메뉴 건너뛰기




Volumn 34, Issue 8, 2015, Pages 1110-1125

SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth

Author keywords

acetylation; GOT2; malate aspartate NADH shuttle; pancreatic cancer

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE AMINOTRANSFERASE ISOENZYME 2; ASPARTIC ACID; LYSINE; MALATE DEHYDROGENASE; MALIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SIRTUIN 3; MALIC ACID DERIVATIVE; SIRT3 PROTEIN, HUMAN;

EID: 84927698067     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201591041     Document Type: Article
Times cited : (158)

References (51)
  • 1
    • 0021867367 scopus 로고
    • Coupled reaction of immobilized aspartate aminotransferase and malate dehydrogenase. A plausible model for the cellular behaviour of these enzymes
    • Arrio-Dupont M, Coulet PR, Gautheron DC, (1985) Coupled reaction of immobilized aspartate aminotransferase and malate dehydrogenase. A plausible model for the cellular behaviour of these enzymes. Biochim Biophys Acta 829: 58-68
    • (1985) Biochim Biophys Acta , vol.829 , pp. 58-68
    • Arrio-Dupont, M.1    Coulet, P.R.2    Gautheron, D.C.3
  • 2
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • Avalos JL, Bever KM, Wolberger C, (2005) Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 17: 855-868
    • (2005) Mol Cell , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 3
    • 0017087227 scopus 로고
    • Enzyme - Enzyme complexes between aspartate aminotransferase and malate dehydrogenase from pig heart muscle
    • Backman L, Johansson G, (1976) Enzyme-enzyme complexes between aspartate aminotransferase and malate dehydrogenase from pig heart muscle. FEBS Lett 65: 39-43
    • (1976) FEBS Lett , vol.65 , pp. 39-43
    • Backman, L.1    Johansson, G.2
  • 4
    • 0032143925 scopus 로고    scopus 로고
    • Malate-aspartate shuttle, cytoplasmic NADH redox potential, and energetics in vascular smooth muscle
    • Barron JT, Gu L, Parrillo JE, (1998) Malate-aspartate shuttle, cytoplasmic NADH redox potential, and energetics in vascular smooth muscle. J Mol Cell Cardiol 30: 1571-1579
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 1571-1579
    • Barron, J.T.1    Gu, L.2    Parrillo, J.E.3
  • 5
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA, (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 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
  • 6
    • 0017254523 scopus 로고
    • The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate
    • Bryce CF, Williams DC, John RA, Fasella P, (1976) The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate. Biochem J 153: 571-577
    • (1976) Biochem J , vol.153 , pp. 571-577
    • Bryce, C.F.1    Williams, D.C.2    John, R.A.3    Fasella, P.4
  • 7
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, Zhao S, Xiong Y, (2011) Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep 12: 534-541
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6    Xiong, Y.7
  • 8
    • 84896756082 scopus 로고    scopus 로고
    • Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer
    • Chen Y, Fu LL, Wen X, Wang XY, Liu J, Cheng Y, Huang J, (2014) Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer. Cell Death Dis 5: e1047
    • (2014) Cell Death Dis , vol.5 , pp. e1047
    • Chen, Y.1    Fu, L.L.2    Wen, X.3    Wang, X.Y.4    Liu, J.5    Cheng, Y.6    Huang, J.7
  • 10
    • 84893109709 scopus 로고    scopus 로고
    • Non-invasive in-cell determination of free cytosolic [NAD+]/[NADH] ratios using hyperpolarized glucose show large variations in metabolic phenotypes
    • Christensen CE, Karlsson M, Winther JR, Jensen PR, Lerche MH, (2014) Non-invasive in-cell determination of free cytosolic [NAD+]/[NADH] ratios using hyperpolarized glucose show large variations in metabolic phenotypes. J Biol Chem 289: 2344-2352
    • (2014) J Biol Chem , vol.289 , pp. 2344-2352
    • Christensen, C.E.1    Karlsson, M.2    Winther, J.R.3    Jensen, P.R.4    Lerche, M.H.5
  • 12
    • 0017146107 scopus 로고
    • The malate-aspartate shuttle in heart mitochondria
    • Digerness SB, Reddy WJ, (1976) The malate-aspartate shuttle in heart mitochondria. J Mol Cell Cardiol 8: 779-785
    • (1976) J Mol Cell Cardiol , vol.8 , pp. 779-785
    • Digerness, S.B.1    Reddy, W.J.2
  • 13
    • 0016374514 scopus 로고
    • Oxidation of reduced nicotinamide-adenine dinucleotide by the malate-aspartate shuttle in Ehrlich ascites tumour cells
    • Dionisi O, Longhi G, Eboli ML, Galeotti T, Terranova T, (1974) Oxidation of reduced nicotinamide-adenine dinucleotide by the malate-aspartate shuttle in Ehrlich ascites tumour cells. Biochim Biophys Acta 333: 577-580
    • (1974) Biochim Biophys Acta , vol.333 , pp. 577-580
    • Dionisi, O.1    Longhi, G.2    Eboli, M.L.3    Galeotti, T.4    Terranova, T.5
  • 14
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • Dooley CT, Dore TM, Hanson GT, Jackson WC, Remington SJ, Tsien RY, (2004) Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J Biol Chem 279: 22284-22293
    • (2004) J Biol Chem , vol.279 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 16
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, Khochbin S, Yoshida M, Horinouchi S, (2001) Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci USA 98: 87-92
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 17
    • 0017274411 scopus 로고
    • Occurrence of the malate-aspartate shuttle in various tumor types
    • Greenhouse WV, Lehninger AL, (1976) Occurrence of the malate-aspartate shuttle in various tumor types. Cancer Res 36: 1392-1396
    • (1976) Cancer Res , vol.36 , pp. 1392-1396
    • Greenhouse, W.V.1    Lehninger, A.L.2
  • 18
    • 0017720320 scopus 로고
    • Magnitude of malate-aspartate reduced nicotinamide adenine dinucleotide shuttle activity in intact respiring tumor cells
    • Greenhouse WV, Lehninger AL, (1977) Magnitude of malate-aspartate reduced nicotinamide adenine dinucleotide shuttle activity in intact respiring tumor cells. Cancer Res 37: 4173-4181
    • (1977) Cancer Res , vol.37 , pp. 4173-4181
    • Greenhouse, W.V.1    Lehninger, A.L.2
  • 19
    • 80155145533 scopus 로고    scopus 로고
    • Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
    • Han Q, Robinson H, Cai T, Tagle DA, Li J, (2011) Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV. Biosci Rep 31: 323-332
    • (2011) Biosci Rep , vol.31 , pp. 323-332
    • Han, Q.1    Robinson, H.2    Cai, T.3    Tagle, D.A.4    Li, J.5
  • 22
    • 80053902441 scopus 로고    scopus 로고
    • Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
    • Hung YP, Albeck JG, Tantama M, Yellen G, (2011) Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab 14: 545-554
    • (2011) Cell Metab , vol.14 , pp. 545-554
    • Hung, Y.P.1    Albeck, J.G.2    Tantama, M.3    Yellen, G.4
  • 23
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases
    • Imai S, Guarente L, (2010) Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol Sci 31: 212-220
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 24
    • 77952076257 scopus 로고    scopus 로고
    • Green tea catechins: Inhibitors of glycerol-3-phosphate dehydrogenase
    • Kao CC, Wu BT, Tsuei YW, Shih LJ, Kuo YL, Kao YH, (2010) Green tea catechins: inhibitors of glycerol-3-phosphate dehydrogenase. Planta Med 76: 694-696
    • (2010) Planta Med , vol.76 , pp. 694-696
    • Kao, C.C.1    Wu, B.T.2    Tsuei, Y.W.3    Shih, L.J.4    Kuo, Y.L.5    Kao, Y.H.6
  • 26
    • 84927696997 scopus 로고
    • Phosphorylation coupled to oxidative dihydrodiphosphopyridine nucleotide
    • Lehninger AL, (1951) phosphorylation coupled to oxidative dihydrodiphosphopyridine nucleotide. J Biol Chem 190: 15
    • (1951) J Biol Chem , vol.190 , pp. 15
    • Lehninger, A.L.1
  • 27
    • 0018410190 scopus 로고
    • Evidence for the oxidation of glycolytic NADH by the malate-aspartate shuttle in Ehrlich ascites tumor cells
    • Lopez-Alarcon L, Eboli ML, De Liberali E, Palombini G, Galeotti T, (1979) Evidence for the oxidation of glycolytic NADH by the malate-aspartate shuttle in Ehrlich ascites tumor cells. Arch Biochem Biophys 192: 391-395
    • (1979) Arch Biochem Biophys , vol.192 , pp. 391-395
    • Lopez-Alarcon, L.1    Eboli, M.L.2    De Liberali, E.3    Palombini, G.4    Galeotti, T.5
  • 28
    • 0022930311 scopus 로고
    • Oxidation of reduced cytosolic nicotinamide adenine dinucleotide by the malate-aspartate shuttle in the K-562 human leukemia cell line
    • Lopez-Alarcon L, Eboli ML, (1986) Oxidation of reduced cytosolic nicotinamide adenine dinucleotide by the malate-aspartate shuttle in the K-562 human leukemia cell line. Cancer Res 46: 5589-5591
    • (1986) Cancer Res , vol.46 , pp. 5589-5591
    • Lopez-Alarcon, L.1    Eboli, M.L.2
  • 31
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee PC, Morgan BA, Mittman BA, Smith MM, (1990) Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 247: 841-845
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 33
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N(epsilon)-acetyllysine in recombinant proteins
    • Neumann H, Peak-Chew SY, Chin JW, (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat Chem Biol 4: 232-234
    • (2008) Nat Chem Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 35
    • 0000734010 scopus 로고
    • Lactic dehydrogenase. V. Inhibition by oxamate and by oxalate
    • Novoa WB, Winer AD, Glaid AJ, Schwert GW, (1959) Lactic dehydrogenase. V. Inhibition by oxamate and by oxalate. J Biol Chem 234: 1143-1148
    • (1959) J Biol Chem , vol.234 , pp. 1143-1148
    • Novoa, W.B.1    Winer, A.D.2    Glaid, A.J.3    Schwert, G.W.4
  • 36
    • 0016771971 scopus 로고
    • Glucagon and insulin control of gluconeogenesis in the perfused isolated rat liver. Effects on cellular metabolite distribution
    • Parrilla R, Jimenez I, Ayuso-Parrilla MS, (1975) Glucagon and insulin control of gluconeogenesis in the perfused isolated rat liver. Effects on cellular metabolite distribution. Eur J Biochem 56: 375-383
    • (1975) Eur J Biochem , vol.56 , pp. 375-383
    • Parrilla, R.1    Jimenez, I.2    Ayuso-Parrilla, M.S.3
  • 37
    • 0015069162 scopus 로고
    • Control of the transport of reducing equivalents across the mitochondrial membrane in perfused rat heart
    • Safer B, Smith CM, Williamson JR, (1971) Control of the transport of reducing equivalents across the mitochondrial membrane in perfused rat heart. J Mol Cell Cardiol 2: 111-124
    • (1971) J Mol Cell Cardiol , vol.2 , pp. 111-124
    • Safer, B.1    Smith, C.M.2    Williamson, J.R.3
  • 38
    • 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 BJ, Frye RA, Ott M, Verdin E, (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 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
  • 39
    • 0017645827 scopus 로고
    • Effect of glucagon on metabolite compartmentation in isolated rat liver cells during gluconeogenesis from lactate
    • Siess EA, Brocks DG, Lattke HK, Wieland OH, (1977) Effect of glucagon on metabolite compartmentation in isolated rat liver cells during gluconeogenesis from lactate. Biochem J 166: 225-235
    • (1977) Biochem J , vol.166 , pp. 225-235
    • Siess, E.A.1    Brocks, D.G.2    Lattke, H.K.3    Wieland, O.H.4
  • 42
    • 84858604270 scopus 로고    scopus 로고
    • Metabolic reprogramming: A cancer hallmark even warburg did not anticipate
    • Ward PS, Thompson CB, (2012) Metabolic reprogramming: a cancer hallmark even warburg did not anticipate. Cancer Cell 21: 297-308
    • (2012) Cancer Cell , vol.21 , pp. 297-308
    • Ward, P.S.1    Thompson, C.B.2
  • 43
    • 0014690951 scopus 로고
    • Inhibition of glucagon effects in perfused rat liver by (+)decanoylcarnitine
    • Williamson JR, Browning ET, Thurman RG, Scholz R, (1969) Inhibition of glucagon effects in perfused rat liver by (+)decanoylcarnitine. J Biol Chem 244: 5055-5064
    • (1969) J Biol Chem , vol.244 , pp. 5055-5064
    • Williamson, J.R.1    Browning, E.T.2    Thurman, R.G.3    Scholz, R.4
  • 44
    • 0014755668 scopus 로고
    • Effects of quinolinic acid on the free and total nicotinamide-adenine dinucleotides of rat liver
    • Williamson DH, Mayor F, Veloso D, (1970) Effects of quinolinic acid on the free and total nicotinamide-adenine dinucleotides of rat liver. Hoppe Seylers Z Physiol Chem 351: 287
    • (1970) Hoppe Seylers Z Physiol Chem , vol.351 , pp. 287
    • Williamson, D.H.1    Mayor, F.2    Veloso, D.3
  • 45
    • 0015240541 scopus 로고
    • Control of the removal of reducing equivalents from the cytosol in perfused rat liver
    • Williamson JR, Jakob A, Refino C, (1971) Control of the removal of reducing equivalents from the cytosol in perfused rat liver. J Biol Chem 246: 7632-7641
    • (1971) J Biol Chem , vol.246 , pp. 7632-7641
    • Williamson, J.R.1    Jakob, A.2    Refino, C.3
  • 46
    • 84927696885 scopus 로고    scopus 로고
    • Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase
    • Xu Y, Li F, Lv L, Li T, Zhou X, Deng C, Guan K-L, Lei Q-Y, Xiong Y, (2014) Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase. Cancer Res 3615: 2013
    • (2014) Cancer Res , vol.3615 , pp. 2013
    • Xu, Y.1    Li, F.2    Lv, L.3    Li, T.4    Zhou, X.5    Deng, C.6    Guan, K.-L.7    Lei, Q.-Y.8    Xiong, Y.9
  • 48
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • Yu W, Dittenhafer-Reed KE, Denu JM, (2012) SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J Biol Chem 287: 14078-14086
    • (2012) J Biol Chem , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 49
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J, Pu M, Zhang Z, Lou Z, (2009) Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 8: 1747-1753
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.