Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3
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We have previously reported that the expression of mitochondrial deacetylase SIRT3 is high in the slow oxidative muscle and that the expression of muscle SIRT3 level is increased by dietary restriction or exercise training. To explore the function of SIRT3 in skeletal muscle, we report here the establishment of a transgenic mouse model with muscle-specific expression of the murine SIRT3 short isoform (SIRT3M3). Calorimetry study revealed that the transgenic mice had increased energy expenditure and lower respiratory exchange rate (RER), indicating a shift towards lipid oxidation for fuel usage, compared to control mice. The transgenic mice exhibited better exercise performance on treadmills, running 45% further than control animals. Moreover, the transgenic mice displayed higher proportion of slow oxidative muscle fibers, with increased muscle AMPK activation and PPARδ expression, both of which are known regulators promoting type I muscle fiber specification. Surprisingly, transgenic expression of SIRT3M3 reduced muscle mass up to 30%, likely through an up-regulation of FOXO1 transcription factor and its downstream atrophy gene MuRF-1. In summary, these results suggest that SIRT3 regulates the formation of oxidative muscle fiber, improves muscle metabolic function, and reduces muscle mass, changes that mimic the effects of caloric restriction.
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SIRT3 plays an important role in regulating metabolic flexibility of muscle.
“SIRT3 recently has been reported to play an important role in regulating metabolic flexibility of muscle (31) as well as regulating muscle mass and OXPHOS (32).”
From Combined Training Enhances Skeletal Muscle Mitochondrial Oxidative Capacity Independent of Age (2015) · cites this paper as [32]
SIRT3 plays an important role in regulating muscle mass and OXPHOS.
“SIRT3 recently has been reported to play an important role in regulating metabolic flexibility of muscle (31) as well as regulating muscle mass and OXPHOS (32).”
From Combined Training Enhances Skeletal Muscle Mitochondrial Oxidative Capacity Independent of Age (2015) · cites this paper as [32]
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Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Kahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799 · see citing works
Srere, P. A. (1969) · Methods in Enzymology · doi:10.1016/0076-6879(69)13005-0 · Cited by 2,005 · see citing works
Rabinowitz, J. D., & White, E. (2010) · Science · doi:10.1126/science.1193497 · Cited by 1,982 · see citing works
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 · see citing works
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539 · see citing works
The plasticity of aging: insights from long-lived mutants
Kenyon, C. (2005) · Cell · doi:10.1016/j.cell.2005.02.002 · Cited by 1,338 · see citing works
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 · see citing works
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 · see citing works
AMPK and PPARδ Agonists Are Exercise Mimetics
Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.051 · Cited by 1,222 · see citing works
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 · see citing works
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 · see citing works
Regulation of Muscle Fiber Type and Running Endurance by PPARδ
Wang, Y.-X., Zhang, C.-L., Yu, R. T., Cho, H. K., Nelson, M. C., Bayuga-Ocampo, C. R., Ham, J., Kang, H., & Evans, R. M. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020294 · Cited by 1,089 · see citing works
Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036 · see citing works
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 996 · see citing works
Three myosin heavy chain isoforms in type 2 skeletal muscle fibres
Schiaffino, S., Gorza, L., Sartore, S., Saggin, L., Ausoni, S., Vianello, M., Gundersen, K., & Lømo, T. (1989) · Journal of Muscle Research and Cell Motility · doi:10.1007/bf01739810 · Cited by 960 · see citing works
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works
Bolster, D. R., Crozier, S. J., Kimball, S. R., & Jefferson, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200171200 · Cited by 851 · see citing works
A guide to analysis of mouse energy metabolism
Tschöp, M. H., Speakman, J. R., Arch, J. R. S., Auwerx, J., Brüning, J. C., Chan, L., Eckel, R. H., Farese, R. V., Galgani, J. E., Hambly, C., et al. (2012) · Nature Methods · doi:10.1038/nmeth.1806 · Cited by 813 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Calorie Restriction Increases Muscle Mitochondrial Biogenesis in Healthy Humans
Civitarese, A. E., Carling, S., Heilbronn, L. K., Hulver, M. H., Ukropcova, B., Deutsch, W. A., Smith, S. R., & Ravussin, E. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040076 · Cited by 790 · see citing works
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 · see citing works
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 · see citing works
Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works
Self-citationSchwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works
A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy
Ruas, J. L., White, J. P., Rao, R. R., Kleiner, S., Brannan, K. T., Harrison, B. C., Greene, N. P., Wu, J., Estall, J. L., Irving, B. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.050 · Cited by 677 · see citing works
FOXO/4E-BP Signaling in Drosophila Muscles Regulates Organism-wide Proteostasis during Aging
Demontis, F., & Perrimon, N. (2010) · Cell · doi:10.1016/j.cell.2010.10.007 · Cited by 656 · see citing works
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
Endurance Exercise as a Countermeasure for Aging
Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S., Basu, R., Joyner, M. J., McConnell, J. P., & Nair, K. S. (2008) · Diabetes · doi:10.2337/db08-0349 · Cited by 582 · see citing works
Kamei, Y., Miura, S., SUZUKI, M. T., Kai, Y., Mizukami, J., Taniguchi, T., Mochida, K., Tomoko, H. A. T. A., Matsuda, J., Aburatani, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400674200 · Cited by 574 · see citing works
Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572 · see citing works
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 547 · see citing works
Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487 · see citing works
Self-citationShimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works
Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria
Çimen, H., Han, M., Yang, Y., Tong, Q., Koc, H., & Koc, E. C. (2009) · Biochemistry · doi:10.1021/bi901627u · Cited by 478 · see citing works
Self-citationJing, 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 · see citing works
Pillai, V. B., Sundaresan, N. R., Kim, G. H., Gupta, M., Rajamohan, S. B., Pillai, J. B., Samant, S. A., Ravindra, P. A., Isbatan, A., & Gupta, M. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077271 · Cited by 420 · see citing works
Joseph, A., Adhihetty, P. J., Buford, T. W., Wohlgemuth, S. E., Lees, H. A., Nguyen, L. M. ‐., Aranda, J. M., Sandesara, B. D., Pahor, M., Manini, T. M., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00844.x · Cited by 395 · see citing works
Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389 · see citing works
Arany, Z., Lebrasseur, N., Morris, C., Smith, E., Yang, W., Ma, Y., Chin, S., & Spiegelman, B. M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.003 · Cited by 370 · see citing works
Waddell, D. S., Baehr, L. M., van den Brandt, J., Johnsen, S. A., Reichardt, H. M., Furlow, J. D., & Bodine, S. C. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00646.2007 · Cited by 360 · see citing works
Skeletal Muscle Adaptation to Exercise Training
Röckl, K. S. C., Hirshman, M. F., Brandauer, J., FUJII, N. L., Witters, L. A., & Goodyear, L. J. (2007) · Diabetes · doi:10.2337/db07-0255 · Cited by 304 · see citing works
Overexpression of dystrophin in transgenic mdx mice eliminates dystrophic symptoms without toxicity
Cox, G. A., Cole, N. M., Matsumura, K., Phelps, S. F., Hauschka, S. D., Campbell, K. P., Faulkner, J. A., & Chamberlain, J. S. (1993) · Nature · doi:10.1038/364725a0 · Cited by 283 · see citing works
Gnaiger, E. (2001) · Respiration Physiology · doi:10.1016/s0034-5687(01)00307-3 · Cited by 280 · see citing works
Chapter 20: Functional Assessment of Isolated Mitochondria In Vitro
Lanza, I. R., & Nair, K. S. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)05020-4 · Cited by 248 · see citing works
Fibre types in skeletal muscle: a personal account
Schiaffino, S. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02130.x · Cited by 227 · see citing works
Targeted ablation of TRAF6 inhibits skeletal muscle wasting in mice
Paul, P. K., Gupta, S. K., Bhatnagar, S., Panguluri, S. K., Darnay, B. G., Choi, Y., & Kumar, A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006098 · Cited by 226 · see citing works
Nakashima, K., & Yakabe, Y. (2007) · Bioscience, biotechnology and biochemistry · doi:10.1271/bbb.70057 · Cited by 224 · see citing works
Embryonic and neonatal myosin heavy chain in denervated and paralyzed rat skeletal muscle
Schiaffino, S., Gorza, L., Pitton, G., Saggin, L., Ausoni, S., Sartore, S., & Lømo, T. (1988) · Developmental Biology · doi:10.1016/0012-1606(88)90183-2 · Cited by 214 · see citing works
Johnson, J. E. B., Wold, B. J., & Hauschka, S. D. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.8.3393-3399.1989 · Cited by 197 · see citing works
Resource Book for the Design of Animal Exercise Protocols
Jones, J. H. (2007) · American Journal of Veterinary Research · doi:10.2460/ajvr.68.6.583 · Cited by 196 · see citing works
Functional differences in lipid metabolism in resting skeletal muscle of various fiber types
Dyck, D. J., Peters, S. J., Glatz, J. F. C., Górski, J., KEIZER, H. A., Kiens, B., Liu, S., Richter, E. A., Spriet, L. L., Vusse, G. J., et al. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.272.3.e340 · Cited by 186 · see citing works
Primary Prevention of Diabetes Mellitus by Prevention of Obesity in Monkeys
HANSEN, B. C., & Bodkin, N. L. (1993) · Diabetes · doi:10.2337/diab.42.12.1809 · Cited by 155 · see citing works
Jin, L., Galonek, H. L., Israelian, K., Choy, W., Morrison, M. C., Xia, Y. X., Wang, X., Xu, Y., Yang, Y., Smith, J. J., et al. (2009) · Protein Science · doi:10.1002/pro.50 · Cited by 153 · see citing works
A forkhead transcription factor FKHR up‐regulates lipoprotein lipase expression in skeletal muscle
Kamei, Y., Mizukami, J., Miura, S., SUZUKI, M. T., Takahashi, N., Kawada, T., Taniguchi, T., & Ezaki, O. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00062-0 · Cited by 136 · see citing works
Krawiec, B., Nystrom, G. J., Frost, R., Jefferson, L., & Lang, C. H. (2007) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00622.2006 · Cited by 129 · see citing works
Ogilvie, R. W., & Feeback, D. L. (1990) · Stain Technology · doi:10.3109/10520299009105613 · Cited by 116 · see citing works
Law, I. K. M., Liu, L., Xu, A., Lam, K. S. L., Vanhoutte, P. M., Che, C., Leung, P. T. Y., & Wang, Y. (2009) · PROTEOMICS · doi:10.1002/pmic.200800738 · Cited by 115 · see citing works
Bao, J., Lu, Z., Joseph, J. J., Carabenciov, D., Dimond, C. C., Pang, L., Samsel, L., McCoy, J. P., Leclerc, J., Nguyen, P., et al. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22531 · Cited by 115 · see citing works
Johnson, J. E. B., Wold, B. J., & Hauschka, S. D. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.8.3393 · Cited by 115 · see citing works
Furuyama, T., Yamashita, H., Kitayama, K., Higami, Y., Shimokawa, I., & Mori, N. (2002) · Microscopy Research and Technique · doi:10.1002/jemt.10213 · Cited by 114 · see citing works
Suppression of adenocarcinoma by the immunological consequences of calorie restriction
Fernandes, G., Yunis, E. J., & Good, R. A. (1976) · Nature · doi:10.1038/263504b0 · Cited by 108 · see citing works
Shabalina, I. G., Joris Hoeks, J., Kramarova, T. V., Schrauwen, P., Cannon, B., & Nedergaard, J. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.033 · Cited by 101 · see citing works
Caloric restriction delays aging-induced cellular phenotypes in rhesus monkey skeletal muscle
McKiernan, S. H., Colman, R. J., Lopez, M. E., Beasley, T. M., Aiken, J. M., Anderson, R. M., & Weindruch, R. H. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.09.011 · Cited by 94 · see citing works
Donoviel, D. B., Shield, M. A., Buskin, J. N., Haugen, H. S., Clegg, C. H., & Hauschka, S. D. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1649 · Cited by 92 · see citing works
Long-term caloric restriction abrogates the age-related decline in skeletal muscle aerobic function
Hepple, R. T., Baker, D. J., Kaczor, J. J., & Krause, D. J. (2005) · The FASEB Journal · doi:10.1096/fj.04-3535fje · Cited by 80 · see citing works
Dixit, M., Bess, E. N., Fißlthaler, B., Härtel, F. V., Noll, T., Busse, R., & Fleming, I. (2007) · Cardiovascular Research · doi:10.1093/cvr/cvm017 · Cited by 68 · see citing works
Nystrom, G. J., & Lang, C. H. (2008) · PubMed · Cited by 56 · see citing works
A New Splice Variant of the Mouse SIRT3 Gene Encodes the Mitochondrial Precursor Protein
Cooper, H. M., Huang, J.-Y., Verdin, E. M., & Spelbrink, J. N. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004986 · Cited by 55 · see citing works
Chen, B., Ma, Y., Meng, R., Xiong, Z., Wang, H., Zeng, J., Liu, C., & Dong, Y. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.73 · Cited by 53 · see citing works
Characterization of murine SIRT3 transcript variants and corresponding protein products
Yang, Y., Hubbard, B. P., Sinclair, D. A., & Tong, Q. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22795 · Cited by 40 · see citing works
Self-citationMurine Sirt3 protein isoforms have variable half-lives
Yang, Y., Chen, K. Y., & Tong, Q. (2011) · Gene · doi:10.1016/j.gene.2011.07.029 · Cited by 17 · see citing works
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Flagged first, then by citations
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Sorted by citations
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 496 · see citing works
Cheng, A., Yang, Y., Zhou, Y., Maharana, C., Lu, D., Peng, W., Liu, Y., Wan, R., Marosi, K., Misiak, M., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.10.013 · Cited by 371 · see citing works
Lai, Y.-C., Tabima, D. M., Dube, J. J., Hughan, K. S., Vanderpool, R. R., Goncharov, D. A., St. Croix, C. M., Garcia-Ocaña, A., Goncharova, E. A., Tofovic, S. P., et al. (2016) · Circulation · doi:10.1161/circulationaha.115.018935 · Cited by 270 · see citing works
Combined Training Enhances Skeletal Muscle Mitochondrial Oxidative Capacity Independent of Age
Irving, B. A., Lanza, I. R., Henderson, G. C., Rao, R. R., Spiegelman, B. M., & Nair, K. S. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-3081 · Cited by 139 · see citing works
Xu, M., Chen, X., Chen, D., Yu, B., & Huang, Z. (2016) · Oncotarget · doi:10.18632/oncotarget.12891 · Cited by 119 · see citing works
Lithocholic acid binds TULP3 to activate sirtuins and AMPK to slow down ageing
Qu, Q., Chen, Y., Wang, Y., Wang, W., Long, S., Yang, H.-Y., Wu, J., Li, M., Tian, X., Wei, X., et al. (2024) · Nature · doi:10.1038/s41586-024-08348-2 · Cited by 126 · see citing works
Self-citationLithocholic acid phenocopies anti-ageing effects of calorie restriction
Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Li, M., Tian, X., Wei, X., Liu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08329-5 · Cited by 117 · see citing works
Self-citationThe ketogenic diet preserves skeletal muscle with aging in mice
Wallace, M. A., Aguirre, N. W., Marcotte, G. R., Marshall, A. G., Baehr, L. M., Hughes, D. C., Hamilton, K. L., Roberts, M. N., Lopez‐Dominguez, J. A., Miller, B. F., et al. (2021) · Aging Cell · doi:10.1111/acel.13322 · Cited by 93 · see citing works
Zhang, R., Shen, Y., Zhou, L., Sangwung, P., Fujioka, H., Zhang, L., & Liao, X. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.09.001 · Cited by 78 · see citing works
Roland, N., Koltai, E., Taylor, A. W., Suzuki, K., Győri, F. J., & Radak, Z. O. (2018) · Antioxidants · doi:10.3390/antiox7070085 · Cited by 77 · see citing works
Zhang, T., Liu, J., Tong, Q., & Lin, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020372 · Cited by 73 · see citing works
Self-citationLippi, L., de Sire, A., Mezian, K., Curci, C., Perrero, L., Turco, A., Andaloro, S., Ammendolia, A., Fusco, N., & Invernizzi, M. (2022) · Aging Clinical and Experimental Research · doi:10.1007/s40520-021-02073-w · Cited by 65 · see citing works
Buso, A., Comelli, M., Picco, R., Isola, M., Magnesa, B., Pišot, R., Rittweger, J., Salvadego, D., Šimunič, B., Grassi, B., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00474 · Cited by 63 · see citing works
Mechanisms of sex differences in exercise capacity
Oydanich, M., Babici, D., Zhang, J., Rynecki, N., Vatner, D. E., & Vatner, S. F. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00394.2018 · Cited by 55 · see citing works
Animal Models of Exercise From Rodents to Pythons
Hastings, M. H., Herrera, J. J., Guseh, J. S., Atlason, B. A., Houstis, N. E., Kadir, A. A., Li, H., Sheffield, C., Singh, A. P., Roh, J. D., et al. (2022) · Circulation Research · doi:10.1161/circresaha.122.320247 · Cited by 55 · see citing works
SIRT3 in cardiovascular diseases: Emerging roles and therapeutic implications
Lü, Y., Wang, Y., Wang, X., Chen, H., Cai, Z., & Xiang, M. (2016) · International Journal of Cardiology · doi:10.1016/j.ijcard.2016.06.236 · Cited by 52 · see citing works
Maissan, P., Mooij, E., & Barberis, M. (2021) · Biology · doi:10.3390/biology10030194 · Cited by 50 · see citing works
Chiu, H., Chiu, C., Yang, R., Chan, D., Liu, S., & Chiang, C. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12289 · Cited by 48 · see citing works
Li, F., Li, T., Ai, J., Sun, L., Zhu, M., Duan, R., Zhu, L., Liu, Y., & Liu, T. C. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00571 · Cited by 41 · see citing works
Honokiol protects hepatocytes from oxidative injury through mitochondrial deacetylase SIRT3
Liu, J., Shen, S.-N., Tong, Q., Wang, Y., & Lin, L. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.07.036 · Cited by 40 · see citing works
Self-citationNAD+ centric mechanisms and molecular determinants of skeletal muscle disease and aging
Wagner, S., Manickam, R., Brotto, M. A. P., & Tipparaju, S. M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04408-1 · Cited by 39 · see citing works
Guitart‐Mampel, M., Juárez‐Flores, D. L., Youssef, L., Morén, C., García‐Otero, L., Agujetas, V. R., Catalán‐García, M., González‐Casacuberta, I., Tobías, E., Milisenda, J. C., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14282 · Cited by 35 · see citing works
Reddy, Y. N. V., Stewart, G. M., Obokata, M., Koepp, K. E., & Borlaug, B. A. (2021) · European Journal of Heart Failure · doi:10.1002/ejhf.2093 · Cited by 33 · see citing works
The Role of Palmitoleic Acid in Regulating Hepatic Gluconeogenesis through SIRT3 in Obese Mice
Guo, X., Jiang, X., Chen, K., Liang, Q., Zhang, S., Zheng, J., Ma, X., Jiang, H., Wu, H., & Tong, Q. (2022) · Nutrients · doi:10.3390/nu14071482 · Cited by 33 · see citing works
Self-citationWinnik, S. H., Gaul, D. S., Siciliani, G., Lohmann, C., Pasterk, L., Calatayud, N., Weber, J., Eriksson, U., Auwerx, J. H., van Tits, L. J., et al. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0552-7 · Cited by 33 · see citing works
Mizunoya, W., Miyahara, H., Okamoto, S., Akahoshi, M., Suzuki, T., Do, M. Q., Ohtsubo, H., Komiya, Y., Lan, M., Waga, T., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134303 · Cited by 32 · see citing works
Xu, J., Li, C., & Kang, X. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1267456 · Cited by 31 · see citing works
Understanding the perspectives of forkhead transcription factors in delayed wound healing
Rajendran, N. K., Kumar, S. S. D., Houreld, N. N., & Abrahamse, H. (2018) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-018-0484-0 · Cited by 31 · see citing works
Sirtuin3 Dysfunction Is the Key Determinant of Skeletal Muscle Insulin Resistance by Angiotensin II
Macconi, D., Perico, L., Longaretti, L., Morigi, M., Cassis, P., Buelli, S., Perico, N., Remuzzi, G., & Benigni, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127172 · Cited by 26 · see citing works
SIRT3 as a Regulator of Non-alcoholic Fatty Liver Disease
Cho, E.-H. (2014) · Journal of Lifestyle Medicine · doi:10.15280/jlm.2014.4.2.80 · Cited by 26 · see citing works
Mizunoya, W., Okamoto, S., Miyahara, H., Akahoshi, M., Suzuki, T., Do, M. Q., Ohtsubo, H., Komiya, Y., Qahar, M., Waga, T., et al. (2016) · Animal Science Journal · doi:10.1111/asj.12655 · Cited by 24 · see citing works
Resveratrol and Vitamin D: Eclectic Molecules Promoting Mitochondrial Health in Sarcopenia
Russo, C., Valle, M. S., D’Angeli, F., Surdo, S., & Malaguarnera, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147503 · Cited by 24 · see citing works
Abdalla, B. A., Xiong, X., Chai, X., Xu, Q., Gong, J., & Xu, J. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.96885 · Cited by 19 · see citing works
Transient changes to metabolic homeostasis initiate mitochondrial adaptation to endurance exercise
Dent, J. R., Stocks, B., Campelj, D. G., & Philp, A. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.022 · Cited by 18 · see citing works
Guitart‐Mampel, M., González-Tendero, A., Niñerola, S., Morén, C., Catalán‐García, M., González‐Casacuberta, I., Juárez‐Flores, D. L., Ugarteburu, O., Matalonga, L., Cascajo, M. V., et al. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.02.006 · Cited by 18 · see citing works
Sirt3 in POMC neurons controls energy balance in a sex- and diet-dependent manner
Quiñones, M., Hernández-Bautista, R., Beiroa, D., Heras, V., Torres‐Leal, F. L., Lam, B., Senra, A., Fernø, J., Gómez-Valadés, A. G., Schwaninger, M., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101945 · Cited by 18 · see citing works
Hsu, T.-H., Wu, T.-J., Tai, Y.-A., Huang, C., Liao, J., & Yeh, S.-L. (2023) · PLoS ONE · doi:10.1371/journal.pone.0291462 · Cited by 16 · see citing works
Brouwers, B., Stephens, N. A., Costford, S. R., Hopf, M. E., Ayala, J. E., Yi, F., Xie, H., Li, J., Gardell, S. J., Sparks, L. M., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00704 · Cited by 15 · see citing works
Exercise enhancement by RGS14 disruption is mediated by brown adipose tissue
Vatner, D. E., Oydanich, M. K., Zhang, J., Campbell, S. C., & Vatner, S. F. (2023) · Aging Cell · doi:10.1111/acel.13791 · Cited by 15 · see citing works
Rolling out physical exercise and energy homeostasis: Focus on hypothalamic circuitries
Cavalcanti‐de‐Albuquerque, J. P., & Donato, J. (2021) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2021.100944 · Cited by 15 · see citing works
Wang, Z., Li, Q., Yang, H., Zhang, D., Zhang, Y., Wang, J., & Liu, J. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01452 · Cited by 13 · see citing works
Self-citationChabi, B., Fouret, G., Lecomte, J., Cortade, F., Pessemesse, L., Baati, N., Coudray, C., Lin, L., Tong, Q., Wrutniak‐Cabello, C., et al. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9752-1 · Cited by 14 · see citing works
Self-citationEstrogen-related Receptor Signaling in Skeletal Muscle Fitness
Sopariwala, D. H., Nguyen, H., & Narkar, V. A. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2035-8192 · Cited by 12 · see citing works
Vil, L., Roca, C., Elias, I., Casellas, A., Lage, R., Franckhauser, S., & Bosch, F. (2016) · Molecular Therapy — Methods & Clinical Development · doi:10.1038/mtm.2016.72 · Cited by 11 · see citing works
Akashi, S., Morita, A., Mochizuki, Y., Shibuya, F., Kamei, Y., & Miura, S. (2021) · Nutrients · doi:10.3390/nu13020497 · Cited by 11 · see citing works
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112933 · Cited by 11 · see citing works
Talib, N. F., Zhu, Z., & Kim, K. S. (2023) · Nutrients · doi:10.3390/nu15224714 · Cited by 11 · see citing works
Effects of a ketogenic diet on motor function and motor unit number estimation in aged C57BL/6 mice
Padilla, C. J., Harris, H. N., Volek, J. S., Clark, B. C., & Arnold, W. D. (2024) · The journal of nutrition health & aging · doi:10.1016/j.jnha.2024.100219 · Cited by 10 · see citing works
Huang, Z., Hu, L., Liu, Z., & Wang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083644 · Cited by 10 · see citing works
Effects of Gestational Hypoxia on PGC1α and Mitochondrial Acetylation in Fetal Guinea Pig Hearts
Song, H., & Thompson, L. P. (2023) · Reproductive Sciences · doi:10.1007/s43032-023-01245-5 · Cited by 8 · see citing works
Shi, P., Ruan, Y., Liu, W., Sun, J., Xu, J., & Xu, H. (2023) · Animals · doi:10.3390/ani13020319 · Cited by 8 · see citing works
Lensu, S., Pekkala, S., Mäkinen, A., Karstunen, N., Turpeinen, A., Hulmi, J. J., Silvennoinen, M., Ma, H., Kujala, U. M., Karvinen, S. M., et al. (2019) · Metabolism Open · doi:10.1016/j.metop.2019.100019 · Cited by 8 · see citing works
Zhang, J., Hu, M., Wu, X., Guo, M., Ma, Y., Qiu, J., Wang, S., Cao, Y., Zhong, Y., Chen, F., et al. (2025) · Advanced Science · doi:10.1002/advs.202510368 · Cited by 5 · see citing works
Ablation of Ghrelin Receptor Mitigates the Metabolic Decline of Aging Skeletal Muscle
O’Reilly, C. L., Lin, L., Wang, H., Fluckey, J. D., & Sun, Y. (2022) · Genes · doi:10.3390/genes13081368 · Cited by 5 · see citing works
Self-citationOldfield, C. J., Moffatt, T. L., Dolinsky, V. W., & Duhamel, T. A. (2021) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2021-0587 · Cited by 4 · see citing works
Hypoxia induces selective modifications to the acetylome in the brain of zebrafish (Danio rerio)
Dhillon, R. S., & Richards, J. G. (2018) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.12.018 · Cited by 5 · see citing works
Lithocholic acid targets TULP3 to activate sirtuins and AMPK to retard ageingPreprint
Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Wu, J., Li, M., Tian, X., Wei, X., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.07.570558 · Cited by 3 · see citing works
Self-citationHockey, B. L., Braun, J. L., Vandenboom, R., LeBlanc, P. J., MacPherson, R. E. K., & Fajardo, V. A. (2025) · Advanced Exercise and Health Science · doi:10.1016/j.aehs.2025.06.001 · Cited by 2 · see citing works
Sirtuins, mitochondria, and exercise in health and disease
Das, A. M., & Dabke, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00016-1 · Cited by 2 · see citing works
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · Research Square · doi:10.21203/rs.3.rs-1519277/v1 · Cited by 2 · see citing works
Xiao, M., Xu, X.-Y., & Lü, J. (2021) · International Conference on Information Technology and Contemporary Sports (TCS) · doi:10.1109/tcs52929.2021.00052 · Cited by 1 · see citing works
SIRT3 overexpression in rat muscle does not ameliorate peripheral insulin resistance
Osborne, B., Wright, L. E., Brandon, A. E., Stuart, E., Small, L., Joris Hoeks, J., Schrauwen, P., Sinclair, D. A., Montgomery, M. K., Cooney, G. J., et al. (2023) · Journal of Endocrinology · doi:10.1530/joe-22-0101 · Cited by 1 · see citing works
Wang, L., Liu, Z., Hou, Y., & Ge, Y. (2015) · Zhongguo zuzhi gongcheng yanjiu yu linchuang kangfu · Cited by 1 · see citing works
Reply to “Letter to the Editor: Mechanisms of sex differences in exercise capacity”
Oydanich, M. K., Berkman, T., Zhang, J., Galindo, C. L., Vatner, D. E., & Vatner, S. F. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00258.2019 · Cited by 1 · see citing works
Lithocholic acid phenocopies rejuvenating and life-extending effects of calorie restrictionPreprint
Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Li, M., Tian, X., Wei, X., Liu, Y., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.07.570559 · Cited by 1 · see citing works
Self-citationHao, S., Hu, Y., Zhang, L., & Li, J. (2025) · Epigenetics and human health · doi:10.1007/978-3-032-08045-5_6
You, C.-L., Bae, J., Jeong, Y., Leem, Y.-E., Kim, J., Park, J., Vuong, T. A., Jang, J., Park, S., Lee, Y.-S., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02935-7
- Authors
- Lin, L., Chen, K., Khalek, W. A., Ward, J. L., Yang, H., Chabi, B., Wrutniak-Cabello, C., & Tong, Q.
- Affiliations
- Baylor College of Medicine (US)
- Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR)
- Corresponding author
- Tong, Qiang
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2014-01-15
- Volume
- 9
- Issue
- 1
- Pages
- e85636
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3893254
- OpenAlex
- W2044275161
- Cited by
- 67
- References
- 71
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 11 · 2022: 8 · 2021: 9 · 2020: 1 · 2019: 5 · 2018: 9 · 2017: 2 · 2016: 6 · 2015: 5 · 2014: 1
- FWCI
- 2.38
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Agriculture (6250-51000-055, 6250‐51000)
- American Heart Association
- National Institutes of Health
- Agricultural Research Service (6250‐51000‐055, 6250-51000)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK56338, DK075978, P30DK079638, R01DK075978, P30DK056338)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- SIRT3, skeletal muscle, muscle mass, muscle atrophy, MuRF1, FOXO1, AMPK, PPARδ, energy expenditure, lipid oxidation, exercise performance, caloric restriction, mitochondrial deacetylase, transgenic mice
- MeSH terms
- Forkhead Box Protein O1, Animals, Citrate (si)-Synthase, Physical Exertion, Female, Male, Mice, Transgenic, Mitochondria, Muscle, Oxidation-Reduction, Oxygen Consumption, Up-Regulation, Muscle, Skeletal, Lipid Metabolism, Mice, Forkhead Transcription Factors, Creatine Kinase, MM Form, Muscle Strength, Sirtuin 3
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