The Effect of Metabolites on Mitochondrial Functions in the Pathogenesis of Skeletal Muscle Aging

References

• Cruz-Jentoft AJ, Baeyens JP, Bauer JM, et al. Sarcopenia: European consensus on definition and diagnosis: report of the European Working Group on sarcopenia in older people. Age Ageing. 2010;39(4):412–423. doi:10.1093/ageing/afq034
   PubMed Web of Science ®Google Scholar
• Shafiee G, Keshtkar A, Soltani A, et al. Prevalence of sarcopenia in the world: a systematic review and meta- analysis of general population studies. J Diabetes Metab Disord. 2017;16:21. doi:10.1186/s40200-017-0302-x
   PubMed Web of Science ®Google Scholar
• Goodpaster BH, Park SW, Harris TB, et al. The loss of skeletal muscle strength, mass, and quality in older adults: the health, aging and body composition study. J Gerontol A Biol Sci Med Sci. 2006;61(10):1059–1064. doi:10.1093/gerona/61.10.1059
   PubMed Web of Science ®Google Scholar
• Beaudart C, Zaaria M, Pasleau F, et al. Health outcomes of sarcopenia: a systematic review and meta-analysis. PLoS One. 2017;12(1):e0169548. doi:10.1371/journal.pone.0169548
   PubMed Web of Science ®Google Scholar
• Dardevet D, Mosoni L, Savary-Auzeloux I, et al. Important determinants to take into account to optimize protein nutrition in the elderly: solutions to a complex equation. Proc Nutr Soc. 2021;80(2):207–220. doi:10.1017/S0029665120007934
   PubMed Web of Science ®Google Scholar
• Cho MR, Lee S, Song SK. A review of sarcopenia pathophysiology, diagnosis, treatment and future direction. J Korean Med Sci. 2022;37(18):e146. doi:10.3346/jkms.2022.37.e146
   PubMed Web of Science ®Google Scholar
• Fulop T, Larbi A, Dupuis G, et al. Immunosenescence and inflamm-aging as two sides of the same coin: friends or foes? Front Immunol. 2017;8:1960. doi:10.3389/fimmu.2017.01960
   PubMed Web of Science ®Google Scholar
• Ferri E, Marzetti E, Calvani R, et al. Role of age-related mitochondrial dysfunction in sarcopenia. Int J Mol Sci. 2020;21(15):5236. doi:10.3390/ijms21155236
   PubMed Web of Science ®Google Scholar
• Marzetti E, Calvani R, Cesari M, et al. Mitochondrial dysfunction and sarcopenia of aging: from signaling pathways to clinical trials. Int J Biochem Cell Biol. 2013;45(10):2288–2301. doi:10.1016/j.biocel.2013.06.024
   PubMed Web of Science ®Google Scholar
• Crane JD, Devries MC, Safdar A, et al. The effect of aging on human skeletal muscle mitochondrial and intramyocellular lipid ultrastructure. J Gerontol A Biol Sci Med Sci. 2010;65(2):119–128. doi:10.1093/gerona/glp179
   PubMed Web of Science ®Google Scholar
• Short KR, Vittone JL, Bigelow ML, et al. Age and aerobic exercise training effects on whole body and muscle protein metabolism. Am J Physiol Endocrinol Metab. 2004;286(1):E92–101. doi:10.1152/ajpendo.00366.2003
   PubMed Web of Science ®Google Scholar
• Petersen KF, Befroy D, Dufour S, et al. Mitochondrial dysfunction in the elderly: possible role in insulin resistance. Science. 2003;300(5622):1140–1142. doi:10.1126/science.1082889
   PubMed Web of Science ®Google Scholar
• Kim Y, Triolo M, Hood DA. Impact of aging and exercise on mitochondrial quality control in skeletal muscle. Oxid Med Cell Longev. 2017;2017:3165396. doi:10.1155/2017/3165396
   PubMed Web of Science ®Google Scholar
• Lustgarten MS, Price LL, Chale A, et al. Branched chain amino acids are associated with muscle mass in functionally limited older adults. J Gerontol a Biol Sci Med Sci. 2014;69(6):717–724. doi:10.1093/gerona/glt152
   PubMed Web of Science ®Google Scholar
• Lu Y, Karagounis LG, Ng TP, et al. Systemic and metabolic signature of sarcopenia in community-dwelling older adults. J Gerontol A Biol Sci Med Sci. 2020;75(2):309–317. doi:10.1093/gerona/glz001
   PubMed Web of Science ®Google Scholar
• Yamada M, Kimura Y, Ishiyama D, et al. Plasma amino acid concentrations are associated with muscle function in older Japanese women. J Nutr Health Aging. 2018;22(7):819–823. doi:10.1007/s12603-018-1014-8
   PubMed Web of Science ®Google Scholar
• Meng L, Yang R, Wang D, et al. Specific lysophosphatidylcholine and acylcarnitine related to sarcopenia and its components in older men. BMC Geriatr. 2022;22(1):249. doi:10.1186/s12877-022-02953-4
   PubMed Web of Science ®Google Scholar
• Le Couteur DG, Solon-Biet SM, Cogger VC, et al. Branched chain amino acids, aging and age-related health. Ageing Res Rev. 2020;64:101198. doi:10.1016/j.arr.2020.101198
   PubMed Web of Science ®Google Scholar
• Holecek M. Branched-chain amino acids in health and disease: metabolism, alterations in blood plasma, and as supplements. Nutr Metab. 2018;15:33. doi:10.1186/s12986-018-0271-1
   Google Scholar
• Biswas D, Duffley L, Pulinilkunnil T. Role of branched-chain amino acid-catabolizing enzymes in intertissue signaling, metabolic remodeling, and energy homeostasis. FASEB J. 2019;33(8):8711–8731. doi:10.1096/fj.201802842RR
   PubMed Web of Science ®Google Scholar
• Neinast M, Murashige D, Arany Z. Branched chain amino acids. Annu Rev Physiol. 2019;81:139–164. doi:10.1146/annurev-physiol-020518-114455
   PubMed Web of Science ®Google Scholar
• D’Antona G, Ragni M, Cardile A, et al. Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab. 2010;12(4):362–372. doi:10.1016/j.cmet.2010.08.016
   PubMed Web of Science ®Google Scholar
• Saxton RA, Knockenhauer KE, Wolfson RL, et al. Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Science. 2016;351(6268):53–58. doi:10.1126/science.aad2087
   PubMed Web of Science ®Google Scholar
• Zhang L, Li F, Guo Q, et al. Leucine supplementation: a novel strategy for modulating lipid metabolism and energy homeostasis. Nutrients. 2020;12(5):1299. doi:10.3390/nu12051299
   PubMed Web of Science ®Google Scholar
• Jewell JL, Russell RC, Guan KL. Amino acid signalling upstream of mTOR. Nat Rev Mol Cell Biol. 2013;14(3):133–139. doi:10.1038/nrm3522
   PubMed Web of Science ®Google Scholar
• Zhenyukh O, Civantos E, Ruiz-Ortega M, et al. High concentration of branched-chain amino acids promotes oxidative stress, inflammation and migration of human peripheral blood mononuclear cells via mTORC1 activation. Free Radic Biol Med. 2017;104:165–177. doi:10.1016/j.freeradbiomed.2017.01.009
   PubMed Web of Science ®Google Scholar
• Yoon MS. The emerging role of branched-chain amino acids in insulin resistance and metabolism. Nutrients. 2016;8(7):405. doi:10.3390/nu8070405
   PubMed Web of Science ®Google Scholar
• Li CW, Yu K, Shyh‐Chang N, et al. Pathogenesis of sarcopenia and the relationship with fat mass: descriptive review. J Cachexia Sarcopenia Muscle. 2022;13(2):781–794. doi:10.1002/jcsm.12901
   PubMed Web of Science ®Google Scholar
• Moaddel R, Fabbri E, Khadeer MA, et al. Plasma biomarkers of poor muscle quality in older men and women from the baltimore longitudinal study of aging. J Gerontol A Biol Sci Med Sci. 2016;71(10):1266–1272. doi:10.1093/gerona/glw046
   PubMed Web of Science ®Google Scholar
• Toyoshima K, Nakamura M, Adachi Y, et al. Increased plasma proline concentrations are associated with sarcopenia in the elderly. PLoS One. 2017;12(9):e0185206. doi:10.1371/journal.pone.0185206
   PubMed Web of Science ®Google Scholar
• Dideriksen K, Reitelseder S, Holm L. Influence of amino acids, dietary protein, and physical activity on muscle mass development in humans. Nutrients. 2013;5(3):852–876. doi:10.3390/nu5030852
   PubMed Web of Science ®Google Scholar
• Ninomiya S, Nakamura N, Nakamura H, et al. Low levels of serum tryptophan underlie skeletal muscle atrophy. Nutrients. 2020;12(4):978. doi:10.3390/nu12040978
   PubMed Web of Science ®Google Scholar
• Lee MN, Ha SH, Kim J, et al. Glycolytic flux signals to mTOR through glyceraldehyde-3-phosphate dehydrogenase-mediated regulation of Rheb. Mol Cell Biol. 2009;29(14):3991–4001. doi:10.1128/MCB.00165-09
   PubMed Web of Science ®Google Scholar
• Tisdale MJ. Mechanisms of cancer cachexia. Physiol Rev. 2009;89(2):381–410. doi:10.1152/physrev.00016.2008
   PubMed Web of Science ®Google Scholar
• Engelman JA, Luo J, Cantley LC. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat Rev Genet. 2006;7(8):606–619. doi:10.1038/nrg1879
   PubMed Web of Science ®Google Scholar
• Roux PP, Topisirovic I. Regulation of mRNA translation by signaling pathways. Cold Spring Harb Perspect Biol. 2012;4(11):a012252–a012252. doi:10.1101/cshperspect.a012252
   PubMed Web of Science ®Google Scholar
• Nacarelli T, Azar A, Sell C. Aberrant mTOR activation in senescence and aging: a mitochondrial stress response? Exp Gerontol. 2015;68:66–70. doi:10.1016/j.exger.2014.11.004
   PubMed Web of Science ®Google Scholar
• Connell NJ, Grevendonk L, Fealy CE, et al. NAD+-precursor supplementation with L-tryptophan, nicotinic acid, and nicotinamide does not affect mitochondrial function or skeletal muscle function in physically compromised older adults. J Nutr. 2021;151(10):2917–2931. doi:10.1093/jn/nxab193
   PubMed Web of Science ®Google Scholar
• Sorgdrager FJH, Naudé PJW, Kema IP, et al. Tryptophan metabolism in inflammaging: from biomarker to therapeutic target. Front Immunol. 2019;10:2565. doi:10.3389/fimmu.2019.02565
   PubMed Web of Science ®Google Scholar
• Vécsei L, Szalárdy L, Fülöp F, Toldi J. Kynurenines in the CNS: recent advances and new questions. Nat Rev Drug Discov. 2013;12(1):64–82. doi:10.1038/nrd3793
   PubMed Web of Science ®Google Scholar
• Calvani R, Picca A, Marini F, et al. A distinct pattern of circulating amino acids characterizes older persons with physical frailty and sarcopenia: results from the BIOSPHERE study. Nutrients. 2018;10(11):1691. doi:10.3390/nu10111691
   PubMed Web of Science ®Google Scholar
• Yeung SSY, Zhu ZL, Kwok T, et al. Serum amino acids patterns and 4-year sarcopenia risk in community-dwelling chinese older adults. Gerontology. 2021;68:1–10.
   PubMed Web of Science ®Google Scholar
• Calvani R, Miccheli A, Landi F, et al. Current nutritional recommendations and novel dietary strategies to manage sarcopenia. J Frailty Aging. 2013;2(1):38–53.
   PubMedGoogle Scholar
• Ducker GS, Rabinowitz JD. One-carbon metabolism in health and disease. Cell Metab. 2017;25(1):27–42. doi:10.1016/j.cmet.2016.08.009
   PubMed Web of Science ®Google Scholar
• Tibbetts AS, Appling DR. Compartmentalization of Mammalian folate-mediated one-carbon metabolism. Annu Rev Nutr. 2010;30:57–81. doi:10.1146/annurev.nutr.012809.104810
   PubMed Web of Science ®Google Scholar
• Herbig K, Chiang E-P, Lee L-R, et al. Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses. J Biol Chem. 2002;277(41):38381–38389. doi:10.1074/jbc.M205000200
   PubMed Web of Science ®Google Scholar
• Yang XM, MacKenzie RE. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene. Biochemistry. 1993;32(41):11118–11123. doi:10.1021/bi00092a022
   PubMed Web of Science ®Google Scholar
• Lopes A. Mitochondrial metabolism and DNA methylation: a review of the interaction between two genomes. Clin Epigenetics. 2020;12(1):182. doi:10.1186/s13148-020-00976-5
   PubMed Web of Science ®Google Scholar
• Bao XR, Ong S-E, Goldberger O, et al. Mitochondrial dysfunction remodels one-carbon metabolism in human cells. Elife. 2016;5. doi:10.7554/eLife.10575
   Web of Science ®Google Scholar
• Nikkanen J, Forsström S, Euro L, et al. Mitochondrial DNA replication defects disturb cellular dNTP pools and remodel one-carbon metabolism. Cell Metab. 2016;23(4):635–648. doi:10.1016/j.cmet.2016.01.019
   PubMed Web of Science ®Google Scholar
• Picca A, Ponziani FR, Calvani R, et al. Gut microbial, inflammatory and metabolic signatures in older people with physical frailty and sarcopenia: results from the BIOSPHERE study. Nutrients. 2019;12(1):65. doi:10.3390/nu12010065
   PubMed Web of Science ®Google Scholar
• Wagenmakers AJ. Muscle amino acid metabolism at rest and during exercise: role in human physiology and metabolism. Exerc Sport Sci Rev. 1998;26:287–314. doi:10.1249/00003677-199800260-00013
   PubMed Web of Science ®Google Scholar
• Kameda M, Teruya T, Yanagida M, et al. Reduced uremic metabolites are prominent feature of sarcopenia, distinct from antioxidative markers for frailty. Aging. 2021;13(17):20915–20934. doi:10.18632/aging.203498
   PubMedGoogle Scholar
• Birsoy K, Wang T, Chen W, et al. An essential role of the mitochondrial electron transport chain in cell proliferation is to enable aspartate synthesis. Cell. 2015;162(3):540–551. doi:10.1016/j.cell.2015.07.016
   PubMed Web of Science ®Google Scholar
• Sullivan LB, Gui D, Hosios A, et al. Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells. Cell. 2015;162(3):552–563. doi:10.1016/j.cell.2015.07.017
   PubMed Web of Science ®Google Scholar
• Cardaci S, Zheng L, MacKay G, et al. Pyruvate carboxylation enables growth of SDH-deficient cells by supporting aspartate biosynthesis. Nat Cell Biol. 2015;17(10):1317–1326. doi:10.1038/ncb3233
   PubMed Web of Science ®Google Scholar
• Krall AS, Xu S, Graeber TG, et al. Asparagine promotes cancer cell proliferation through use as an amino acid exchange factor. Nat Commun. 2016;7:11457. doi:10.1038/ncomms11457
   PubMed Web of Science ®Google Scholar
• Krall AS, Mullen PJ, Surjono F, et al. Asparagine couples mitochondrial respiration to ATF4 activity and tumor growth. Cell Metab. 2021;33(5):1013–1026 e6. doi:10.1016/j.cmet.2021.02.001
   PubMed Web of Science ®Google Scholar
• Alkan HF, Walter KE, Luengo A, et al. Cytosolic aspartate availability determines cell survival when glutamine is limiting. Cell Metab. 2018;28(5):706–720 e6. doi:10.1016/j.cmet.2018.07.021
   PubMed Web of Science ®Google Scholar
• Klimova T, Chandel NS. Mitochondrial complex III regulates hypoxic activation of HIF. Cell Death Differ. 2008;15(4):660–666. doi:10.1038/sj.cdd.4402307
   PubMed Web of Science ®Google Scholar
• Jezek P, Plecitá-Hlavatá L, Smolková K, et al. Distinctions and similarities of cell bioenergetics and the role of mitochondria in hypoxia, cancer, and embryonic development. Int J Biochem Cell Biol. 2010;42(5):604–622. doi:10.1016/j.biocel.2009.11.008
   PubMed Web of Science ®Google Scholar
• Kim JW, Tchernyshyov I, Semenza GL, et al. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab. 2006;3(3):177–185. doi:10.1016/j.cmet.2006.02.002
   PubMed Web of Science ®Google Scholar
• Semenza GL. Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1. Biochem J. 2007;405(1):1–9. doi:10.1042/BJ20070389
   PubMed Web of Science ®Google Scholar
• Ng TKS, Kovalik J-P, Ching J, et al. Novel metabolomics markers are associated with pre-clinical decline in hand grip strength in community-dwelling older adults. Mech Ageing Dev. 2021;193:111405. doi:10.1016/j.mad.2020.111405
   PubMed Web of Science ®Google Scholar
• Sensi SL. Alzheimer’s disease, time to turn the tide. Aging. 2018;10(10):2537–2538. doi:10.18632/aging.101581
   PubMedGoogle Scholar
• Gancheva S, Jelenik T, Álvarez-Hernández E, et al. Interorgan metabolic crosstalk in human insulin resistance. Physiol Rev. 2018;98(3):1371–1415. doi:10.1152/physrev.00015.2017
   PubMed Web of Science ®Google Scholar
• Magi S, Piccirillo S, Amoroso S. The dual face of glutamate: from a neurotoxin to a potential survival factor-metabolic implications in health and disease. Cell Mol Life Sci. 2019;76(8):1473–1488. doi:10.1007/s00018-018-3002-x
   PubMed Web of Science ®Google Scholar
• Fiermonte G, Palmieri L, Todisco S, et al. Identification of the mitochondrial glutamate transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms. J Biol Chem. 2002;277(22):19289–19294. doi:10.1074/jbc.M201572200
   PubMed Web of Science ®Google Scholar
• Schantz PG, Henriksson J. Enzyme levels of the NADH shuttle systems: measurements in isolated muscle fibres from humans of differing physical activity. Acta Physiol Scand. 1987;129(4):505–515. doi:10.1111/j.1748-1716.1987.tb08090.x
   PubMedGoogle Scholar
• Verma M, Lizama BN, Chu CT. Excitotoxicity, calcium and mitochondria: a triad in synaptic neurodegeneration. Transl Neurodegener. 2022;11(1):3. doi:10.1186/s40035-021-00278-7
   PubMed Web of Science ®Google Scholar
• Zhao K, Hong H, Zhao L, et al. Postsynaptic cAMP signalling regulates the antagonistic balance of Drosophila glutamate receptor subtypes. Development. 2020;147(24). doi:10.1242/dev.191874
   Web of Science ®Google Scholar
• Deschenes MR, Flannery R, Hawbaker A, et al. Adaptive remodeling of the neuromuscular junction with aging. Cells. 2022;11(7):1150. doi:10.3390/cells11071150
   PubMed Web of Science ®Google Scholar
• Miyamoto K, Hirayama A, Sato Y, et al. A metabolomic profile predictive of new osteoporosis or sarcopenia development. Metabolites. 2021;11(5):278. doi:10.3390/metabo11050278
   PubMed Web of Science ®Google Scholar
• Scicchitano BM, Sica G. The beneficial effects of taurine to counteract sarcopenia. Curr Protein Pept Sci. 2018;19(7):673–680. doi:10.2174/1389203718666161122113609
   PubMed Web of Science ®Google Scholar
• Huxtable RJ. Physiological actions of taurine. Physiol Rev. 1992;72(1):101–163. doi:10.1152/physrev.1992.72.1.101
   PubMed Web of Science ®Google Scholar
• Ramos-Mandujano G, Hernandez-Benitez R, Pasantes-Morales H. Multiple mechanisms mediate the taurine-induced proliferation of neural stem/progenitor cells from the subventricular zone of the adult mouse. Stem Cell Res. 2014;12(3):690–702. doi:10.1016/j.scr.2014.02.009
   PubMed Web of Science ®Google Scholar
• Lambert IH, Kristensen DM, Holm JB, et al. Physiological role of taurine–from organism to organelle. Acta Physiol. 2015;213(1):191–212. doi:10.1111/apha.12365
   PubMed Web of Science ®Google Scholar
• Silva LA, Silveira PCL, Ronsani MM, et al. Taurine supplementation decreases oxidative stress in skeletal muscle after eccentric exercise. Cell Biochem Funct. 2011;29(1):43–49. doi:10.1002/cbf.1716
   PubMed Web of Science ®Google Scholar
• Jong CJ, Azuma J, Schaffer S. Mechanism underlying the antioxidant activity of taurine: prevention of mitochondrial oxidant production. Amino Acids. 2012;42(6):2223–2232. doi:10.1007/s00726-011-0962-7
   PubMed Web of Science ®Google Scholar
• Suzuki T, Suzuki T, Wada T, et al. Taurine as a constituent of mitochondrial tRNAs: new insights into the functions of taurine and human mitochondrial diseases. EMBO J. 2002;21(23):6581–6589. doi:10.1093/emboj/cdf656
   PubMed Web of Science ®Google Scholar
• Ricci C, Pastukh V, Leonard J, et al. Mitochondrial DNA damage triggers mitochondrial-superoxide generation and apoptosis. Am J Physiol Cell Physiol. 2008;294(2):C413–22. doi:10.1152/ajpcell.00362.2007
   PubMed Web of Science ®Google Scholar
• De Luca A, Pierno S, Camerino DC. Taurine: the appeal of a safe amino acid for skeletal muscle disorders. J Transl Med. 2015;13:243. doi:10.1186/s12967-015-0610-1
   PubMed Web of Science ®Google Scholar
• Ter Borg S, de Groot LC, Mijnarends DM, et al. Differences in nutrient intake and biochemical nutrient status between sarcopenic and nonsarcopenic older adults-results from the maastricht sarcopenia study. J Am Med Dir Assoc. 2016;17(5):393–401. doi:10.1016/j.jamda.2015.12.015
   PubMed Web of Science ®Google Scholar
• Holick MF. Vitamin D status: measurement, interpretation, and clinical application. Ann Epidemiol. 2009;19(2):73–78. doi:10.1016/j.annepidem.2007.12.001
   PubMed Web of Science ®Google Scholar
• Latham CM, Brightwell CR, Keeble AR, et al. Vitamin D promotes skeletal muscle regeneration and mitochondrial health. Front Physiol. 2021;12:660498. doi:10.3389/fphys.2021.660498
   PubMed Web of Science ®Google Scholar
• Ricca C, Aillon A, Bergandi L, Alotto D, Castagnoli C, Silvagno F. Vitamin D receptor is necessary for mitochondrial function and cell health. Int J Mol Sci. 2018;19:1672.
   PubMed Web of Science ®Google Scholar
• Dzik K, Skrobot W, Flis DJ, et al. Vitamin D supplementation attenuates oxidative stress in paraspinal skeletal muscles in patients with low back pain. Eur J Appl Physiol. 2018;118(1):143–151. doi:10.1007/s00421-017-3755-1
   PubMed Web of Science ®Google Scholar
• Bhat M, Ismail A. Vitamin D treatment protects against and reverses oxidative stress induced muscle proteolysis. J Steroid Biochem Mol Biol. 2015;152:171–179. doi:10.1016/j.jsbmb.2015.05.012
   PubMed Web of Science ®Google Scholar
• Ashcroft SP, Bass JJ, Kazi AA, et al. The vitamin D receptor regulates mitochondrial function in C2C12 myoblasts. Am J Physiol Cell Physiol. 2020;318(3):C536–C541. doi:10.1152/ajpcell.00568.2019
   PubMed Web of Science ®Google Scholar
• Alkharfy KM, Al-Daghri NM, Ahmed M, et al. Effects of vitamin D treatment on skeletal muscle histology and ultrastructural changes in a rodent model. Molecules. 2012;17(8):9081–9089. doi:10.3390/molecules17089081
   PubMed Web of Science ®Google Scholar
• Glerup H, Mikkelsen K, Poulsen L, et al. Hypovitaminosis D myopathy without biochemical signs of osteomalacic bone involvement. Calcif Tissue Int. 2000;66(6):419–424. doi:10.1007/s002230010085
   PubMed Web of Science ®Google Scholar
• Bauer JM, Verlaan S, Bautmans I, et al. Effects of a vitamin D and leucine-enriched whey protein nutritional supplement on measures of sarcopenia in older adults, the PROVIDE study: a randomized, double-blind, placebo-controlled trial. J Am Med Dir Assoc. 2015;16(9):740–747. doi:10.1016/j.jamda.2015.05.021
   PubMed Web of Science ®Google Scholar
• Fearon KC. Cancer cachexia and fat-muscle physiology. N Engl J Med. 2011;365(6):565–567. doi:10.1056/NEJMcibr1106880
   PubMed Web of Science ®Google Scholar
• Reuter SE, Evans AM. Carnitine and acylcarnitines: pharmacokinetic, pharmacological and clinical aspects. Clin Pharmacokinet. 2012;51(9):553–572. doi:10.1007/BF03261931
   PubMed Web of Science ®Google Scholar
• McGill MR, Li F, Sharpe MR, et al. Circulating acylcarnitines as biomarkers of mitochondrial dysfunction after Acetaminophen overdose in mice and humans. Arch Toxicol. 2014;88(2):391–401. doi:10.1007/s00204-013-1118-1
   PubMed Web of Science ®Google Scholar
• Rizza S, Copetti M, Rossi C, et al. Metabolomics signature improves the prediction of cardiovascular events in elderly subjects. Atherosclerosis. 2014;232(2):260–264. doi:10.1016/j.atherosclerosis.2013.10.029
   PubMed Web of Science ®Google Scholar
• Meng L, Shi H, Wang D-G, et al. Specific metabolites involved in antioxidation and mitochondrial function are correlated with frailty in elderly men. Front Med. 2022;9:816045. doi:10.3389/fmed.2022.816045
   Web of Science ®Google Scholar
• Tonsgard JH, Getz GS. Effect of Reye’s syndrome serum on isolated chinchilla liver mitochondria. J Clin Invest. 1985;76(2):816–825. doi:10.1172/JCI112039
   PubMed Web of Science ®Google Scholar
• Hirabara SM, Curi R, Maechler P. Saturated fatty acid-induced insulin resistance is associated with mitochondrial dysfunction in skeletal muscle cells. J Cell Physiol. 2010;222(1):187–194. doi:10.1002/jcp.21936
   PubMed Web of Science ®Google Scholar
• Gao X, Lee K, Reid MA, et al. Serine availability influences mitochondrial dynamics and function through lipid metabolism. Cell Rep. 2018;22(13):3507–3520. doi:10.1016/j.celrep.2018.03.017
   PubMed Web of Science ®Google Scholar
• Senyilmaz-Tiebe D, Pfaff DH, Virtue S, et al. Dietary stearic acid regulates mitochondria in vivo in humans. Nat Commun. 2018;9(1):3129. doi:10.1038/s41467-018-05614-6
   PubMed Web of Science ®Google Scholar
• Senyilmaz D, Virtue S, Xu X, et al. Regulation of mitochondrial morphology and function by stearoylation of TFR1. Nature. 2015;525(7567):124–128. doi:10.1038/nature14601
   PubMed Web of Science ®Google Scholar
• Tian Q, Mitchell BA, Zampino M, et al. Longitudinal associations between blood lysophosphatidylcholines and skeletal muscle mitochondrial function. Geroscience. 2022. doi:10.1007/s11357-022-00548-w
   Web of Science ®Google Scholar
• da Silva JF, Alves J, Silva-Neto J, et al. Lysophosphatidylcholine induces oxidative stress in human endothelial cells via NOX5 activation - implications in atherosclerosis. Clin Sci. 2021;135(15):1845–1858. doi:10.1042/CS20210468
   Web of Science ®Google Scholar
• Hung ND, Sok DE, Kim MR. Prevention of 1-palmitoyl lysophosphatidylcholine-induced inflammation by polyunsaturated acyl lysophosphatidylcholine. Inflamm Res. 2012;61(5):473–483. doi:10.1007/s00011-012-0434-x
   PubMed Web of Science ®Google Scholar
• Klingler C, Zhao X, Adhikary T, et al. Lysophosphatidylcholines activate PPARdelta and protect human skeletal muscle cells from lipotoxicity. Biochim Biophys Acta. 2016;1861(12 Pt A):1980–1992. doi:10.1016/j.bbalip.2016.09.020
   PubMed Web of Science ®Google Scholar
• Schlame M, Greenberg ML. Biosynthesis, remodeling and turnover of mitochondrial cardiolipin. Biochim Biophys Acta Mol Cell Biol Lipids. 2017;1862(1):3–7. doi:10.1016/j.bbalip.2016.08.010
   PubMed Web of Science ®Google Scholar
• Falabella M, Vernon HJ, Hanna MG, et al. Cardiolipin, mitochondria, and neurological disease. Trends Endocrinol Metab. 2021;32(4):224–237. doi:10.1016/j.tem.2021.01.006
   PubMed Web of Science ®Google Scholar
• Paradies G, Paradies V, De Benedictis V, et al. Functional role of cardiolipin in mitochondrial bioenergetics. Biochim Biophys Acta. 2014;1837(4):408–417. doi:10.1016/j.bbabio.2013.10.006
   PubMed Web of Science ®Google Scholar
• Stepanyants N, Macdonald PJ, Francy CA, et al. Cardiolipin’s propensity for phase transition and its reorganization by dynamin-related protein 1 form a basis for mitochondrial membrane fission. Mol Biol Cell. 2015;26(17):3104–3116. doi:10.1091/mbc.E15-06-0330
   PubMed Web of Science ®Google Scholar
• Ban T, Ishihara T, Kohno H, et al. Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin. Nat Cell Biol. 2017;19(7):856–863. doi:10.1038/ncb3560
   PubMed Web of Science ®Google Scholar
• Chu CT, Bayir H, Kagan VE. LC3 binds externalized cardiolipin on injured mitochondria to signal mitophagy in neurons: implications for Parkinson disease. Autophagy. 2014;10(2):376–378. doi:10.4161/auto.27191
   PubMed Web of Science ®Google Scholar
• Chu CT, Ji J, Dagda RK, et al. Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells. Nat Cell Biol. 2013;15(10):1197–1205. doi:10.1038/ncb2837
   PubMed Web of Science ®Google Scholar
• Bucci L, Yani SL, Fabbri C, et al. Circulating levels of adipokines and IGF-1 are associated with skeletal muscle strength of young and old healthy subjects. Biogerontology. 2013;14(3):261–272. doi:10.1007/s10522-013-9428-5
   PubMed Web of Science ®Google Scholar
• Lu G, Sun H, She P, et al. Protein phosphatase 2Cm is a critical regulator of branched-chain amino acid catabolism in mice and cultured cells. J Clin Invest. 2009;119(6):1678–1687. doi:10.1172/JCI38151
   PubMed Web of Science ®Google Scholar
• Bifari F, Nisoli E. Branched-chain amino acids differently modulate catabolic and anabolic states in mammals: a pharmacological point of view. Br J Pharmacol. 2017;174(11):1366–1377. doi:10.1111/bph.13624
   PubMed Web of Science ®Google Scholar
• Iwabu M, Yamauchi T, Okada-Iwabu M, et al. Adiponectin and AdipoR1 regulate PGC-1alpha and mitochondria by Ca(2+) and AMPK/SIRT1. Nature. 2010;464(7293):1313–1319. doi:10.1038/nature08991
   PubMed Web of Science ®Google Scholar
• Kalinkovich A, Livshits G. Sarcopenic obesity or obese sarcopenia: a cross talk between age-associated adipose tissue and skeletal muscle inflammation as a main mechanism of the pathogenesis. Ageing Res Rev. 2017;35:200–221. doi:10.1016/j.arr.2016.09.008
   PubMed Web of Science ®Google Scholar
• Alizadeh Pahlavani H. Exercise therapy for people with sarcopenic obesity: myokines and adipokines as effective actors. Front Endocrinol (Lausanne). 2022;13:811751. doi:10.3389/fendo.2022.811751
   PubMed Web of Science ®Google Scholar
• Peng J, Yin L, Wang X. Central and peripheral leptin resistance in obesity and improvements of exercise. Horm Behav. 2021;133:105006. doi:10.1016/j.yhbeh.2021.105006
   PubMed Web of Science ®Google Scholar
• Li L, Pan R, Li R, et al. Mitochondrial biogenesis and peroxisome proliferator-activated receptor-gamma coactivator-1alpha (PGC-1alpha) deacetylation by physical activity: intact adipocytokine signaling is required. Diabetes. 2011;60(1):157–167. doi:10.2337/db10-0331
   PubMed Web of Science ®Google Scholar
• Kim H, Kim M, Kojima N, et al. Exercise and nutritional supplementation on community-dwelling elderly Japanese women with sarcopenic obesity: a randomized controlled trial. J Am Med Dir Assoc. 2016;17(11):1011–1019. doi:10.1016/j.jamda.2016.06.016
   PubMed Web of Science ®Google Scholar
• Dieli-Conwright CM, Courneya KS, Demark-Wahnefried W, et al. Effects of aerobic and resistance exercise on metabolic syndrome, sarcopenic obesity, and circulating biomarkers in overweight or obese survivors of breast cancer: a randomized controlled trial. J Clin Oncol. 2018;36(9):875–883. doi:10.1200/JCO.2017.75.7526
   PubMed Web of Science ®Google Scholar
• The Human Microbiome Project Consortium. Structure, function and diversity of the healthy human microbiome. Nature. 2012;486(7402):207–214. doi:10.1038/nature11234
   PubMed Web of Science ®Google Scholar
• Guinane CM, Cotter PD. Role of the gut microbiota in health and chronic gastrointestinal disease: understanding a hidden metabolic organ. Therap Adv Gastroenterol. 2013;6(4):295–308. doi:10.1177/1756283X13482996
   PubMed Web of Science ®Google Scholar
• Picca A, Calvani R, Cesari M, et al. Biomarkers of physical frailty and sarcopenia: coming up to the place? Int J Mol Sci. 2020;21(16):5635. doi:10.3390/ijms21165635
   PubMed Web of Science ®Google Scholar
• Murphy EA, Velazquez KT, Herbert KM. Influence of high-fat diet on gut microbiota: a driving force for chronic disease risk. Curr Opin Clin Nutr Metab Care. 2015;18(5):515–520. doi:10.1097/MCO.0000000000000209
   PubMed Web of Science ®Google Scholar
• van Krimpen SJ, Jansen FAC, Ottenheim VL, et al. The effects of pro-, pre-, and synbiotics on muscle wasting, a systematic review-gut permeability as potential treatment target. Nutrients. 2021;13(4):1115. doi:10.3390/nu13041115
   PubMed Web of Science ®Google Scholar
• Ticinesi A, Nouvenne A, Cerundolo N, et al. Gut microbiota, muscle mass and function in aging: a focus on physical frailty and sarcopenia. Nutrients. 2019;11(7):1633. doi:10.3390/nu11071633
   PubMed Web of Science ®Google Scholar
• Vrieze A, Van Nood E, Holleman F, et al. Transfer of intestinal microbiota from lean donors increases insulin sensitivity in individuals with metabolic syndrome. Gastroenterology. 2012;143(4):913–6 e7. doi:10.1053/j.gastro.2012.06.031
   PubMed Web of Science ®Google Scholar
• Munukka E, Rintala A, Toivonen R, et al. Faecalibacterium prausnitzii treatment improves hepatic health and reduces adipose tissue inflammation in high-fat fed mice. ISME J. 2017;11(7):1667–1679. doi:10.1038/ismej.2017.24
   PubMed Web of Science ®Google Scholar
• Chen LH, Chang -S-S, Chang H-Y, et al. Probiotic supplementation attenuates age-related sarcopenia via the gut-muscle axis in SAMP8 mice. J Cachexia Sarcopenia Muscle. 2022;13(1):515–531. doi:10.1002/jcsm.12849
   PubMed Web of Science ®Google Scholar
• Sridharan GV, Choi K, Klemashevich C, et al. Prediction and quantification of bioactive microbiota metabolites in the mouse gut. Nat Commun. 2014;5:5492. doi:10.1038/ncomms6492
   PubMed Web of Science ®Google Scholar
• Zhang N, Jin M, Wang K, et al. Functional oligosaccharide fermentation in the gut: improving intestinal health and its determinant factors-a review. Carbohydr Polym. 2022;284:119043. doi:10.1016/j.carbpol.2021.119043
   PubMed Web of Science ®Google Scholar
• Verbeke KA, Boobis AR, Chiodini A, et al. Towards microbial fermentation metabolites as markers for health benefits of prebiotics. Nutr Res Rev. 2015;28(1):42–66. doi:10.1017/S0954422415000037
   PubMed Web of Science ®Google Scholar
• Cook SI, Sellin JH. Review article: short chain fatty acids in health and disease. Aliment Pharmacol Ther. 1998;12(6):499–507. doi:10.1046/j.1365-2036.1998.00337.x
   PubMed Web of Science ®Google Scholar
• Li M, van Esch BC, Wagenaar GTM, et al. Pro- and anti-inflammatory effects of short chain fatty acids on immune and endothelial cells. Eur J Pharmacol. 2018;831:52–59. doi:10.1016/j.ejphar.2018.05.003
   PubMed Web of Science ®Google Scholar
• Kim S, Kim J-H, Park BO, et al. Perspectives on the therapeutic potential of short-chain fatty acid receptors. BMB Rep. 2014;47(3):173–178. doi:10.5483/BMBRep.2014.47.3.272
   PubMed Web of Science ®Google Scholar
• McLoughlin RF, Berthon BS, Jensen ME, et al. Short-chain fatty acids, prebiotics, synbiotics, and systemic inflammation: a systematic review and meta-analysis. Am J Clin Nutr. 2017;106(3):930–945. doi:10.3945/ajcn.117.156265
   PubMed Web of Science ®Google Scholar
• den Besten G, Bleeker A, Gerding A, et al. Short-chain fatty acids protect against high-fat diet-induced obesity via a PPARgamma-dependent switch from lipogenesis to fat oxidation. Diabetes. 2015;64(7):2398–2408. doi:10.2337/db14-1213
   PubMed Web of Science ®Google Scholar
• Gao Z, Yin J, Zhang J, et al. Butyrate improves insulin sensitivity and increases energy expenditure in mice. Diabetes. 2009;58(7):1509–1517. doi:10.2337/db08-1637
   PubMed Web of Science ®Google Scholar
• Maruta H, Yoshimura Y, Araki A, et al. Activation of AMP-activated protein kinase and stimulation of energy metabolism by acetic acid in L6 myotube cells. PLoS One. 2016;11(6):e0158055. doi:10.1371/journal.pone.0158055
   PubMed Web of Science ®Google Scholar
• Wang H, Listrat A, Meunier B, et al. Apoptosis in capillary endothelial cells in ageing skeletal muscle. Aging Cell. 2014;13(2):254–262. doi:10.1111/acel.12169
   PubMed Web of Science ®Google Scholar
• Chen W, Chen Y, Liu Y, et al. Autophagy in muscle regeneration: potential therapies for myopathies. J Cachexia Sarcopenia Muscle. 2022;13:1673–1685. doi:10.1002/jcsm.13000
   PubMed Web of Science ®Google Scholar
• Arsic N, Zacchigna S, Zentilin L, et al. Vascular endothelial growth factor stimulates skeletal muscle regeneration in vivo. Mol Ther. 2004;10(5):844–854. doi:10.1016/j.ymthe.2004.08.007
   PubMed Web of Science ®Google Scholar
• Das A, Huang GX, Bonkowski MS, et al. Impairment of an endothelial NAD(+)-H2S signaling network is a reversible cause of vascular aging. Cell. 2018;173(1):74–89 e20. doi:10.1016/j.cell.2018.02.008
   PubMed Web of Science ®Google Scholar
• Jeong IH, Bae W-Y, Choi J-S, et al. Ischemia induces autophagy of endothelial cells and stimulates angiogenic effects in a hindlimb ischemia mouse model. Cell Death Dis. 2020;11(8):624. doi:10.1038/s41419-020-02849-4
   PubMed Web of Science ®Google Scholar
• Nederveen JP, Joanisse S, Snijders T, et al. Skeletal muscle satellite cells are located at a closer proximity to capillaries in healthy young compared with older men. J Cachexia Sarcopenia Muscle. 2016;7(5):547–554. doi:10.1002/jcsm.12105
   PubMed Web of Science ®Google Scholar
• Christov C, Chrétien F, Abou-Khalil R, et al. Muscle satellite cells and endothelial cells: close neighbors and privileged partners. Mol Biol Cell. 2007;18(4):1397–1409. doi:10.1091/mbc.e06-08-0693
   PubMed Web of Science ®Google Scholar
• Silva BSA, Uzeloto JS, Lira FS, et al. Exercise as a peripheral circadian clock resynchronizer in vascular and skeletal muscle aging. Int J Environ Res Public Health. 2021;18(24):12949. doi:10.3390/ijerph182412949
   PubMed Web of Science ®Google Scholar
• Zhao MM, Xu M-J, Cai Y, et al. Mitochondrial reactive oxygen species promote p65 nuclear translocation mediating high-phosphate-induced vascular calcification in vitro and in vivo. Kidney Int. 2011;79(10):1071–1079. doi:10.1038/ki.2011.18
   PubMed Web of Science ®Google Scholar
• Wu W, Xu H, Wang Z, et al. PINK1-parkin-mediated mitophagy protects mitochondrial integrity and prevents metabolic stress-induced endothelial injury. PLoS One. 2015;10(7):e0132499. doi:10.1371/journal.pone.0132499
   PubMed Web of Science ®Google Scholar
• Settembre C, Di malta C, Polito VA, et al. TFEB links autophagy to lysosomal biogenesis. Science. 2011;332(6036):1429–1433. doi:10.1126/science.1204592
   PubMed Web of Science ®Google Scholar
• Duncan ER, Crossey PA, Walker S, et al. Effect of endothelium-specific insulin resistance on endothelial function in vivo. Diabetes. 2008;57(12):3307–3314. doi:10.2337/db07-1111
   PubMed Web of Science ®Google Scholar
• Kubota T, Kubota N, Kumagai H, et al. Impaired insulin signaling in endothelial cells reduces insulin-induced glucose uptake by skeletal muscle. Cell Metab. 2011;13(3):294–307. doi:10.1016/j.cmet.2011.01.018
   PubMed Web of Science ®Google Scholar
• Hou YC, Lu C-L, Zheng C-M, et al. The role of vitamin D in modulating mesenchymal stem cells and endothelial progenitor cells for vascular calcification. Int J Mol Sci. 2020;21(7):2466. doi:10.3390/ijms21072466
   PubMed Web of Science ®Google Scholar
• Zhang J, Shan Y, Li Y, et al. Palmitate impairs angiogenesis via suppression of cathepsin activity. Mol Med Rep. 2017;15(6):3644–3650. doi:10.3892/mmr.2017.6463
   PubMed Web of Science ®Google Scholar
• Yuan L, Mao Y, Luo W, et al. Palmitic acid dysregulates the Hippo-YAP pathway and inhibits angiogenesis by inducing mitochondrial damage and activating the cytosolic DNA sensor cGAS-STING-IRF3 signaling mechanism. J Biol Chem. 2017;292(36):15002–15015. doi:10.1074/jbc.M117.804005
   PubMed Web of Science ®Google Scholar
• Liu T, Wang X, Guo F, et al. Lysophosphatidylcholine induces apoptosis and inflammatory damage in brain microvascular endothelial cells via GPR4-mediated NLRP3 inflammasome activation. Toxicol In Vitro. 2021;77:105227. doi:10.1016/j.tiv.2021.105227
   PubMedGoogle Scholar
• Ouchi N, Kobayashi H, Kihara S, et al. Adiponectin stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signaling in endothelial cells. J Biol Chem. 2004;279(2):1304–1309. doi:10.1074/jbc.M310389200
   PubMed Web of Science ®Google Scholar
• Jiang T, Liu T, Deng X, et al. Adiponectin ameliorates lung ischemia-reperfusion injury through SIRT1-PINK1 signaling-mediated mitophagy in type 2 diabetic rats. Respir Res. 2021;22(1):258. doi:10.1186/s12931-021-01855-0
   PubMed Web of Science ®Google Scholar
• Li M, van Esch BC, Henricks PAJ, et al. The anti-inflammatory effects of short chain fatty acids on lipopolysaccharide- or tumor necrosis factor alpha-stimulated endothelial cells via activation of GPR41/43 and inhibition of HDACs. Front Pharmacol. 2018;9:533. doi:10.3389/fphar.2018.00533
   PubMed Web of Science ®Google Scholar
• Herzig S, Shaw RJ. AMPK: guardian of metabolism and mitochondrial homeostasis. Nat Rev Mol Cell Biol. 2018;19(2):121–135. doi:10.1038/nrm.2017.95
   PubMed Web of Science ®Google Scholar
• Zhang B, Pan C, Feng C, et al. Role of mitochondrial reactive oxygen species in homeostasis regulation. Redox Rep. 2022;27(1):45–52. doi:10.1080/13510002.2022.2046423
   PubMed Web of Science ®Google Scholar
• Suda T, Takubo K, Semenza GL. Metabolic regulation of hematopoietic stem cells in the hypoxic niche. Cell Stem Cell. 2011;9(4):298–310. doi:10.1016/j.stem.2011.09.010
   PubMed Web of Science ®Google Scholar
• Smith C, Woessner MN, Sim M, et al. Sarcopenia definition: does it really matter? Implications for resistance training. Ageing Res Rev. 2022;78:101617. doi:10.1016/j.arr.2022.101617
   PubMed Web of Science ®Google Scholar
• Bao W, Sun Y, Zhang T, et al. Exercise programs for muscle mass, muscle strength and physical performance in older adults with sarcopenia: a systematic review and meta-analysis. Aging Dis. 2020;11(4):863–873. doi:10.14336/AD.2019.1012
   PubMed Web of Science ®Google Scholar
• Harper C, Gopalan V, Goh J, et al. Exercise rescues mitochondrial coupling in aged skeletal muscle: a comparison of different modalities in preventing sarcopenia. J Transl Med. 2021;19(1):71. doi:10.1186/s12967-021-02737-1
   PubMed Web of Science ®Google Scholar
• Denison HJ, Cooper C, Sayer AA, et al. Prevention and optimal management of sarcopenia: a review of combined exercise and nutrition interventions to improve muscle outcomes in older people. Clin Interv Aging. 2015;10:859–869. doi:10.2147/CIA.S55842
   PubMed Web of Science ®Google Scholar