메뉴 건너뛰기




Volumn 1813, Issue 7, 2011, Pages 1279-1285

Caloric excess or restriction mediated modulation of metabolic enzyme acetylation-proposed effects on cardiac growth and function

Author keywords

Acetyl CoA; Acetyltransferase; Cardiac contraction; Cardiac hypertrophy; NAD+; Sirtuins

Indexed keywords

REACTIVE OXYGEN METABOLITE;

EID: 79957965071     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.01.032     Document Type: Review
Times cited : (12)

References (100)
  • 1
    • 75649084186 scopus 로고    scopus 로고
    • Cardiovascular risk factor trends and potential for reducing coronary heart disease mortality in the United States of America
    • World Health Organ
    • S. Capewell, E.S. Ford, J.B. Croft, J.A. Critchley, K.J. Greenlund, D.R. Labarthe, Cardiovascular risk factor trends and potential for reducing coronary heart disease mortality in the United States of America, Bull. World Health Organ, 88 120-130.
    • Bull. , vol.88 , pp. 120-130
    • Capewell, S.1    Ford, E.S.2    Croft, J.B.3    Critchley, J.A.4    Greenlund, K.J.5    Labarthe, D.R.6
  • 5
    • 63849162173 scopus 로고    scopus 로고
    • AMP-activated protein kinase: a core signalling pathway in the heart
    • Kim A.S., Miller E.J., Young L.H. AMP-activated protein kinase: a core signalling pathway in the heart. Acta Physiol. (Oxf) 2009, 196:37-53.
    • (2009) Acta Physiol. (Oxf) , vol.196 , pp. 37-53
    • Kim, A.S.1    Miller, E.J.2    Young, L.H.3
  • 7
    • 77950788493 scopus 로고    scopus 로고
    • Shedding light on the enigma of myocardial lipotoxicity: the involvement of known and putative regulators of fatty acid storage and mobilization
    • Brindley D.N., Kok B.P., Kienesberger P.C., Lehner R., Dyck J.R. Shedding light on the enigma of myocardial lipotoxicity: the involvement of known and putative regulators of fatty acid storage and mobilization. Am. J. Physiol. Endocrinol. Metab. 2010, 298:E897-E908.
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.298
    • Brindley, D.N.1    Kok, B.P.2    Kienesberger, P.C.3    Lehner, R.4    Dyck, J.R.5
  • 9
    • 67349249847 scopus 로고    scopus 로고
    • Type 2 diabetes, mitochondrial biology and the heart
    • Sack M.N. Type 2 diabetes, mitochondrial biology and the heart. J. Mol. Cell. Cardiol. 2009, 46:842-849.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 842-849
    • Sack, M.N.1
  • 10
    • 76149131004 scopus 로고    scopus 로고
    • The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance
    • Pagel-Langenickel I., Bao J., Pang L., Sack M.N. The role of mitochondria in the pathophysiology of skeletal muscle insulin resistance. Endocr. Rev. 2010, 31:25-51.
    • (2010) Endocr. Rev. , vol.31 , pp. 25-51
    • Pagel-Langenickel, I.1    Bao, J.2    Pang, L.3    Sack, M.N.4
  • 11
    • 39749098677 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: hypertension, diabetes, obesity/sleep apnea, and hypertrophic and infiltrative cardiomyopathy
    • Desai A., Fang J.C. Heart failure with preserved ejection fraction: hypertension, diabetes, obesity/sleep apnea, and hypertrophic and infiltrative cardiomyopathy. Heart Fail. Clin. 2008, 4:87-97.
    • (2008) Heart Fail. Clin. , vol.4 , pp. 87-97
    • Desai, A.1    Fang, J.C.2
  • 12
    • 0342408791 scopus 로고
    • Serial studies on the metabolism of human adipose tissue. II. Effects of caloric restriction and refeeding on lipogenesis, and the uptake and release of free fatty acids in obese and nonobese individuals
    • Goldrick R.B., Hirsch J. Serial studies on the metabolism of human adipose tissue. II. Effects of caloric restriction and refeeding on lipogenesis, and the uptake and release of free fatty acids in obese and nonobese individuals. J. Clin. Invest. 1964, 43:1793-1804.
    • (1964) J. Clin. Invest. , vol.43 , pp. 1793-1804
    • Goldrick, R.B.1    Hirsch, J.2
  • 13
    • 36848999820 scopus 로고    scopus 로고
    • Short-term caloric restriction induces accumulation of myocardial triglycerides and decreases left ventricular diastolic function in healthy subjects
    • van der Meer R.W., Hammer S., Smit J.W., Frolich M., Bax J.J., Diamant M., Rijzewijk L.J., de R.A., Romijn J.A., Lamb H.J. Short-term caloric restriction induces accumulation of myocardial triglycerides and decreases left ventricular diastolic function in healthy subjects. Diabetes 2007, 56:2849-2853.
    • (2007) Diabetes , vol.56 , pp. 2849-2853
    • van der Meer, R.W.1    Hammer, S.2    Smit, J.W.3    Frolich, M.4    Bax, J.J.5    Diamant, M.6    Rijzewijk, L.J.7    de, R.A.8    Romijn, J.A.9    Lamb, H.J.10
  • 14
    • 39049116617 scopus 로고    scopus 로고
    • Progressive caloric restriction induces dose-dependent changes in myocardial triglyceride content and diastolic function in healthy men
    • Hammer S., van der Meer R.W., Lamb H.J., Schar M., de R.A., Smit J.W., Romijn J.A. Progressive caloric restriction induces dose-dependent changes in myocardial triglyceride content and diastolic function in healthy men. J. Clin. Endocrinol. Metab. 2008, 93:497-503.
    • (2008) J. Clin. Endocrinol. Metab. , vol.93 , pp. 497-503
    • Hammer, S.1    van der Meer, R.W.2    Lamb, H.J.3    Schar, M.4    de, R.A.5    Smit, J.W.6    Romijn, J.A.7
  • 15
    • 2342647592 scopus 로고    scopus 로고
    • Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans
    • Fontana L., Meyer T.E., Klein S., Holloszy J.O. Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans. Proc. Natl Acad. Sci. USA 2004, 101:6659-6663.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6659-6663
    • Fontana, L.1    Meyer, T.E.2    Klein, S.3    Holloszy, J.O.4
  • 16
    • 50949116173 scopus 로고    scopus 로고
    • Prolonged caloric restriction in obese patients with type 2 diabetes mellitus decreases myocardial triglyceride content and improves myocardial function
    • Hammer S., Snel M., Lamb H.J., Jazet I.M., van der Meer R.W., Pijl H., Meinders E.A., Romijn J.A., de R.A., Smit J.W. Prolonged caloric restriction in obese patients with type 2 diabetes mellitus decreases myocardial triglyceride content and improves myocardial function. J. Am. Coll. Cardiol. 2008, 52:1006-1012.
    • (2008) J. Am. Coll. Cardiol. , vol.52 , pp. 1006-1012
    • Hammer, S.1    Snel, M.2    Lamb, H.J.3    Jazet, I.M.4    van der Meer, R.W.5    Pijl, H.6    Meinders, E.A.7    Romijn, J.A.8    de, R.A.9    Smit, J.W.10
  • 19
    • 77949343027 scopus 로고    scopus 로고
    • The cardiomyocyte circadian clock: emerging roles in health and disease
    • Durgan D.J., Young M.E. The cardiomyocyte circadian clock: emerging roles in health and disease. Circ. Res. 2010, 106:647-658.
    • (2010) Circ. Res. , vol.106 , pp. 647-658
    • Durgan, D.J.1    Young, M.E.2
  • 20
    • 0035827721 scopus 로고    scopus 로고
    • Clock genes in the heart: characterization and attenuation with hypertrophy
    • Young M.E., Razeghi P., Taegtmeyer H. Clock genes in the heart: characterization and attenuation with hypertrophy. Circ. Res. 2001, 88:1142-1150.
    • (2001) Circ. Res. , vol.88 , pp. 1142-1150
    • Young, M.E.1    Razeghi, P.2    Taegtmeyer, H.3
  • 22
    • 27444441492 scopus 로고    scopus 로고
    • Reduced mitochondrial oxidative capacity and increased mitochondrial uncoupling impair myocardial energetics in obesity
    • Boudina S., Sena S., O'Neill B.T., Tathireddy P., Young M.E., Abel E.D. Reduced mitochondrial oxidative capacity and increased mitochondrial uncoupling impair myocardial energetics in obesity. Circulation 2005, 112:2686-2695.
    • (2005) Circulation , vol.112 , pp. 2686-2695
    • Boudina, S.1    Sena, S.2    O'Neill, B.T.3    Tathireddy, P.4    Young, M.E.5    Abel, E.D.6
  • 23
    • 34548848059 scopus 로고    scopus 로고
    • Mitochondrial energetics in the heart in obesity-related diabetes: direct evidence for increased uncoupled respiration and activation of uncoupling proteins
    • Boudina S., Sena S., Theobald H., Sheng X., Wright J.J., Hu X.X., Aziz S., Johnson J.I., Bugger H., Zaha V.G., Abel E.D. Mitochondrial energetics in the heart in obesity-related diabetes: direct evidence for increased uncoupled respiration and activation of uncoupling proteins. Diabetes 2007, 56:2457-2466.
    • (2007) Diabetes , vol.56 , pp. 2457-2466
    • Boudina, S.1    Sena, S.2    Theobald, H.3    Sheng, X.4    Wright, J.J.5    Hu, X.X.6    Aziz, S.7    Johnson, J.I.8    Bugger, H.9    Zaha, V.G.10    Abel, E.D.11
  • 24
    • 33644784921 scopus 로고    scopus 로고
    • Increased myocardial oxygen consumption reduces cardiac efficiency in diabetic mice
    • How O.J., Aasum E., Severson D.L., Chan W.Y., Essop M.F., Larsen T.S. Increased myocardial oxygen consumption reduces cardiac efficiency in diabetic mice. Diabetes 2006, 55:466-473.
    • (2006) Diabetes , vol.55 , pp. 466-473
    • How, O.J.1    Aasum, E.2    Severson, D.L.3    Chan, W.Y.4    Essop, M.F.5    Larsen, T.S.6
  • 27
    • 0036353834 scopus 로고    scopus 로고
    • Echocardiographic assessment of cardiac function in diabetic db/db and transgenic db/db-hGLUT4 mice
    • Semeniuk L.M., Kryski A.J., Severson D.L. Echocardiographic assessment of cardiac function in diabetic db/db and transgenic db/db-hGLUT4 mice. Am. J. Physiol. Heart Circ. Physiol. 2002, 283:H976-H982.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Semeniuk, L.M.1    Kryski, A.J.2    Severson, D.L.3
  • 28
    • 0034003574 scopus 로고    scopus 로고
    • Alteration in left ventricular diastolic filling and accumulation of myocardial collagen at insulin-resistant prediabetic stage of a type II diabetic rat model
    • Mizushige K., Yao L., Noma T., Kiyomoto H., Yu Y., Hosomi N., Ohmori K., Matsuo H. Alteration in left ventricular diastolic filling and accumulation of myocardial collagen at insulin-resistant prediabetic stage of a type II diabetic rat model. Circulation 2000, 101:899-907.
    • (2000) Circulation , vol.101 , pp. 899-907
    • Mizushige, K.1    Yao, L.2    Noma, T.3    Kiyomoto, H.4    Yu, Y.5    Hosomi, N.6    Ohmori, K.7    Matsuo, H.8
  • 38
    • 70350706093 scopus 로고    scopus 로고
    • The emerging characterization of lysine residue deacetylation on the modulation of mitochondrial function and cardiovascular biology
    • Lu Z., Scott I., Webster B.R., Sack M.N. The emerging characterization of lysine residue deacetylation on the modulation of mitochondrial function and cardiovascular biology. Circ. Res. 2009, 105:830-841.
    • (2009) Circ. Res. , vol.105 , pp. 830-841
    • Lu, Z.1    Scott, I.2    Webster, B.R.3    Sack, M.N.4
  • 39
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T., Deng C.X., Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature 2009, 460:587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 40
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G., Guarente L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 2004, 73:417-435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 41
    • 38649132337 scopus 로고    scopus 로고
    • Mitochondria-a nexus for aging, calorie restriction, and sirtuins?
    • Guarente L. Mitochondria-a nexus for aging, calorie restriction, and sirtuins?. Cell 2008, 132:171-176.
    • (2008) Cell , vol.132 , pp. 171-176
    • Guarente, L.1
  • 42
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 2000, 273:793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 43
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction
    • Haigis M.C., Guarente L.P. Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006, 20:2913-2921.
    • (2006) Genes Dev. , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 44
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T., Lomb D.J., Haigis M.C., Guarente L. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 2009, 137:560-570.
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 45
    • 38649123072 scopus 로고    scopus 로고
    • Conserved metabolic regulatory functions of sirtuins
    • Schwer B., Verdin E. Conserved metabolic regulatory functions of sirtuins. Cell Metab. 2008, 7:104-112.
    • (2008) Cell Metab. , vol.7 , pp. 104-112
    • Schwer, B.1    Verdin, E.2
  • 46
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi T., Wang F., Stieren E., Tong Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 2005, 280:13560-13567.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 47
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno M., Sakamoto J., Miura T., Shimamoto K., Horio Y. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem. 2007, 282:6823-6832.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 48
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B., North B.J., Frye R.A., Ott M., Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 2002, 158:647-657.
    • (2002) J. Cell Biol. , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 49
  • 51
    • 42449132299 scopus 로고    scopus 로고
    • The human SIRT3 protein deacetylase is exclusively mitochondrial
    • Cooper H.M., Spelbrink J.N. The human SIRT3 protein deacetylase is exclusively mitochondrial. Biochem. J. 2008, 411:279-285.
    • (2008) Biochem. J. , vol.411 , pp. 279-285
    • Cooper, H.M.1    Spelbrink, J.N.2
  • 52
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • Sundaresan N.R., Samant S.A., Pillai V.B., Rajamohan S.B., Gupta M.P. SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol. 2008, 28:6384-6401.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 53
    • 37549026223 scopus 로고    scopus 로고
    • Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5
    • Nakamura Y., Ogura M., Tanaka D., Inagaki N. Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem. Biophys. Res. Commun. 2008, 366:174-179.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 174-179
    • Nakamura, Y.1    Ogura, M.2    Tanaka, D.3    Inagaki, N.4
  • 54
    • 34247271282 scopus 로고    scopus 로고
    • SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
    • Scher M.B., Vaquero A., Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007, 21:920-928.
    • (2007) Genes Dev. , vol.21 , pp. 920-928
    • Scher, M.B.1    Vaquero, A.2    Reinberg, D.3
  • 55
    • 77951705893 scopus 로고    scopus 로고
    • Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms
    • Bao J., Lu Z., Joseph J.J., Carabenciov D., Dimond C.C., Pang L., Samsel L., McCoy J.P., Leclerc J., Nguyen P., Gius D., Sack M.N. Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms. J. Cell. Biochem. 2010, 110:238-247.
    • (2010) J. Cell. Biochem. , vol.110 , pp. 238-247
    • Bao, J.1    Lu, Z.2    Joseph, J.J.3    Carabenciov, D.4    Dimond, C.C.5    Pang, L.6    Samsel, L.7    McCoy, J.P.8    Leclerc, J.9    Nguyen, P.10    Gius, D.11    Sack, M.N.12
  • 57
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin S.J., Defossez P.A., Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 2000, 289:2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 59
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum E.M., Chen R., Alexander M.S., Zhang Q., Hogg R.T., Gerard R.D., Garcia J.A. Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 2009, 324:1289-1293.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 60
    • 77953289374 scopus 로고    scopus 로고
    • Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose
    • Tong L., Denu J.M. Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose. Biochim. Biophys. Acta 2010.
    • (2010) Biochim. Biophys. Acta
    • Tong, L.1    Denu, J.M.2
  • 61
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., Sinclair D.A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 2002, 277:45099-45107.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 63
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • Revollo J.R., Grimm A.A., Imai S. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. 2004, 279:50754-50763.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 64
    • 27744501798 scopus 로고    scopus 로고
    • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
    • Berger F., Lau C., Dahlmann M., Ziegler M. Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J. Biol. Chem. 2005, 280:36334-36341.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36334-36341
    • Berger, F.1    Lau, C.2    Dahlmann, M.3    Ziegler, M.4
  • 66
    • 73449133720 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase regulates cell survival through autophagy in cardiomyocytes
    • Hsu C.P., Hariharan N., Alcendor R.R., Oka S., Sadoshima J. Nicotinamide phosphoribosyltransferase regulates cell survival through autophagy in cardiomyocytes. Autophagy 2009, 5:1229-1231.
    • (2009) Autophagy , vol.5 , pp. 1229-1231
    • Hsu, C.P.1    Hariharan, N.2    Alcendor, R.R.3    Oka, S.4    Sadoshima, J.5
  • 68
    • 0029800177 scopus 로고    scopus 로고
    • Fatty acid oxidation enzyme gene expression is downregulated in the failing heart
    • Sack M.N., Rader T.A., Park S., Bastin J., McCune S.A., Kelly D.P. Fatty acid oxidation enzyme gene expression is downregulated in the failing heart. Circulation 1996, 94:2837-2842.
    • (1996) Circulation , vol.94 , pp. 2837-2842
    • Sack, M.N.1    Rader, T.A.2    Park, S.3    Bastin, J.4    McCune, S.A.5    Kelly, D.P.6
  • 69
    • 0031598583 scopus 로고    scopus 로고
    • The energy substrate switch during development of heart failure: gene regulatory mechanisms (Review)
    • Sack M.N., Kelly D.P. The energy substrate switch during development of heart failure: gene regulatory mechanisms (Review). Int. J. Mol. Med. 1998, 1:17-24.
    • (1998) Int. J. Mol. Med. , vol.1 , pp. 17-24
    • Sack, M.N.1    Kelly, D.P.2
  • 72
    • 70350447430 scopus 로고    scopus 로고
    • A high-fat diet increases adiposity but maintains mitochondrial oxidative enzymes without affecting development of heart failure with pressure overload
    • Chess D.J., Khairallah R.J., O'Shea K.M., Xu W., Stanley W.C. A high-fat diet increases adiposity but maintains mitochondrial oxidative enzymes without affecting development of heart failure with pressure overload. Am. J. Physiol. Heart Circ. Physiol. 2009, 297:H1585-H1593.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Chess, D.J.1    Khairallah, R.J.2    O'Shea, K.M.3    Xu, W.4    Stanley, W.C.5
  • 76
    • 55549096745 scopus 로고    scopus 로고
    • SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation
    • Lan F., Cacicedo J.M., Ruderman N., Ido Y. SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J. Biol. Chem. 2008, 283:27628-27635.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27628-27635
    • Lan, F.1    Cacicedo, J.M.2    Ruderman, N.3    Ido, Y.4
  • 78
    • 8844247034 scopus 로고    scopus 로고
    • Silent information regulator 2alpha, a longevity factor and class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes
    • Alcendor R.R., Kirshenbaum L.A., Imai S., Vatner S.F., Sadoshima J. Silent information regulator 2alpha, a longevity factor and class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes. Circ. Res. 2004, 95:971-980.
    • (2004) Circ. Res. , vol.95 , pp. 971-980
    • Alcendor, R.R.1    Kirshenbaum, L.A.2    Imai, S.3    Vatner, S.F.4    Sadoshima, J.5
  • 81
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • Sundaresan N.R., Gupta M., Kim G., Rajamohan S.B., Isbatan A., Gupta M.P. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 2009, 119:2758-2771.
    • (2009) J. Clin. Invest. , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6
  • 82
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows W.C., Lee S., Denu J.M. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl Acad. Sci. USA 2006, 103:10230-10235.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 83
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl Acad. Sci. USA 2006, 103:10224-10229.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 86
    • 75349111140 scopus 로고    scopus 로고
    • Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
    • Cimen H., Han M.J., Yang Y., Tong Q., Koc H., Koc E.C. Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry 2010, 49:304-311.
    • (2010) Biochemistry , vol.49 , pp. 304-311
    • Cimen, H.1    Han, M.J.2    Yang, Y.3    Tong, Q.4    Koc, H.5    Koc, E.C.6
  • 87
    • 66249144685 scopus 로고    scopus 로고
    • Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins
    • Law I.K., Liu L., Xu A., Lam K.S., Vanhoutte P.M., Che C.M., Leung P.T., Wang Y. Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins. Proteomics 2009, 9:2444-2456.
    • (2009) Proteomics , vol.9 , pp. 2444-2456
    • Law, I.K.1    Liu, L.2    Xu, A.3    Lam, K.S.4    Vanhoutte, P.M.5    Che, C.M.6    Leung, P.T.7    Wang, Y.8
  • 88
    • 77956173286 scopus 로고    scopus 로고
    • SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
    • Bao J., Scott I., Lu Z., Pang L., Dimond C.C., Gius D., Sack M.N. SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity. Free Radic. Biol. Med. 2010, 49:1230-1237.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1230-1237
    • Bao, J.1    Scott, I.2    Lu, Z.3    Pang, L.4    Dimond, C.C.5    Gius, D.6    Sack, M.N.7
  • 89
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X., Brown K., Hirschey M.D., Verdin E., Chen D. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab. 2010, 12:662-667.
    • (2010) Cell Metab. , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 90
    • 78651468722 scopus 로고    scopus 로고
    • Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
    • Someya S., Yu W., Hallows W.C., Xu J., Vann J.M., Leeuwenburgh C., Tanokura M., Denu J.M., Prolla T.A. Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 2010, 143:802-812.
    • (2010) Cell , vol.143 , pp. 802-812
    • Someya, S.1    Yu, W.2    Hallows, W.C.3    Xu, J.4    Vann, J.M.5    Leeuwenburgh, C.6    Tanokura, M.7    Denu, J.M.8    Prolla, T.A.9
  • 91
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F., Nguyen M., Qin F.X., Tong Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 2007, 6:505-514.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 92
    • 48749098341 scopus 로고    scopus 로고
    • SIRT2 is a negative regulator of anoxia-reoxygenation tolerance via regulation of 14-3-3 zeta and BAD in H9c2 cells
    • Lynn E.G., McLeod C.J., Gordon J.P., Bao J., Sack M.N. SIRT2 is a negative regulator of anoxia-reoxygenation tolerance via regulation of 14-3-3 zeta and BAD in H9c2 cells. FEBS Lett. 2008, 582:2857-2862.
    • (2008) FEBS Lett. , vol.582 , pp. 2857-2862
    • Lynn, E.G.1    McLeod, C.J.2    Gordon, J.P.3    Bao, J.4    Sack, M.N.5
  • 93
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • Vakhrusheva O., Smolka C., Gajawada P., Kostin S., Boettger T., Kubin T., Braun T., Bober E. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ. Res. 2008, 102:703-710.
    • (2008) Circ. Res. , vol.102 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3    Kostin, S.4    Boettger, T.5    Kubin, T.6    Braun, T.7    Bober, E.8
  • 94
    • 67649637998 scopus 로고    scopus 로고
    • Chromatin places metabolism center stage
    • Ladurner A.G. Chromatin places metabolism center stage. Cell 2009, 138:18-20.
    • (2009) Cell , vol.138 , pp. 18-20
    • Ladurner, A.G.1
  • 96
    • 67749124479 scopus 로고    scopus 로고
    • GCN5-mediated transcriptional control of the metabolic coactivator PGC-1beta through lysine acetylation
    • Kelly T.J., Lerin C., Haas W., Gygi S.P., Puigserver P. GCN5-mediated transcriptional control of the metabolic coactivator PGC-1beta through lysine acetylation. J. Biol. Chem. 2009.
    • (2009) J. Biol. Chem.
    • Kelly, T.J.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Puigserver, P.5
  • 97
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}
    • Nemoto S., Fergusson M.M., Finkel T. SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}. J. Biol. Chem. 2005, 280:16456-16460.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 98
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly D.P., Scarpulla R.C. Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Genes Dev. 2004, 18:357-368.
    • (2004) Genes Dev. , vol.18 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 99
    • 22544431970 scopus 로고    scopus 로고
    • The mitochondrial biogenesis regulatory program in cardiac adaptation to ischemia-a putative target for therapeutic intervention
    • McLeod C.J., Pagel I., Sack M.N. The mitochondrial biogenesis regulatory program in cardiac adaptation to ischemia-a putative target for therapeutic intervention. Trends Cardiovasc. Med. 2005, 15:118-123.
    • (2005) Trends Cardiovasc. Med. , vol.15 , pp. 118-123
    • McLeod, C.J.1    Pagel, I.2    Sack, M.N.3
  • 100
    • 0022458178 scopus 로고
    • Changes in CoA pools in hepatic peroxisomes of the rat under various conditions
    • Horie S., Isobe M., Suga T. Changes in CoA pools in hepatic peroxisomes of the rat under various conditions. J. Biochem. 1986, 99:1345-1352.
    • (1986) J. Biochem. , vol.99 , pp. 1345-1352
    • Horie, S.1    Isobe, M.2    Suga, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.