References
- Kassem M, Abdallah BM. Human bone-marrow-derived mesenchymal stem cells: biological characteristics and potential role in therapy of degenerative diseases. Cell Tissue Res. 2008;331:157–163.
- Pittenger MF, Mackay AM, Beck SC, et al. Multilineage potential of adult human mesenchymal stem cells. Science. 1999;284:143–147.
- Lee K-D, Kuo TK-C, Whang-Peng J, et al. In vitro hepatic differentiation of human mesenchymal stem cells. Hepatology. 2004;40:1275–1284.
- Dezawa M, Kanno H, Hoshino M, et al. Specific induction of neuronal cells from bone marrow stromal cells and application for autologous transplantation. J Clin Invest. 2004;113:1701–1710.
- Quarto R, Mastrogiacomo M, Cancedda R, et al. Repair of large bone defects with the use of autologous bone marrow stromal cells. N Engl J Med. 2001;344:385–386.
- Wollert KC, Meyer GP, Lotz J, et al. Intracoronary autologous bone-marrow cell transfer after myocardial infarction: the BOOST randomised controlled clinical trial. Lancet. 2004;364:141–148.
- Bang OY, Lee JS, Lee PH, et al. Autologous mesenchymal stem cell transplantation in stroke patients. Ann Neurol. 2005;57:874–882.
- Hsu Y-C, Wu Y-T, Yu T-H, et al. Mitochondria in mesenchymal stem cell biology and cell therapy: from cellular differentiation to mitochondrial transfer. Semin Cell Dev Biol. 2016;52:119–131.
- Ieda M, Fu J-D, Delgado-Olguin P, et al. Direct reprogramming of fibroblasts into functional cardiomyocytes by defined factors. Cell. 2010;142:375–386.
- Zhang Y, Marsboom G, Toth PT, et al. Mitochondrial respiration regulates adipogenic differentiation of human mesenchymal stem cells. PLoS One. 2013;8:e77077.
- Storz P. Reactive oxygen species-mediated mitochondria-to-nucleus signaling: a key to aging and radical-caused diseases. Sci STKE. 2006;2006:re3.
- Quirós PM, Mottis A, Auwerx J. Mitonuclear communication in homeostasis and stress. Nat Rev Mol Cell Biol. 2016;17:213–226.
- Vyas S, Zaganjor E, Haigis MC. Mitochondria and cancer. Cell. 2016;166:555–566.
- Chen C-T, Shih Y-RV, Kuo TK, et al. Coordinated changes of mitochondrial biogenesis and antioxidant enzymes during osteogenic differentiation of human mesenchymal stem cells. Stem Cells. 2008;26:960–968.
- Hofmann AD, Beyer M, Krause-Buchholz U, et al. OXPHOS supercomplexes as a hallmark of the mitochondrial phenotype of adipogenic differentiated human MSCs. PLoS One. 2012;7:e35160.
- Lombard DB, Alt FW, Cheng H-L, et al. Mammalian Sir2 homolog Sirt3 regulates global mitochondrial lysine acetylation. Mol Cell Biol. 2007;27:8807–8814.
- Scher MB, Vaquero A, Reinberg D. Sirt3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007;21:920–928.
- Hirschey MD, Shimazu T, Goetzman E, et al. Sirt3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature. 2010;464:121–125.
- Someya S, Yu W, Hallows WC, et al. Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell. 2010;143:802–812.
- Wu YT, Wu SB, Wei YH. Roles of sirtuins in the regulation of antioxidant defense and bioenergetic function of mitochondria under oxidative stress. Free Radic Res. 2014;48:1070–1084.
- Rangarajan P, Karthikeyan A, Lu J, et al. Sirtuin 3 regulates FoxO3a-mediated antioxidant pathway in microglia. Neuroscience. 2015;311:398–414.
- Abdel Khalek W, Cortade F, Ollendorff V, et al. Sirt3, a mitochondrial NAD(+)-dependent deacetylase, is involved in the regulation of myoblast differentiation. PLoS One. 2014;9:e114388.
- Ding Y, Yang H, Wang Y, et al. Sirtuin 3 is required for osteogenic differentiation through maintenance of PGC-1α-SOD2-mediated regulation of mitochondrial function. Int J Biol Sci. 2017;13:254–264.
- Hirschey MD, Shimazu T, Jing E, et al. Sirt3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome. Mol Cell. 2011;44:177–190.
- Lantier L, Williams Ashley S, Williams Ian M, et al. Sirt3 is crucial for maintaining skeletal muscle insulin action and protects against severe insulin resistance in high-fat-fed mice. Diabetes. 2015;64:3081–3092.
- Yu W, Gao B, Li N, et al. Sirt3 deficiency exacerbates diabetic cardiac dysfunction: role of FoxO3A-Parkin-mediated mitophagy. Biochim Biophys Acta. 2017;1863:1973–1983.
- Wu Y-T, Lee H-C, Liao C-C, et al. Regulation of mitochondrial F(o)F(1)ATPase activity by Sirt3-catalyzed deacetylation and its deficiency in human cells harboring 4977bp deletion of mitochondrial DNA. Biochim Biophys Acta. 2013;1832:216–227.
- Lowell BB, Shulman GI. Mitochondrial dysfunction and type 2 diabetes. Science. 2005;307:384–387.
- Caton PW, Richardson SJ, Kieswich J, et al. Sirtuin 3 regulates mouse pancreatic beta cell function and is suppressed in pancreatic islets isolated from human type 2 diabetic patients. Diabetologia. 2013;56:1068–1077.
- Klein J, Perwitz N, Kraus D, et al. Adipose tissue as source and target for novel therapies. Trends Endocrinol Metab. 2006;17:26–32.
- Guilherme A, Virbasius JV, Puri V, et al. Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes. Nat Rev Mol Cell Biol. 2008;9:367–377.
- Choo H-J, Kim J-H, Kwon O-B, et al. Mitochondria are impaired in the adipocytes of type 2 diabetic mice. Diabetologia. 2006;49:784–791.
- Petersen KF, Dufour S, Befroy DB, et al. Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes. N Engl J Med. 2004;350:664–671.
- Wang C-H, Wang C-C, Huang H-C, et al. Mitochondrial dysfunction leads to impairment of insulin sensitivity and adiponectin secretion in adipocytes. FEBS J. 2013;280:1039–1050.
- Chang Y-J, Shih DT, Tseng C-P, et al. Disparate mesenchyme-lineage tendencies in mesenchymal stem cells from human bone marrow and umbilical cord blood. Stem Cells. 2006;24:679–685.
- Tormos KV, Anso E, Hamanaka RB, et al. Mitochondrial complex III ROS regulate adipocyte differentiation. Cell Metab. 2011;14:537–544.
- Dali‐Youcef N, Lagouge M, Froelich S, et al. Sirtuins: the “magnificent seven”, function, metabolism and longevity. Ann Med. 2007;39:335–345.
- Hsu Y-C, Wu Y-T, Tsai C-L, et al. Current understanding and future perspectives of the roles of sirtuins in the reprogramming and differentiation of pluripotent stem cells. Exp Biol Med (Maywood). 2018;243:563–575.
- Yuan Z, Li Q, Luo S, et al. PPARgamma and Wnt signaling in adipogenic and osteogenic differentiation of mesenchymal stem cells. Curr Stem Cell Res Ther. 2016;11:216–225.
- Giralt A, Hondares E, Villena JA, et al. Peroxisome proliferator-activated receptor-gamma coactivator-1alpha controls transcription of the Sirt3 gene, an essential component of the thermogenic brown adipocyte phenotype. J Biol Chem. 2011;286:16958–16966.
- Dai S-H, Chen T, Wang Y-H, et al. Sirt3 protects cortical neurons against oxidative stress via regulating mitochondrial Ca2+ and mitochondrial biogenesis. IJMS. 2014;15:14591–14609.
- Kong X, Wang R, Xue Y, et al. Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS One. 2010;5:e11707.
- Palacios OM, Carmona JJ, Michan S, et al. Diet and exercise signals regulate Sirt3 and activate AMPK and PGC-1alpha in skeletal muscle. Aging. 2009;1:771–783.
- Tseng AH-H, Wu L-H, Shieh S-S, et al. Sirt3 interactions with FoxO3 acetylation, phosphorylation and ubiquitinylation mediate endothelial cell responses to hypoxia. Biochem J. 2014;464:157–168.
- Sundaresan NR, Gupta M, Kim G, et al. Sirt3 blocks the cardiac hypertrophic response by augmenting FoxO3a-dependent antioxidant defense mechanisms in mice. J Clin Invest. 2009;119:2758–2771.
- Zhang S, Hulver MW, McMillan RP, et al. The pivotal role of pyruvate dehydrogenase kinases in metabolic flexibility. Nutr Metab (Lond). 2014;11:10.
- Jing E, O'Neill BT, Rardin MJ, et al. Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation. Diabetes. 2013;62:3404–3417.
- Yang L, Zhang J, Xing W, et al. Sirt3 Deficiency induces endothelial insulin resistance and blunts endothelial-dependent vasorelaxation in mice and human with obesity. Sci Rep. 2016;6:23366.
- Jukarainen S, Heinonen S, Rämö JT, et al. Obesity is associated with low NAD+/SIRT pathway expression in adipose tissue of BMI-discordant monozygotic twins. J Clin Endocrinol Metab. 2016;101:275–283.
- Boyle KE, Newsom SA, Janssen RC, et al. Skeletal muscle MnSOD, mitochondrial complex II, and Sirt3 enzyme activities are decreased in maternal obesity during human pregnancy and gestational diabetes mellitus. J Clin Endocrinol Metab. 2013;98:E1601–E1609.
- Moschen AR, Wieser V, Gerner RR, et al. Adipose tissue and liver expression of SIRT1, 3, and 6 increase after extensive weight loss in morbid obesity. J Hepatol. 2013;59;59:1315–1322.
- Porter LC, Franczyk MP, Pietka T, et al. NAD+-dependent deacetylase Sirt3 in adipocytes is dispensable for maintaining normal adipose tissue mitochondrial function and whole-body metabolism. Am J Physiol Endocrinol Metab. 2018. [Epub ahead of print]. doi: 10.1152/ajpendo.00057.2018
- Barbagallo I, Li Volti G, Galvano F, et al. Diabetic human adipose tissue-derived mesenchymal stem cells fail to differentiate in functional adipocytes. Exp Biol Med (Maywood). 2017;242:1079–1085.