaldi C, Miola M, et al. (1996). High blood ketone body concentration in type 2 non-insulin dependent diabetic patients. J Endocrinol Invest 19:99–105
   PubMed Web of Science ®Google Scholar
• Befroy DE, Petersen KF, Dufour S, et al. (2007). Impaired mitochondrial substrate oxidation in muscle of insulin-resistant offspring of type 2 diabetic patients. Diabetes 56:1376–81
   PubMed Web of Science ®Google Scholar
• Berg JM, Tymoczko JL, Stryer L. (2002). Biochemistry. 5th ed. New York, NY: W H Freeman, Section 30.5, Ethanol Alters Energy Metabolism in the Liver
   Google Scholar
• Berríos-Rivera SJ, Bennett GN, San KY. (2002). Metabolic engineering of Escherichia coli: increase of NADH availability by overexpressing an NAD(+)-dependent formate dehydrogenase. Metab Eng 4:217–29
   PubMed Web of Science ®Google Scholar
• Beyer TA, Xu W, Teupser D, et al. (2008). Impaired liver regeneration in Nrf2 knockout mice: role of ROS-mediated insulin/IGF-1 resistance. EMBO J 27:212–23
   Google Scholar
• Blinova K, Carroll S, Bose S, et al. (2005). Distribution of mitochondrial NADH fluorescence lifetimes: steady-state kinetics of matrix NADH interactions. Biochemistry 44:2585–94
   Google Scholar
• Boden, G. (2003). Effects of free fatty acids (FFA) on glucose metabolism: significance for insulin resistance and type 2 diabetes. Exp Clin Endocrinol Diabetes 111:121–4
   PubMed Web of Science ®Google Scholar
• Brownlee M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813–20
   PubMed Web of Science ®Google Scholar
• Brownlee M, Cerami, A. (1981). The biochemistry of the complications of diabetes-mellitus. Ann Rev Biochem 50:385–432
   PubMed Web of Science ®Google Scholar
• Cantó C, Auwerx J. (2009). PGC-1 alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Curr Opin Lipidol 20:98–105
   PubMed Web of Science ®Google Scholar
• Chabi B, Adhihetty PJ, O’Leary MF, et al. (2009). Relationship between Sirt1 expression and mitochondrial proteins during conditions of chronic muscle use and disuse. J Appl Physiol 107:1730–5
   PubMedGoogle Scholar
• Chau MD, Gao J, Yang Q, et al. (2010). Fibroblast growth factor 21 regulates energy metabolism by activating the AMPK-SIRT1-PGC-1alpha pathway. Proc Natl Acad Sci USA 107:12553–8
   PubMed Web of Science ®Google Scholar
• Chaudhary N, Pfluger PT. (2009). Metabolic benefits from Sirt1 and Sirt1 activators. Curr Opin Clin Nutr Metab Care 12:431–7
   PubMed Web of Science ®Google Scholar
• Choi YS, Kim S, Pak YK. (2001). Mitochondrial transcription factor A (mtTFA) and diabetes. Diabetes Res Clin Pract 54:S3–9
   Google Scholar
• Chung SS, Ho EC, Lam KS, Chung SK. (2003). Contribution of polyol pathway to diabetes-induced oxidative stress. J Am Soc Nephrol 14:S233–6
   PubMed Web of Science ®Google Scholar
• Costa CD, Hammes TO, Rohden F, et al. (2009). SIRT1 transcription is decreased in visceral adipose tissue of morbidly obese patients with severe hepatic steatosis. Obes Surg 20:633–9
   PubMed Web of Science ®Google Scholar
• Feige JN, Lagouge M, Canto C, et al. (2008). Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation. Cell Metab 8:347–58
   PubMed Web of Science ®Google Scholar
• Frohlich J, Steiner G. (2000). Dyslipidaemia and coagulation defects of insulin resistance. Int J Clin Pract Suppl 113:14–22
   Google Scholar
• Gardner CD, Eguchi S, Reynolds CM, et al. (2003). Hydrogen peroxide inhibits insulin signaling in vascular smooth muscle cells. Exp Biol Med (Maywood) 228:836–42
   PubMed Web of Science ®Google Scholar
• Gembal M, Gilon P, Henquin JC. (1992). Evidence that glucose can control insulin release independently from its action on ATP-sensitive K+ channels in mouse B cells. J Clin Invest 89:1288–95
   PubMed Web of Science ®Google Scholar
• Goldstein BJ, Mahadev K, Wu X, et al. (2005). Role of insulin-induced reactive oxygen species in the insulin signaling pathway. Antioxid Redox Signal 7:1021–31
   PubMed Web of Science ®Google Scholar
• Gumaa KA, McLean P, Greenbaum AL. (1971). Compartmentation in relation to metabolic control in liver. Essays Biochem 7:39–86
   PubMedGoogle Scholar
• Gurd BJ, Yoshida Y, Lally J, et al. (2009). The deacetylase enzyme SIRT1 is not associated with oxidative capacity in rat heart and skeletal muscle and its overexpression reduces mitochondrial biogenesis. J Physiol 587:1817–28
   PubMedGoogle Scholar
• Hammes HP, Du X, Edelstein D, et al. (2003). Benfotiamine blocks three major pathways of hyperglycemic damage and prevents experimental diabetic retinopathy. Nat Med 9:294–9
   PubMed Web of Science ®Google Scholar
• Hardie DG, Carling D. (1997). The AMP-activated protein kinase – fuel gauge of the mammalian cell? Eur J Biochem 246:259–73
   PubMedGoogle Scholar
• Henquin JC, Meissner P. (1984). Significance of ionic fluxes and changes in membrane potential for stimulus-secretion coupling in pancreatic B-cells. Experientia (Basel) 40:1043–52
   PubMedGoogle Scholar
• Houten SM, Auwerx J. (2004). PGC-1α: Turbocharging mitochondria. Cell 119:5–7
   PubMedGoogle Scholar
• Hwang YC, Bakr S, Ellery CA, et al. (2003). Sorbitol dehydrogenase: a novel target for adjunctive protection of ischemic myocardium. FASEB J 17:2331–3
   PubMedGoogle Scholar
• Ido Y. (2007). Pyridine nucleotide redox abnormalities in diabetes. Antioxid Redox Signal 9:931–42
   PubMedGoogle Scholar
• Ii S, Ohta M, Kudo E, et al. (2004). Redox state-dependent and sorbitol accumulation-independent diabetic albuminuria in mice with transgene-derived human aldose reductase and sorbitol dehydrogenase deficiency. Diabetologia 47:541–8
   PubMedGoogle Scholar
• Jäger S, Handschin C, St-Pierre J, Spiegelman BM. (2007). AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc Natl Acad Sci USA 104:12017–22
   PubMed Web of Science ®Google Scholar
• Kaneko M, Bucciarelli L, Hwang YC, et al. (2005). Aldose reductase and AGE-RAGE pathways: key players in myocardial ischemic injury. Ann NY Acad Sci 1043:702–9
   PubMed Web of Science ®Google Scholar
• Kelley DE, Mandarino LJ. (1990). Hyperglycemia normalizes insulin-stimulated skeletal muscle glucose oxidation and storage in noninsulin-dependent diabetes mellitus. J Clin Invest 86:1999–2007
   PubMedGoogle Scholar
• Laye MJ, Rector RS, Warner SO, et al. (2009). Changes in visceral adipose tissue mitochondrial content with type 2 diabetes and daily voluntary wheel running in OLETF rats. J Physiol, 587:3729–39
   PubMedGoogle Scholar
• Liang W, Ward, WF. (2006). PGC-1α: a key regulator of energy metabolism. Adv Physiol Educ, 30:145–51
   PubMed Web of Science ®Google Scholar
• López–Lluch G, Hunt N, Jones B, et al. (2006). Calorie restriction induces mitochondrial biogenesis and bioenergetic efficiency. Proc Natl Acad Sci USA 103:1768–73
   PubMed Web of Science ®Google Scholar
• MacDonald MJ. (1995). Feasibility of a mitochondrial pyruvate malate shuttle in pancreatic islets. Further implication of cytosolic NADPH in insulin secretion. J Biol Chem 270:20051–8
   PubMed Web of Science ®Google Scholar
• McGarry JD, Dobbins RL. (1999). Fatty acids, lipotoxicity and insulin secretion. Diabetologia 42:128–38
   PubMed Web of Science ®Google Scholar
• Menshikova EV, Ritov VB, Fairfull L, et al. (2006). Effects of exercise on mitochondrial content and function in aging human skeletal muscle. J Gerontol A Biol Sci Med Sci 61:534–40
   PubMed Web of Science ®Google Scholar
• Miettinen TA, Taskinen MR, Pelkonen R, Nikkilä EA. (1969). Glucose tolerance and plasma insulin in man during acute and chronic administration of nicotinic acid. Acta Med Scand 186:247–53
   PubMedGoogle Scholar
• Mintun MA, Vlassenko AG, Rundle MM, Raichle ME. (2004). Increased lactate/pyruvate ratio augments blood flow in physiologically activated human brain. Proc Natl Acad Sci USA 101:659–64
   PubMedGoogle Scholar
• Nemoto S, Fergusson MM, Finkel T. (2005). SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α. J Biol Chem 280:16456–60
   PubMed Web of Science ®Google Scholar
• Nishikawa T, Edelstein D, Du XL, et al. (2000). Normalizing mitochondrial superox-ide production blocks three pathways of hyperglycaemic damage. Nature 404:787–90
   PubMed Web of Science ®Google Scholar
• Okazaki IJ, Moss J. (1999). Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases. Annu Rev Nutr 19:485–509
   PubMedGoogle Scholar
• Oliveira RL, Ueno M, de Souza CT, et al. (2004). Cold-induced PGC-1alpha expression modulates muscle glucose uptake through an insulin receptor/Akt-independent, AMPK-dependent pathway. Am J Physiol Endocrinol Metab 287:E686–95
   Google Scholar
• Palmeira CM, Rolo AP, Berthiaume J, et al. (2007). Hyperglycemia decreases mitochondrial function: the regulatory role of mitochondrial biogenesis. Toxicol Appl Pharmacol 225:214–20
   PubMed Web of Science ®Google Scholar
• Purushotham A, Schug TT, Xu Q, et al. (2009). Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab 9:327–38
   PubMed Web of Science ®Google Scholar
• Rabøl R, Højberg PM, Almdal T, et al. (2009). Effect of hyperglycemia on mitochondrial respiration in type 2 diabetes. J Clin Endocrinol Metab 94:1372–8
   PubMedGoogle Scholar
• Randle PJ, Garland PB, Hales CN, Newsholme EA. (1963). The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. Lancet 1:785–9
   Google Scholar
• Rao P, Kodavanti P, Mehendale H. (1991). Biochemical methods of studying hepatotoxicity. In Meeks RG Harrison SD, Bull RJ, eds. Hepatotoxicity. Boca Raton (FL): CRC Press, 241–326
   Google Scholar
• Rodgers JT, Lerin C, Haas W, et al. (2005). Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434:113–18
   PubMed Web of Science ®Google Scholar
• Rodrigues F, Ludovico P, Leão C. (2006). Sugar metabolism in yeasts: an overview of aerobic and anaerobic glucose Catabolism. In Péter G, Rosa C, eds. Biodiversity and ecophysiology of yeasts. The yeast handbook. Berlin: Springer-Verlag, 101–21
   Google Scholar
• Rolo AP, Palmeira CM. (2006). Diabetes and mitochondrial function: role of hyperglycemia and oxidative stress. Toxicol Appl Pharmacol 212:167–78
   PubMed Web of Science ®Google Scholar
• Ruderman NB, Xu XJ, Nelson L, et al. (2010). AMPK and SIRT1: a long-standing partnership? Am J Physiol Endocrinol Metab 298:E751–60
   PubMed Web of Science ®Google Scholar
• Salway JG. (1999). Metabolism at a glance. 2nd ed. Cambridge: Blackwell Science
   Google Scholar
• Scarpulla RC. (2008). Transcriptional paradigms in mammalian mitochondrial biogenesis and function. Physiol Rev 88:611–38
   PubMed Web of Science ®Google Scholar
• Shaw JE, Sicree RA, Zimmet PZ. (2009). Global estimates of the prevalence of diabetes for 2010 and 2030. Diabetes Res Clin Pract 87:4–14
   PubMed Web of Science ®Google Scholar
• Sinclair DA. (2005). Toward a unified theory of caloric restriction and longevity regulation. Mech Ageing Dev 126:987–1002
   PubMed Web of Science ®Google Scholar
• Steinberg GR, Kemp BE. (2009). AMPK in health and disease. Physiol Rev 89:1025–78
   PubMed Web of Science ®Google Scholar
• Streffer C, Brauer W, Benes J. (1971). Levels of pyridine nucleotides after repeated applications of nicotinic acid in animal tissues. In Gey KF, Carlson LA, eds. Metabolic effects of nicotinic acid and its derivatives. Bern, Switzerland: Hans Huber Verlag, 97–114
   Google Scholar
• Tilton RG, Chang K, Nyengaard JR, et al. (1995). Inhibition of sorbitol dehydrogenase. Effects on vascular and neural dysfunction in streptozocin-induced diabetic rats. Diabetes 44:234–42
   Google Scholar
• Tilton RG, Kawamura T, Chang KC, et al. (1997). Vascular dysfunction induced by elevated glucose levels in rats is mediated by vascular endothelial growth factor. J Clin Invest, 99:2192–202
   PubMed Web of Science ®Google Scholar
• Ukropcova B, Sereda O, de Jonge L, et al. (2007). Family history of diabetes links impaired substrate switching and reduced mitochondrial content in skeletal muscle. Diabetes 56:720–7
   PubMed Web of Science ®Google Scholar
• Vannini P, Marchesini G, Forlani G, et al. (1982). Branched-chain amino acids and alanine as indices of the metabolic control in type 1 (insulin-dependent) and type 2 (non-insulin-dependent) diabetic patients. Diabetologia 22:217–19
   PubMedGoogle Scholar
• Vemuri GN, Eiteman MA, McEwen JE, et al. (2007). Increasing NADH oxidation reduces overflow metabolism in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 104:2402–7
   PubMed Web of Science ®Google Scholar
• Vettor R, Lombardi AM, Fabris R, et al. (1997). Lactate infusion in anesthetized rats produces insulin resistance in heart and skeletal muscles. Metabolism 46:684–90
   PubMedGoogle Scholar
• Wahlberg G, Walldius G, Efendic S. (1992). Effects of nicotinic acid treatment on glucose tolerance and glucose incorporation into adipose tissue in hypertriglyceridemia. Scand J Clin Lab Invest 52:537–45
   PubMed Web of Science ®Google Scholar
• Winder WW. (2001). Energy-sensing and signaling by AMP-activated protein kinase in skeletal muscle. J Appl Physiol 91:1017–28
   PubMed Web of Science ®Google Scholar
• Wong J, McLennan SV, Molyneaux L, et al. (2009). Mitochondrial DNA content in peripheral blood monocytes: relationship with age of diabetes onset and diabetic complications. Diabetologia 52:1953–61
   PubMed Web of Science ®Google Scholar