Mitochondrial acetylation and diseases of aging

Journal of Aging Research

Volumn 2011, Issue , 2011, Pages

  Wagner, Gregory R ^a   Payne, R Mark ^a  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVATE KINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SIRTUIN; TUMOR SUPPRESSOR PROTEIN;

ACETYLATION; AGING; CANCER GROWTH; CARBON METABOLISM; CARBON UTILIZATION; ENZYME METABOLISM; ENZYME MODIFICATION; EUKARYOTE; HEART FAILURE; HUMAN; MITOCHONDRIAL RESPIRATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROCESSING; REVIEW;

EID: 80052281488     PISSN: 20902204     EISSN: 20902212     Source Type: Journal    
DOI: 10.4061/2011/234875     Document Type: Review

References (121)

1. Strahl B. D., Allis C. D., The language of covalent histone modifications. Nature 2000 403 6765 41 45 2-s2.0-0034610814 10.1038/47412 (Pubitemid 30038513)
2. Kim S. C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N. V., White M., Yang X. J., Zhao Y., Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Molecular Cell 2006 23 4 607 618 2-s2.0-33746992118 10.1016/j.molcel.2006.06.026 (Pubitemid 44205490)
3. Wang Q., Zhang Y., Yang C., Xiong H., Lin Y., Yao J., Li H., Xie LU., Zhao W., Yao Y., Ning Z. B., Zeng R., Xiong Y., Guan K. L., Zhao S., Zhao G. P., Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 2010 327 5968 1004 1007 2-s2.0-77149120797 10.1126/science.1179687
4. Hirschey M. D., Shimazu T., Goetzman E., Jing E., Schwer B., Lombard D. B., Grueter C. A., Harris C., Biddinger S., Ilkayeva O. R., Stevens R. D., Li Y., Saha A. K., Ruderman N. B., Bain J. R., Newgard C. B., Farese R. V., Alt F. W., Kahn C. R., Verdin E., SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 2010 464 1 121 125 2-s2.0-77950806433 10.1038/nature08778
5. Schlicker C., Gertz M., Papatheodorou P., Kachholz B., Becker C. F. W., Steegborn C., Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. Journal of Molecular Biology 2008 382 3 790 801 2-s2.0-50149103440 10.1016/j.jmb.2008.07.048
6. Nakagawa T., Lomb D. J., Haigis M. C., Guarente L., SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 2009 137 3 560 570 2-s2.0-65249087389 10.1016/j.cell.2009.02.026
7. Ahn B. H., Kim H. S., Song S., In H. L., Liu J., Vassilopoulos A., Deng C. X., Finkel T., A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proceedings of the National Academy of Sciences of the United States of America 2008 105 38 14447 14452 2-s2.0-55749084738 10.1073/pnas.0803790105
8. Guarente L., Calorie restriction and SIR2 genes-towards a mechanism. Mechanisms of Ageing and Development 2005 126 9 923 928 2-s2.0-22744444561 10.1016/j.mad.2005.03.013 (Pubitemid 41033172)
9. Haigis M. C., Guarente L. P., Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes and Development 2006 20 21 2913 2921 2-s2.0-33751113602 10.1101/gad.1467506 (Pubitemid 44771725)
10. Krebs H. A., The citric acid cycle and the Szent-Györgyi cycle in pigeon breast muscle. Biochemical Journal 1940 34 5 775 779
11. Mitchell P., Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 1961 191 4784 144 148 2-s2.0-36949083936 10.1038/191144a0
12. Bauer D. E., Hatzivassiliou G., Zhao F., Andreadis C., Thompson C. B., ATP citrate lyase is an important component of cell growth and transformation. Oncogene 2005 24 41 6314 6322 2-s2.0-30544433533 10.1038/sj.onc.1208773 (Pubitemid 43080054)
13. Bloch K., The biological synthesis of cholesterol. Science 1965 150 3692 19 28 2-s2.0-0002380192
14. Edwards P. A., Ericsson J., Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway. Annual Review of Biochemistry 1999 68 157 185 2-s2.0-0032851111 10.1146/annurev.biochem.68.1.157 (Pubitemid 29449190)
15. Nosadini R., Avogaro A., Doria A., Fioretto P., Trevisan R., Morocutti A., Ketone body metabolism: a physiological and clinical overview. Diabetes/Metabolism Reviews 1989 5 3 299 319 2-s2.0-0024556458 (Pubitemid 19116196)
16. Luong A., Hannah V. C., Brown M. S., Goldstein J. L., Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. Journal of Biological Chemistry 2000 275 34 26458 26466 2-s2.0-0034714382 10.1074/jbc.M004160200
17. Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T. T., Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. Journal of Biological Chemistry 2001 276 14 11420 11426 2-s2.0-0035815751 10.1074/jbc.M008782200 (Pubitemid 38089336)
18. Sakakibara I., Fujino T., Ishii M., Tanaka T., Shimosawa T., Miura S., Zhang W., Tokutake Y., Yamamoto J., Awano M., Iwasaki S., Motoike T., Okamura M., Inagaki T., Kita K., Ezaki O., Naito M., Kuwaki T., Chohnan S., Yamamoto T. T., Hammer R. E., Kodama T., Yanagisawa M., Sakai J., Fasting-induced hypothermia and reduced energy production in mice lacking acetyl-CoA synthetase 2. Cell Metabolism 2009 9 2 191 202 2-s2.0-58749117235 10.1016/j.cmet.2008.12. 008
19. Wellen K. E., Hatzivassiliou G., Sachdeva U. M., Bui T. V., Cross J. R., Thompson C. B., ATP-citrate lyase links cellular metabolism to histone acetylation. Science 2009 324 5930 1076 1080 2-s2.0-66249105703 10.1126/science.1164097
20. Gershey E. L., Vidali G., Allfrey V. G., Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. Journal of Biological Chemistry 1968 243 19 5018 5022 2-s2.0-0014409959
21. Inoue A., Fujimoto D., Enzymatic deacetylation of histone. Biochemical and Biophysical Research Communications 1969 36 1 146 150 2-s2.0-0014666991
22. Fujimoto D., Segawa K., Enzymatic deacetylation of f2a2 histone. FEBS Letters 1973 32 1 59 61 2-s2.0-0015846997 10.1016/0014-5793(73)80737-9
23. Kervabon A., Mery J., Parello J., Enzymatic deacetylation of a synthetic peptide fragment of histone H4. FEBS Letters 1979 106 1 93 96 2-s2.0-0018533245
24. Taunton J., Hassig C. A., Schreiber S. L., A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 1996 272 5260 408 411 2-s2.0-0029932598 (Pubitemid 26138177)
25. Jenuwein T., Allis C. D., Translating the histone code. Science 2001 293 5532 1074 1080 2-s2.0-0035839136 10.1126/science.1063127 (Pubitemid 32758077)
26. Copeland A., Buglio D., Younes A., ayounes@mdanderson.org Histone deacetylase inhibitors in lymphoma. Current Opinion in Oncology 2010 22 5 431 436 10.1097/CCO.0b013e32833d5954
27. Gregoretti I. V., Lee Y. M., Goodson H. V., Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. Journal of Molecular Biology 2004 338 1 17 31 2-s2.0-1842578986 10.1016/j.jmb.2004.02.006 (Pubitemid 38429783)
28. Allis C. D., Berger S. L., Cote J., Dent S., Jenuwien T., Kouzarides T., Pillus L., Reinberg D., Shi Y., Shiekhattar R., Shilatifard A., Workman J., Zhang YI., New nomenclature for chromatin-modifying enzymes. Cell 2007 131 4 633 636 2-s2.0-36049028058 10.1016/j.cell.2007.10.039 (Pubitemid 350089969)
29. de Ruijter A. J. M., van Gennip A. H., Caron H. N., Kemp S., van Kuilenburg A. B. P., Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochemical Journal 2003 370 3 737 749 2-s2.0-0037444803 10.1042/BJ20021321 (Pubitemid 36399066)
30. Bannister A. J., Miska E. A., Regulation of gene expression by transcription factor acetylation. Cellular and Molecular Life Sciences 2000 57 8-9 1184 1192 2-s2.0-0033837634 (Pubitemid 30663476)
31. Gu W., Roeder R. G., Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997 90 4 595 606 2-s2.0-0030797585 10.1016/S0092-8674(00)80521-8 (Pubitemid 27357952)
32. Glozak M. A., Sengupta N., Zhang X., Seto E., Acetylation and deacetylation of non-histone proteins. Gene 2005 363 1-2 15 23 2-s2.0-28044471827 10.1016/j.gene.2005.09.010 (Pubitemid 41691888)
33. Bali P., Pranpat M., Bradner J., Balasis M., Fiskus W., Guo F., Rocha K., Kumaraswamy S., Boyapalle S., Atadja P., Seto E., Bhalla K., Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. Journal of Biological Chemistry 2005 280 29 26729 26734 2-s2.0-22844432021 10.1074/jbc.C500186200 (Pubitemid 41040705)
34. Sekimoto T., Matsuyama T., Fukui T., Tanizawa K., Evidence for lysine 80 as general base catalyst of leucine dehydrogenase. Journal of Biological Chemistry 1993 268 36 27039 27045 2-s2.0-0027761914 (Pubitemid 24006416)
35. Yu W., Lin Y., Yao J., Huang W., Lei Q., Xiong Y., Zhao S., Guan K. L., Lysine 88 acetylation negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals. Journal of Biological Chemistry 2009 284 20 13669 13675 2-s2.0-67649395959 10.1074/jbc.M901921200
36. Yuan Z. L., Guan Y. J., Chatterjee D., Chin Y. E., Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 2005 307 5707 269 273 2-s2.0-12244251445 10.1126/science.1105166 (Pubitemid 40116244)
37. Sadoul K., Boyault C., Pabion M., Khochbin S., Regulation of protein turnover by acetyltransferases and deacetylases. Biochimie 2008 90 2 306 312 2-s2.0-38649092744 10.1016/j.biochi.2007.06.009 (Pubitemid 351172566)
38. Yang X. J., Seto E., Lysine acetylation: codified crosstalk with other posttranslational modifications. Molecular Cell 2008 31 4 449 461 2-s2.0-49349107518 10.1016/j.molcel.2008.07.002
39. Onyango P., Celic I., McCaffery J. M., Boeke J. D., Feinberg A. P., SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proceedings of the National Academy of Sciences of the United States of America 2002 99 21 13653 13658 2-s2.0-0037108799 10.1073/pnas. 222538099 (Pubitemid 35215436)
40. Michishita E., Park J. Y., Burneskis J. M., Barrett J. C., Horikawa I., Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Molecular Biology of the Cell 2005 16 10 4623 4635 2-s2.0-26244436281 10.1091/mbc.E05-01-0033 (Pubitemid 41416446)
41. Aquilano K., Vigilanza P., Baldelli S., Pagliei B., Rotilio G., Ciriolo M. R., ciriolo@bio.uniroma2.it Peroxisome proliferator-activated receptor γ co-activator 1 α (PGC-1 α) and sirtuin 1 (SIRT1) reside in mitochondria: possible direct function in mitochondrial biogenesis. Journal of Biological Chemistry 2010 285 28 21590 21599 10.1074/jbc.M109.070169
42. Amat R., Planavila A., Chen S. L., Iglesias R., Giralt M., Villarroya F., SIRT1 controls the transcription of the peroxisome proliferator-activated receptor- γ co-activator-1 α (PGC-1 α) gene in skeletal muscle through the PGC-1 α autoregulatory loop and interaction with MyoD. Journal of Biological Chemistry 2009 284 33 21872 21880 2-s2.0-69249116960 10.1074/jbc.M109.022749
43. 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. Molecular and Cellular Biology 2008 28 20 6384 6401 2-s2.0-53549105529 10.1128/MCB.00426-08
44. Kaidi A., Weinert B. T., Choudhary C., Jackson S. P., s.jackson@gurdon.cam.ac.uk Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science 2010 329 5997 1348 1353 10.1126/science.1192049
45. Dioum E. M., Chen R., Alexander M. S., Zhang Q., Hogg R. T., Gerard R. D., Garcia J. A., Regulation of hypoxia-inducible factor 2 α signaling by the stress-responsive deacetylase sirtuin 1. Science 2009 324 5932 1289 1293 2-s2.0-66749129781 10.1126/science.1169956
46. Kim H.-S., Xiao C., Wang R.-H., Lahusen T., Xu X., Vassilopoulos A., Vazquez-Ortiz G., Jeong W.-I., Park O., Ki S. H., Gao B., Deng C.-X., chuxiad@bdg10.niddk.nih.gov Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metabolism 2010 12 3 224 236 10.1016/j.cmet.2010.06.009
47. Sauve A. A., Wolberger C., Schramm V. L., Boeke J. D., The biochemistry of sirtuins. Annual Review of Biochemistry 2006 75 435 465 2-s2.0-33745203038 10.1146/annurev.biochem.74.082803.133500 (Pubitemid 44118039)
48. Yang T., Sauve A. A., NAD metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity. AAPS Journal 2006 8 4 E632 E643 2-s2.0-33750445309 10.1208/aapsj080472 (Pubitemid 44644162)
49. Jiang J. C., Jaruga E., Repnevskaya M. V., Jazwinski S. M., An intervention resembling caloric restriction prolongs life span and retards aging in yeast. FASEB Journal 2000 14 14 2135 2137 2-s2.0-0033738362
50. Mair W., Goymer P., Pletcher S. D., Partridge L., Demography of dietary restriction and death in Drosophila. Science 2003 301 5640 1731 1733 2-s2.0-0141766912 10.1126/science.1086016 (Pubitemid 37174368)
51. Mattison J., Roth G., Lane M., Ingram D., Dietary restriction in aging nonhuman primates. Interdisciplinary Topics in Gerontology 2007 35 137 158 2-s2.0-34249000287 10.1159/000096560
52. Weindruch R., Walford R. L., Dietary restriction in mice beginning at 1 year of age: effect on life-span and spontaneous cancer incidence. Science 1982 215 4538 1415 1418 2-s2.0-0020044308 (Pubitemid 12129729)
53. Milne J. C., Denu J. M., The Sirtuin family: therapeutic targets to treat diseases of aging. Current Opinion in Chemical Biology 2008 12 1 11 17 2-s2.0-40849135481 10.1016/j.cbpa.2008.01.019
54. Daub H., Olsen J. V., Bairlein M., Gnad F., Oppermann F. S., Körner R., Greff Z., Kéri G., Stemmann O., Mann M., Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Molecular Cell 2008 31 3 438 448 2-s2.0-48349138726 10.1016/j.molcel.2008.07.007
55. Cantu D., Schaack J., Patel M., Oxidative inactivation of mitochondrial aconitase results in iron and H2O2 neurotoxicity in rat primary mesencephalic cultures. PLoS One 2009 4 9 2-s2.0-70349464469 10.1371/journal.pone.0007095 e7095
56. Peng T.-I., Jou M.-J., mjjou@mail.cgu.edu.tw Oxidative stress caused by mitochondrial calcium overload. Annals of the New York Academy of Sciences 2010 1201 183 188 10.1111/j.1749-6632.2010.05634.x
57. Blache D., Devaux S., Joubert O., Loreau N., Schneider M., Durand P., Prost M., Gaume V., Adrian M., Laurant P., Berthelot A., Long-term moderate magnesium-deficient diet shows relationships between blood pressure, inflammation and oxidant stress defense in aging rats. Free Radical Biology and Medicine 2006 41 2 277 284 2-s2.0-33745467478 10.1016/j.freeradbiomed.2006.04. 008 (Pubitemid 43949467)
58. Shi T., Wang F., Stieren E., Tong Q., SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. Journal of Biological Chemistry 2005 280 14 13560 13567 2-s2.0-17144424946 10.1074/jbc.M414670200 (Pubitemid 40517248)
59. 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. Proceedings of the National Academy of Sciences of the United States of America 2006 103 27 10224 10229 2-s2.0-33745889628 10.1073/pnas.0603968103 (Pubitemid 44051148)
60. Hallows W. C., Lee S., Denu J. M., Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proceedings of the National Academy of Sciences of the United States of America 2006 103 27 10230 10235 2-s2.0-33745931074 10.1073/pnas.0604392103 (Pubitemid 44051149)
61. Starai V. J., Celic I., Cole R. N., Boeke J. D., Escalante-Semerena J. C., Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 2002 298 5602 2390 2392 2-s2.0-0347457075 10.1126/science.1077650 (Pubitemid 36014212)
62. Schwer B., Eckersdorff M., Li Y., Silva J. C., Fermin D., Kurtev M. V., Giallourakis C., Comb M. J., Alt F. W., Lombard D. B., Calorie restriction alters mitochondrial protein acetylation. Aging Cell 2009 8 5 604 606 2-s2.0-73949123433 10.1111/j.1474-9726.2009.00503.x
63. Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou LI., Zeng Y., Li H., Li Y., Shi J., An W., Hancock S. M., He F., Qin L., Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K. L., Regulation of cellular metabolism by protein lysine acetylation. Science 2010 327 5968 1000 1004 2-s2.0-77149148756 10.1126/science.1179689
64. Lombard D. B., Alt F. W., Cheng H. L., Bunkenborg J., Streeper R. S., Mostoslavsky R., Kim J., Yancopoulos G., Valenzuela D., Murphy A., Yang Y., Chen Y., Hirschey M. D., Bronson R. T., Haigis M., Guarente L. P., Farese R. V., Weissman S., Verdin E., Schwer B., Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Molecular and Cellular Biology 2007 27 24 8807 8814 2-s2.0-37549002891 10.1128/MCB.01636-07
65. 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. Journal of Clinical Investigation 2009 119 9 2758 2771 2-s2.0-70349208608 10.1172/JCI39162
66. Shulga N., Wilson-Smith R., Pastorino J. G., Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria. Journal of Cell Science 2010 123 6 894 902 2-s2.0-77951176793 10.1242/jcs.061846
67. Rinaldo P., Matern D., Disorders of fatty acid transport and mitochondrial oxidation: challenges and dilemmas of metabolic evaluation. Genetics in Medicine 2000 2 6 338 344 2-s2.0-0034521895 (Pubitemid 32045712)
68. Someya S., Yu W., Hallows W. C., Xu J., Vann J. M., Leeuwenburgh C., Tanokura M., Denu J. M., jmdenu@wisc.edu Prolla T. A., taprolla@wisc.edu Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 143 5 802 812 10.1016/j.cell.2010.10.002
69. + -dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10. Journal of Biological Chemistry 2010 285 10 7417 7429 2-s2.0-77951235122 10.1074/jbc.M109.053421
70. 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 2 304 311 2-s2.0-75349111140 10.1021/bi901627u
71. Haigis M. C., Mostoslavsky R., Haigis K. M., Fahie K., Christodoulou D. C., Murphy A., Valenzuela D. M., Yancopoulos G. D., Karow M., Blander G., Wolberger C., Prolla T. A., Weindruch R., Alt F. W., Guarente L., SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells. Cell 2006 126 5 941 954 2-s2.0-33748316536 10.1016/j.cell.2006.06.057 (Pubitemid 44321935)
72. Ahuja N., Schwer B., Carobbio S., Waltregny D., North B. J., Castronovo V., Maechler P., Verdin E., Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase. Journal of Biological Chemistry 2007 282 46 33583 33592 2-s2.0-36349030394 10.1074/jbc.M705488200 (Pubitemid 350159524)
73. Nasrin N., Wu X., Fortier E., Feng Y., Baré O. C., Chen S., Ren X., Wu Z., Streeper R. S., Bordone L., laura.bordone@novartis.com SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells. Journal of Biological Chemistry 2010 285 42 31995 32002 10.1074/jbc.M110.124164
74. Nakagawa T., Guarente L., Urea cycle regulation by mitochondrial sirtuin, SIRT5. Aging 2009 1 6 578 581 2-s2.0-77953933813
75. Allison S. J., Milner J., SIRT3 is pro-apoptotic and participates in distinct basal apoptotic pathways. Cell Cycle 2007 6 21 2669 2677 2-s2.0-36849002444 (Pubitemid 350224051)
76. Kim H. S., Patel K., Muldoon-Jacobs K., Bisht K. S., Aykin-Burns N., Pennington J. D., van der Meer R., Nguyen P., Savage J., Owens K. M., Vassilopoulos A., Ozden O., Park S. H., Singh K. K., Abdulkadir S. A., Spitz D. R., Deng C. X., Gius D., SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 2010 17 1 41 52 2-s2.0-74049094817 10.1016/j.ccr.2009.11.023
77. Jacobs K. M., Pennington J. D., Bisht K. S., Aykin-Burns N., Kim H. S., Mishra M., Sun L., Nguyen P., Ahn B. H., Leclerc J., Deng C. X., Spitz D. R., Gius D., SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression. International Journal of Biological Sciences 2008 4 5 291 299 2-s2.0-51449083112
78. Qiu X., Brown K., Hirschey M. D., Verdin E., Chen D., danicac@berkeley.edu Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metabolism 2010 12 6 662 667 10.1016/j.cmet.2010.11.015
79. Tao R., Coleman M. C., Pennington J. D., Ozden O., Park S.-H., Jiang H., Kim H.-S., Flynn C. R., Hill S., McDonald W. H., Olivier A. K., Spitz D. R., Gius D., david.gius@vanderbilt.edu Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Molecular Cell 2010 40 6 893 904 10.1016/j.molcel.2010.12.013
80. + levels dictate cell survival. Cell 2007 130 6 1095 1107 2-s2.0-34548627517 10.1016/j.cell.2007. 07.035 (Pubitemid 47410271)
81. Li S., Banck M., Mujtaba S., Zhou M.-M., Sugrue M. M., msugrue@celgene.com Walsh M. J., martin.walsh@mssm.edu p53-Induced growth arrest is regulated by the Mitochondrial SirT3 deacetylase. PLoS One 2010 5 5 e10486 10.1371/journal.pone.0010486
82. Kawamura Y., Uchijima Y., Horike N., Tonami K., Nishiyama K., Amano T., Asano T., Kurihara Y., Kurihara H., kuri-tky@umin.ac.jp Sirt3 protects in vitro-fertilized mouse preimplantation embryos against oxidative stress-induced p53-mediated developmental arrest. Journal of Clinical Investigation 2010 120 8 2817 2828 10.1172/JCI42020
83. Choudhary C., Kumar C., Gnad F., Nielsen M. L., Rehman M., Walther T. C., Olsen J. V., Mann M., Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009 325 5942 834 840 2-s2.0-68949212379 10.1126/science.1175371
84. Paik W. K., Pearson D., Lee H. W., Kim S., Nonenzymatic acetylation of histones with acetyl-CoA. Biochimica et Biophysica Acta 1970 213 2 513 522 2-s2.0-0014937061
85. Hoyert D. L., Heron M. P., Murphy S. L., Kung H. C., Deaths: final data for 2003. National Vital Statistics Reports 2006 54 13 1 120 2-s2.0-33744826290
86. Di Donato S., Multisystem manifestations of mitochondrial disorders. Journal of Neurology 2009 256 5 693 710 2-s2.0-67349120136 10.1007/s00415-009- 5028-3
87. Ingwall J. S., Energy metabolism in heart failure and remodelling. Cardiovascular Research 2009 81 3 412 419 2-s2.0-59449085388 10.1093/cvr/cvn301
88. Neubauer S., The failing heart-an engine out of fuel. The New England Journal of Medicine 2007 356 11 1140 1151 2-s2.0-33947239659 10.1056/NEJMra063052 (Pubitemid 46425598)
89. Pillai V. B., Sundaresan N. R., Kim G., Gupta M., Rajamohan S. B., Pillai J. B., Samant S., Ravindra P. V., Isbatan A., Gupta M. P., Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. Journal of Biological Chemistry 2010 285 5 3133 3144 2-s2.0-77449120223 10.1074/jbc.M109.077271
90. + synthesis in cardiac myocytes. Circulation Research 2009 105 5 481 491 2-s2.0-70149095672 10.1161/CIRCRESAHA.109.203703
91. Ruzicka M., mruzicka@ottawahospital.on.ca Coletta E., White R., Davies R., Haddad H., Leenen F. H.H., Effects of ACE inhibitors on cardiac angiotensin II and aldosterone in humans: relevance of lipophilicity and affinity for ACE. American Journal of Hypertension 2010 23 11 1179 1182 10.1038/ajh.2010.148
92. Benigni A., Corna D., Zoja C., Sonzogni A., Latini R., Salio M., Conti S., Rottoli D., Longaretti L., Cassis P., Morigi M., Coffman T. M., Remuzzi G., Disruption of the Ang II type 1 receptor promotes longevity in mice. Journal of Clinical Investigation 2009 119 3 524 530 2-s2.0-65349128571 10.1172/JCI36703
93. Ventura-Clapier R., renee.ventura@u-psud.fr Garnier A., Veksler V., Joubert F., Bioenergetics of the failing heart. Biochimica et Biophysica Acta. In press 10.1016/j.bbamcr.2010.09.006
94. Ventura-Clapier R., Garnier A., Veksler V., Energy metabolism in heart failure. Journal of Physiology 2004 555 1 1 13 2-s2.0-1542299777 10.1113/jphysiol.2003.055095 (Pubitemid 38313058)
95. Lopaschuk G. D., Ussher J. R., Folmes C. D. L., Jaswal J. S., Stanley W. C., Myocardial fatty acid metabolism in health and disease. Physiological Reviews 2010 90 1 207 258 2-s2.0-74949133862 10.1152/physrev.00015.2009
96. Lopaschuk G. D., Belke D. D., Gamble J., Itoi T., Schonekess B. O., Regulation of fatty acid oxidation in the mammalian heart in health and disease. Biochimica et Biophysica Acta 1994 1213 3 263 276 2-s2.0-0027978916 10.1016/0005-2760(94)00082-4 (Pubitemid 24262910)
97. Neubauer S., The failing heart-an engine out of fuel. The New England Journal of Medicine 2007 356 11 1140 1151 2-s2.0-33947239659 10.1056/NEJMra063052 (Pubitemid 46425598)
98. Rosca M. G., Vazquez E. J., Kerner J., Parland W., Chandler M. P., Stanley W., Sabbah H. N., Hoppel C. L., Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation. Cardiovascular Research 2008 80 1 30 39 2-s2.0-51749113618 10.1093/cvr/cvn184
99. Allard M. F., Schonekess B. O., Henning S. L., English D. R., Lopaschuk G. D., Contribution of oxidative metabolism and glycolysis to ATP production in hypertrophied hearts. American Journal of Physiology 1994 267 2 H742 H750 2-s2.0-0027930794 (Pubitemid 24272494)
100. Sharov V. G., Goussev A., Lesch M., Goldstein S., Sabbah H. N., Abnormal mitochondrial function in myocardium of dogs with chronic heart failure. Journal of Molecular and Cellular Cardiology 1998 30 9 1757 1762 2-s2.0-0032168434 10.1006/jmcc.1998.0739 (Pubitemid 28430189)
101. Taegtmeyer H., Cardiac metabolism as a target for the treatment of heart failure. Circulation 2004 110 8 894 896 2-s2.0-4344697195 10.1161/01.CIR. 0000139340.88769.D5 (Pubitemid 39128613)
102. Warburg K. P. O., Negelein E., Ueber den Stoffwechsel der Tumoren. Biochemische Zeitschrift 1924 152 319 344
103. Warburg O., On the origin of cancer cells. Science 1956 123 3191 309 314 2-s2.0-12444279265
104. Mazurek S., Boschek C. B., Hugo F., Eigenbrodt E., Pyruvate kinase type M2 and its role in tumor growth and spreading. Seminars in Cancer Biology 2005 15 4 300 308 2-s2.0-23044500915 10.1016/j.semcancer.2005.04.009 (Pubitemid 41058775)
105. Christofk H. R., Vander Heiden M. G., Harris M. H., Ramanathan A., Gerszten R. E., Wei RU., Fleming M. D., Schreiber S. L., Cantley L. C., The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 2008 452 7184 230 233 2-s2.0-40749163248 10.1038/nature06734 (Pubitemid 351380249)
106. Vander Heiden M. G., Locasale J. W., Swanson K. D., Sharfi H., Heffron G. J., Amador-Noguez D., Christofk H. R., Wagner G., Rabinowitz J. D., Asara J. M., Cantley L. C., lewiscantley@hms.harvard.edu Evidence for an alternative glycolytic pathway in rapidly proliferating cells. Science 2010 329 5998 1492 1499 10.1126/science.1188015
107. DeBerardinis R. J., Mancuso A., Daikhin E., Nissim I., Yudkoff M., Wehrli S., Thompson C. B., craig@mail.med.upenn.edu Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Proceedings of the National Academy of Sciences of the United States of America 2007 104 49 19345 19350 10.1073/pnas.0709747104
108. Wise D. R., Deberardinis R. J., Mancuso A., Sayed N., Zhang X. Y., Pfeiffer H. K., Nissim I., Daikhin E., Yudkoff M., McMahon S. B., Thompson C. B., Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction. Proceedings of the National Academy of Sciences of the United States of America 2008 105 48 18782 18787 2-s2.0-57749088701 10.1073/pnas.0810199105
109. DeBerardinis R. J., Lum J. J., Hatzivassiliou G., Thompson C. B., The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metabolism 2008 7 1 11 20 2-s2.0-37449024702 10.1016/j.cmet.2007.10.002
110. Taub R., Kirsch I., Morton C., Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells. Proceedings of the National Academy of Sciences of the United States of America 1982 79 24 7837 7841 (Pubitemid 13182474)
111. Schwab M., Alitalo K., Klempnauer K. H., Amplified DNA with limited homology to myc cellular oncogene is shared by human neuroblastoma cell lines and a neuroblastoma tumour. Nature 1983 305 5931 245 248 (Pubitemid 14227614)
112. Nau M. M., Brooks B. J., Battey J., L-myc, a new myc-related gene amplified and expressed in human small cell lung cancer. Nature 1985 318 6041 69 73 (Pubitemid 16230338)
113. Jenne D. E., djenne@alf.biochem.mpg.dc Reimann H., Nezu J.-I., Friedel W., Loff S., Jeschke R., Müller O., Back W., Zimmer M., Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. Nature Genetics 1998 18 1 38 43 10.1038/ng0198-38 (Pubitemid 28027876)
114. Zhou J., Scholes J., Hsieh J. T., Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in normal prostatic epithelium and cancer. Journal of Biological Chemistry 2003 278 9 6936 6941 2-s2.0-0037470132 10.1074/jbc.M210628200 (Pubitemid 36800686)
115. Castaneda C. A., carloscastanedaaltamirano@yahoo.com Cortes-Funes H., Gomez H. L., Ciruelos E. M., The phosphatidyl inositol 3-kinase/AKT signaling pathway in breast cancer. Cancer and Metastasis Reviews 2010 29 4 751 759 10.1007/s10555-010-9261-0
116. Comoglio P. M., Di Renzo M. F., Gaudino G., Protein tyrosine kinases associated with human malignancies. Annals of the New York Academy of Sciences 1987 511 256 261 2-s2.0-0023612950 (Pubitemid 18093048)
117. Hoshino I., Matsubara H., Recent advances in histone deacetylase targeted cancer therapy. Surgery Today 2010 40 9 809 815 10.1007/s00595-010-4300-6
118. Rose G., Dato S., Altomare K., Bellizzi D., Garasto S., Greco V., Passarino G., Feraco E., Mari V., Barbi C., BonaFe M., Franceschi C., Tan Q., Boiko S., Yashin A. I., de Benedictis G., Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. Experimental Gerontology 2003 38 10 1065 1070 2-s2.0-10744232772 10.1016/S0531-5565(03)00209-2 (Pubitemid 37324417)
119. Bellizzi D., Rose G., Cavalcante P., Covello G., Dato S., de Rango F., Greco V., Maggiolini M., Feraco E., Mari V., Franceschi C., Passarino G., de Benedictis G., A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics 2005 85 2 258 263 2-s2.0-19944433088 10.1016/j.ygeno.2004.11.003 (Pubitemid 40164791)
120. Bellizzi D., Covello G., Cianni F., Tong Q., de Benedictis G., Identification of GATA2 and AP-1 activator elements within the enhancer VNTR occurring in intron 5 of the human SIRT3 gene. Molecules and Cells 2009 28 2 87 92 2-s2.0-69849094644 10.1007/s10059-009-0110-3
121. Lescai F., Blanché H., Nebel A., Beekman M., Sahbatou M., Flachsbart F., Slagboom E., Schreiber S., Sorbi S., Passarino G., Franceschi C., Human longevity and 11p15.5: a study in 1321 centenarians. European Journal of Human Genetics 2009 17 11 1515 1519 2-s2.0-70350365059 10.1038/ejhg.2009.54