Cited by 217Sirtuins and Resveratrol in MedicineMitochondrial Function and PathologyGenetics, Aging, and Longevity in Model Organisms

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SIRT3 regulates progression and development of diseases of aging

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McDonnell, Eoin, Peterson, Brett S., Bomze, Howard M., Hirschey, Matthew D.·2015·Trends in Endocrinology & Metabolism

DOI 10.1016/j.tem.2015.06.001PMC PMC4558250

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Abstract

The mitochondrial sirtuin SIRT3 is a protein deacylase that influences almost every major aspect of mitochondrial biology, including nutrient oxidation, ATP generation, reactive oxygen species (ROS) detoxification, mitochondrial dynamics, and the mitochondrial unfolded protein response (UPR). Interestingly, mice lacking SIRT3 (SIRT3KO), either spontaneously or when crossed with mouse models of disease, develop several diseases of aging at an accelerated pace, such as cancer, metabolic syndrome, cardiovascular disease, and neurodegenerative diseases, and, thus, might be a valuable model of accelerated aging. In this review, we discuss functions of SIRT3 in pathways involved in diseases of aging and how the lack of SIRT3 might accelerate the aging process. We also suggest that further studies on SIRT3 will help uncover important new pathways driving the aging process.

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Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
The Hallmarks of Aging
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Inflammation and metabolic disorders
Hotamisligil, G. S. (2006) · Nature · doi:10.1038/nature05485 · Cited by 9,199
ROS function in redox signaling and oxidative stress
Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931
The Clonal Evolution of Tumor Cell Populations: Acquired genetic lability permits stepwise selection of variant sublines and underlies tumor progression.
Nowell, P. C. (1976) · Science · doi:10.1126/science.959840 · Cited by 6,471
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088
On Respiratory Impairment in Cancer Cells
Warburg, O. H. (1956) · Science · doi:10.1126/science.124.3215.269 · Cited by 3,472
Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes
Land, H., Parada, L. F., & Weinberg, R. A. (1983) · Nature · doi:10.1038/304596a0 · Cited by 2,804
The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 1×
“An additional SIR2 allele can increase lifespan by 30%, whereas ablation of SIR2 decreased lifespan in yeast [2].”
Mitochondrial dysfunction in the elderly: possible role in insulin resistance
Petersen, K. F., Befroy, D., Dufour, S., Dziura, J., Ariyan, C., Rothman, D. L., DiPietro, L., Cline, G. W., & Shulman, G. I. (2003) · Science · doi:10.1126/science.1082889 · Cited by 2,107
Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1α during hypoxia
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000
Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687
Self-citation
Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310
Self-citation
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216
Self-citation
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. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150
Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
Sundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 1,006
Mitochondria take center stage in aging and neurodegeneration
Beal, M. F. (2005) · Annals of Neurology · doi:10.1002/ana.20624 · Cited by 957
Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity
Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809
SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · cited 3×
“SIRT3KO mice fed a HFD showed accelerated development of several hallmarks of the metabolic syndrome, including weight gain, impaired glucose tolerance, and insulin resistance (IR)[52].”
Self-citation
SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress
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., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785
SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization
Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.02.014 · Cited by 782
Circadian Clock NAD + Cycle Drives Mitochondrial Oxidative Metabolism in Mice
Peek, C. B., Affinati, A. H., Ramsey, K. M., Kuo, H.-Y., Yu, W., Sena, L. A., Ilkayeva, O., Marcheva, B., Kobayashi, Y., Omura, C., et al. (2013) · Science · doi:10.1126/science.1243417 · Cited by 678
The contribution of endogenous sources of DNA damage to the multiple mutations in cancer
Jackson, A. L., & Loeb, L. A. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00091-4 · Cited by 640
Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins
Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · cited 1×
“SIRT3 has also been reported to remove other acyl modifications such as long-chain fatty acyl modifications and histone decrotonylation [13, 14], although understanding the biological relevance of these modifications requires further work.”
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636
Metabolic Syndrome, Aging and Involvement of Oxidative Stress
Bonomini, F., Rodella, L. F., & Rezzani, R. (2015) · Aging and Disease · doi:10.14336/ad.2014.0305 · Cited by 599
Mutation is required to activate the p53 gene for cooperation with the ras oncogene and transformation
Hinds, P. W., Finlay, C. A., & Levine, A. J. (1989) · Journal of Virology · doi:10.1128/jvi.63.2.739-746.1989 · Cited by 595
SIRT3, a human SIR2 homologue, is an NAD- dependent deacetylase localized to mitochondria
Onyango, P. O., Celic, I., McCaffery, J. M., Boeke, J. D., & Feinberg, A. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222538099 · Cited by 573
The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568
Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 554
Insulin resistance is a cellular antioxidant defense mechanism
Hoehn, K. L., Salmon, A. B., Hohnen-Behrens, C., Turner, N., Hoy, A. J., Maghzal, G. J., Stocker, R., Van Remmen, H., Kraegen, E. W., Cooney, G. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902380106 · Cited by 540
Lipid-induced oxidative stress causes steatohepatitis in mice fed an atherogenic diet
Matsuzawa, N., Takamura, T., Kurita, S., Misu, H., Ota, T., Ando, H., Yokoyama, M., Honda, M., Zen, Y., Nakanuma, Y., et al. (2007) · Hepatology · doi:10.1002/hep.21874 · Cited by 516
Disruption of the Ang II type 1 receptor promotes longevity in mice
Benigni, A., Corna, D., Zoja, C., Sonzogni, A., Latini, R., Salio, M., Conti, S., Rottoli, D., Longaretti, L., Cassis, P., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci36703 · Cited by 486
Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production
Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., Verdin, E. M., & Kahn, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111308108 · Cited by 469
Self-citation
Mitochondria and Cardiovascular Aging
Dai, D., Rabinovitch, P. S., & Ungvari, Z. I. (2012) · Circulation Research · doi:10.1161/circresaha.111.246140 · Cited by 446
SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways
Rardin, M. J., Newman, J. C., Held, J. M., Cusack, M. P., Sorensen, D. J., Li, B., Schilling, B., Mooney, S. D., Kahn, C. R., Verdin, E. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302961110 · Cited by 446
SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440
Palmitate induces insulin resistance in H4IIEC3 hepatocytes through reactive oxygen species produced by mitochondria.
Nakamura, S., Takamura, T., Matsuzawa-Nagata, N., Takayama, H., Misu, H., Noda, H., Nabemoto, S., Kurita, S., Ota, T., Ando, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901488200 · Cited by 426
Pyruvate Dehydrogenase Complex Activity Controls Metabolic and Malignant Phenotype in Cancer Cells
McFate, T., Mohyeldin, A., Lu, H., Thakar, J. H., Henriques, J., Halim, N. D., Wu, H., Schell, M. J., Tsang, T. M., Teahan, O., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801765200 · Cited by 395
Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
Kendrick, A. A., Choudhury, M., Rahman, S. M., McCurdy, C. E., Friederich, M., Van Hove, J. L. K., Watson, P. A., Birdsey, N., Bao, J., Gius, D., et al. (2011) · Biochemical Journal · doi:10.1042/bj20100791 · Cited by 382
A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages
Bellizzi, D., Rose, G., Cavalcante, P., Covello, G., Dato, S., De Rango, F., Greco, V., Maggiolini, M., Feraco, E., Mari, V., et al. (2005) · Genomics · doi:10.1016/j.ygeno.2004.11.003 · Cited by 367
Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach
Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324
Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases
Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 323
Self-citation
Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex
Fan, J., Shan, C., Kang, H.-B., Elf, S., Xie, J., Tucker, M., Gu, T.-L., Aguiar, M., Lonning, S., Chen, H., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.026 · Cited by 305
SirT3 Regulates the Mitochondrial Unfolded Protein Response
Papa, L., & Germain, D. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01337-13 · Cited by 292
SIRT3 interacts with the daf-16 homolog FOXO3a in the Mitochondria, as well as increases FOXO3a Dependent Gene expression
Jacobs, K. M., Pennington, J. D., Bisht, K. S., Aykin‐Burns, N., Kim, H., Mishra, M. V., Sun, L., Nguyen, P., Ahn, B., Leclerc, J., et al. (2008) · International Journal of Biological Sciences · doi:10.7150/ijbs.4.291 · Cited by 285
Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae
Weinert, B. T., Iešmantavičius, V., Moustafa, T., Scholz, C. W., Wagner, S., Magnes, C., Zechner, R., & Choudhary, C. (2014) · Molecular Systems Biology · doi:10.1002/msb.134766 · Cited by 283
Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation
Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283
Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly
Rose, G., Dato, S., Altomare, K., Bellizzi, D., Garasto, S., Greco, V, Passarino, G., Feraco, E., Mari, V, Barbi, C., et al. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00209-2 · Cited by 282
Activation of SIRT3 by the NAD(+) precursor nicotinamide riboside protects from noise-induced hearing loss
Brown, K. D., Maqsood, S., Huang, J.-Y., Pan, Y., Harkcom, W., Li, W., Sauve, A., Verdin, E., & Jaffrey, S. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.003 · Cited by 277
SIRT3‐dependent GOT2 acetylation status affects the malate–aspartate NADH shuttle activity and pancreatic tumor growth
Yang, H., Zhou, L., Shi, Q., Zhao, Y., Lin, H., Zhang, M., Zhao, S., Yang, Y. A., Ling, Z., Guan, K., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591041 · Cited by 225
Obesity-induced lysine acetylation increases cardiac fatty acid oxidation and impairs insulin signalling
Alrob, O. A., Sankaralingam, S., Ma, C., Wagg, C. S., Fillmore, N., Jaswal, J. S., Sack, M. N., Lehner, R. S., Gupta, M. P., Michelakis, E. D., et al. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu156 · Cited by 223
Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1α
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 220
Mitochondrial dysfunction and its role in motor neuron degeneration in ALS
Manfredi, G., & Xu, Z. (2005) · Mitochondrion · doi:10.1016/j.mito.2005.01.002 · Cited by 215
SIRT3 Is a Mitochondrial Tumor Suppressor: A Scientific Tale That Connects Aberrant Cellular ROS, the Warburg Effect, and Carcinogenesis
Haigis, M. C., Deng, C., Finley, L. W. S., Kim, H., & Gius, D. R. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3633 · Cited by 196
SIRT3 Mediates Multi-Tissue Coupling for Metabolic Fuel Switching
Dittenhafer‐Reed, K. E., Richards, A., Fan, J., Smallegan, M. J., Siahpirani, A. F., Kemmerer, Z. A., Prolla, T. A., Roy, S., Coon, J. J., & Denu, J. M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.03.007 · Cited by 194
Mitochondrial function in heart muscle from patients with idiopathic dilated cardiomyopathy
Jarreta, D. (2000) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00388-0 · Cited by 189
SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells
Özden, Ö., Park, S., Wagner, B. A., Song, H. Y., Zhu, Y., Vassilopoulos, A., Jung, B. H., Buettner, G. R., & Gius, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.08.001 · Cited by 189
Sirtuin 3 (SIRT3) Protein Regulates Long-chain Acyl-CoA Dehydrogenase by Deacetylating Conserved Lysines Near the Active Site
Bharathi, S. S., Zhang, Y., Mohsen, A.-W. A., Uppala, R., Balasubramani, M., Schreiber, E. M., Uechi, G. T., Beck, M. E., Rardin, M. J., Vockley, J., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510354 · Cited by 181
Self-citation
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. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.009 · Cited by 157
Proteomic Investigations of Lysine Acetylation Identify Diverse Substrates of Mitochondrial Deacetylase Sirt3
Sol, E.-R. M., Wagner, S., Weinert, B. T., Kumar, A., Kim, H., Deng, C., & Choudhary, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050545 · Cited by 155
Stoichiometry of site-specific lysine acetylation in an entire proteome
Baeza, J., Dowell, J. A., Smallegan, M. J., Fan, J., Amador-Noguez, D., Khan, Z., & Denu, J. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.581843 · Cited by 154
SIRT3 is crucial for maintaining skeletal muscle insulin action and protects against severe insulin resistance in high-fat-fed mice
Lantier, L., Williams, A. S., Williams, I. M., Yang, K. K., Bracy, D. P., Goelzer, M., James, F. D., Gius, D., & Wasserman, D. H. (2015) · Diabetes · doi:10.2337/db14-1810 · Cited by 151
Mitochondrial response to nutrient availability and its role in metabolic disease
Gao, A. W., Cantó, C., & Houtkooper, R. H. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201303782 · Cited by 148
Molecular mechanisms mediating mitochondrial dynamics and mitophagy and their functional roles in the cardiovascular system
Ikeda, Y., Shirakabe, A., Brady, C., Zablocki, D., Ohishi, M., & Sadoshima, J. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.019 · Cited by 145
Cardiac hypertrophy is enhanced in PPAR -/- mice in response to chronic pressure overload
Smeets, P. J. H., Teunissen, B. E. J., Willemsen, P. H. M., van Nieuwenhoven, F. A., Brouns, A. E., Janssen, B. J., Cleutjens, J. P. M., Staels, B., Vusse, G. J., & van Bilsen, M. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn001 · Cited by 126
Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation
Still, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483396 · Cited by 123
SIRT3 and SIRT5 Regulate the Enzyme Activity and Cardiolipin Binding of Very Long-Chain Acyl-CoA Dehydrogenase
Zhang, Y., Bharathi, S. S., Rardin, M. J., Uppala, R., Verdin, E. M., Gibson, B. W., & Goetzman, E. S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122297 · Cited by 118
Sirtuin 3 regulates mouse pancreatic beta cell function and is suppressed in pancreatic islets isolated from human type 2 diabetic patients
Caton, P., Richardson, S. J., Kieswich, J. E., Bugliani, M., Holland, M. L., Marchetti, P., Morgan, N. G., Yaqoob, M. M., Holness, M. J., & Sugden, M. C. (2013) · Diabetologia · doi:10.1007/s00125-013-2851-y · Cited by 118
CNS SIRT3 Expression Is Altered by Reactive Oxygen Species and in Alzheimer’s Disease
Weir, H. J. M., Murray, T. K., Kehoe, P. G., Love, S., Verdin, E. M., O’Neill, M. J., Lane, J. D., & Balthasar, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048225 · Cited by 115
Involvement of oxidatively damaged DNA and repair in cancer development and aging.
Tudek, B., Winczura, A., Janik, J., Siomek, A., Foksiński, M., & Oliński, R. (2010) · PubMed Central · Cited by 112
Pituitary adenylate cyclase-activating polypeptide protects against β-amyloid toxicity
Han, P., Tang, Z., Yin, J., Maalouf, M., Beach, T. G., Reiman, E. M., & Shi, J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.022 · Cited by 110
In adipose tissue, increased mitochondrial emission of reactive oxygen species is important for short-term high-fat diet-induced insulin resistance in mice
Paglialunga, S., Ludzki, A. C., Root-McCaig, J., & Holloway, G. P. (2015) · Diabetologia · doi:10.1007/s00125-015-3531-x · Cited by 104
Age-Related Decrease in the Mitochondrial Sirtuin Deacetylase Sirt3 Expression Associated with ROS Accumulation in the Auditory Cortex of the Mimetic Aging Rat Model
Zeng, L., Yang, Y., Hu, Y., Sun, Y., Du, Z., Xie, Z., Zhou, T., & Kong, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088019 · Cited by 103
Sirt3 inhibits hepatocellular carcinoma cell growth through reducing Mdm2-mediated p53 degradation
Zhang, Y., & Zhou, L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.05.053 · Cited by 102
Increased α2 Subunit–Associated AMPK Activity and PRKAG2 Cardiomyopathy
Ahmad, F., Arad, M., Musi, N., He, H., Wolf, C. M., Branco, D. M., Pérez‐Atayde, A. R., Stapleton, D., Bali, D. S., Xing, Y., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.550806 · Cited by 93
Differential expression of sirtuin family members in the developing, adult, and aged rat brain
Sidorova‐Darmos, E., Wither, R. G., Shulyakova, N., Fisher, C., Ratnam, M., Aarts, M. M., Lilge, L. D., Monnier, P. P., & Eubanks, J. H. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00333 · Cited by 90
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Zhang, C. Z., Liu, L., Cai, M., Pan, Y., Fu, J., Cao, Y., & Yun, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051703 · Cited by 73
Aging impairs myocardial fatty acid and ketone oxidation and modifies cardiac functional and metabolic responses to insulin in mice
Hyyti, O. M., Ledee, D. R., Ning, X.-H., Ge, M. J., & Portman, M. A. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00931.2009 · Cited by 66
Cardiac hypertrophy in mice with long-chain acyl-CoA dehydrogenase or very long-chain acyl-CoA dehydrogenase deficiency
Cox, K. B., Liu, J., Tian, L., Barnes, S., Yang, Q., & Wood, P. A. (2009) · Laboratory Investigation · doi:10.1038/labinvest.2009.86 · Cited by 66
Human longevity and 11p15.5: a study in 1321 centenarians
Lescai, F., Blanché, H., Nebel, A., Beekman, M., Sahbatou, M., Flachsbart, F., Slagboom, P. E., Schreiber, S., Sorbi, S., Passarino, G., et al. (2009) · European Journal of Human Genetics · doi:10.1038/ejhg.2009.54 · Cited by 66
Reduced capacity for fatty acid oxidation in rats with inherited susceptibility to diet-induced obesity
Ji, H. L., & Friedman, M. I. (2007) · Metabolism · doi:10.1016/j.metabol.2007.04.006 · Cited by 61
Aberrant expression of SIRT3 is conversely correlated with the progression and prognosis of human gastric cancer
Yang, B. L., Fu, X., Shao, L., Ding, Y., & Zeng, D. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.068 · Cited by 52
SIRT3 Overexpression Attenuates Palmitate-Induced Pancreatic β-Cell Dysfunction
Kim, M., Lee, J. S., Oh, J. E., Nan, J., Lee, H., Jung, H. S., Chung, S. S., & Park, K. S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124744 · Cited by 48
Heterozygous SOD2 Deletion Impairs Glucose-Stimulated Insulin Secretion, but Not Insulin Action, in High-Fat–Fed Mice
Kang, L., Dai, C., Lustig, M. E., Bonner, J. S., Mayes, W. H., Mokshagundam, S., James, F. D., Thompson, C. S., Lin, C., Perry, C. G. R., et al. (2014) · Diabetes · doi:10.2337/db13-1845 · Cited by 46
Analysis of Transformation and Tumorigenicity Using Mouse Embryonic Fibroblast Cells
Sun, H., & Taneja, R. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-335-6_19 · Cited by 42
Light–dark condition regulates sirtuin mRNA levels in the retina
Ban, N., Ozawa, Y., Inaba, T., Miyake, S., 渡辺, 光., Shinmura, K., & Tsubota, K. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.04.010 · Cited by 37
A novel sampling design to explore gene-longevity associations: the ECHA study
Rango, F. D., Dato, S., Bellizzi, D., Rose, G., Marzi, E., Cavallone, L., Franceschi, C., Skytthe, A., Jeune, B., Cournil, A., et al. (2007) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201950 · Cited by 23
Correction for Papa and Germain, “SirT3 Regulates a Novel Arm of the Mitochondrial Unfolded Protein Response”
Papa, L., & Germain, D. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00191-17 · Cited by 21
Functional Disorders of the Oxidative Phosphorylation System in the Heart Mitochondria of Mice with Juvenile Visceral Steatosis.
Suenaga, M., Arakaki, N., Morokami, K., Himeda, T., Shibata, H., Kuwajima, M., & Higuti, T. (2003) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.26.289 · Cited by 5

Research works printed but not linked: 1

Altekruse, S. et al. (2015) SEER Cancer Statistics Review 1975–2007, National Cancer Institute

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See all 217

Authors: McDonnell, E., Peterson, B. S., Bomze, H. M., & Hirschey, M. D.
Affiliations: Duke University (US)
Corresponding author: Hirschey, Matthew D.
ORCID: Bomze, Howard M.
Hirschey, Matthew D.
Venue: Trends in Endocrinology & Metabolism
Publisher: Elsevier BV
Published: 2015-09
Volume: 26
Issue: 9
Pages: 486-492
ISSN: 1043-2760 (ISSN-L)
DOI: 10.1016/j.tem.2015.06.001
PMC: PMC4558250
OpenAlex: W1491563504
Cited by: 217
References: 97
Citations by year: 2026: 11 · 2025: 16 · 2024: 18 · 2023: 21 · 2022: 31 · 2021: 21 · 2020: 17 · 2019: 22 · 2018: 16 · 2017: 23 · 2016: 18 · 2015: 2
FWCI: 2.05
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Alcohol Abuse and Alcoholism (R01AA022146)
National Institute on Aging (R01AG045351, P30AG028716)
National Cancer Institute (T32CA059365)
National Institute of General Medical Sciences (T32GM007184, T32GM007105)
National Institute of Diabetes and Digestive and Kidney Diseases (R24DK085610)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: SIRT3, mitochondrial sirtuins, aging, age-related diseases, SIRT3 knockout mice, accelerated aging, mitochondrial dynamics, mitochondrial unfolded protein response, reactive oxygen species scavenging, cancer, metabolic syndrome, cardiovascular disease, neurodegenerative diseases
MeSH terms: Aging, Animals, Disease, Humans, Longevity, Mice, Sirtuin 3

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SIRT3 regulates progression and development of diseases of aging

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