Egerman MA, Glass DJ. Signaling pathways controlling skeletal muscle mass. Crit Rev Biochem Mol Biol. 2014;49:59–68.
Pollock ML, Franklin BA, Balady GJ, Chaitman BL, Fleg JL, Fletcher B, Limacher M, Pina IL, Stein RA, Williams M, AHA Science Advisory, et al. Resistance exercise in individuals with and without cardiovascular disease: benefits, rationale, safety, and prescription: An advisory from the Committee on Exercise, Rehabilitation, and Prevention, Council on Clinical Cardiology, American Heart Association; Position paper endorsed by the American College of Sports Medicine. Circulation. 2000;101:828–33.
Tisdale MJ. Wasting in cancer. J Nutr. 1999;129:243S–6S.
Smerdu V, Karsch-Mizrachi I, Campione M, Leinwand L, Schiaffino S. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. Am J Physiol. 1994;267:C1723–8.
Chemello F, Bean C, Cancellara P, Laveder P, Reggiani C, Lanfranchi G. Microgenomic analysis in skeletal muscle: expression signatures of individual fast and slow myofibers. PLoS ONE. 2011;6, e16807.
Alway SE, MacDougall JD, Sale DG, Sutton JR, McComas AJ. Functional and structural adaptations in skeletal muscle of trained athletes. J Appl Physiol. 1988;64:1114–20.
Larsson L. Histochemical characteristics of human skeletal muscle during aging. Acta Physiol Scand. 1983;117:469–71.
Tosi C, Jerusalem F. Selective muscle fiber type anomalies in neuromusclar disorders. An analysis of 124 consecutive muscle biopsies (author’s transl). J Neurol. 1976;214:13–34.
Koutakis P, Weiss DJ, Miserlis D, Shostrom VK, Papoutsi E, Ha DM, Carpenter LA, McComb RD, Casale GP, Pipinos II. Oxidative damage in the gastrocnemius of patients with peripheral artery disease is myofiber type selective. Redox Biol. 2014;2:921–8.
Engel WK. Selective and nonselective susceptibility of muscle fiber types. A new approach to human neuromuscular diseases. Arch Neurol. 1970;22:97–117.
Gutmann L, Blumenthal D, Gutmann L, Schochet SS. Acute type II myofiber atrophy in critical illness. Neurology. 1996;46:819–21.
Webster C, Silberstein L, Hays AP, Blau HM. Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy. Cell. 1988;52:503–13.
Lillioja S, Young AA, Culter CL, Ivy JL, Abbott WG, Zawadzki JK, Yki-Jarvinen H, Christin L, Secomb TW, Bogardus C. Skeletal muscle capillary density and fiber type are possible determinants of in vivo insulin resistance in man. J Clin Invest. 1987;80:415–24.
Meng ZX, Wang L, Xiao Y, Lin JD. The Baf60c/Deptor pathway links skeletal muscle inflammation to glucose homeostasis in obesity. Diabetes. 2014;63:1533–45.
Izumiya Y, Hopkins T, Morris C, Sato K, Zeng L, Viereck J, Hamilton JA, Ouchi N, LeBrasseur NK, Walsh K. Fast/Glycolytic muscle fiber growth reduces fat mass and improves metabolic parameters in obese mice. Cell Metab. 2008;7:159–72.
Fujio Y, Guo K, Mano T, Mitsuuchi Y, Testa JR, Walsh K. Cell cycle withdrawal promotes myogenic induction of Akt, a positive modulator of myocyte survival. Mol Cell Biol. 1999;19:5073–82.
Rommel C, Bodine SC, Clarke BA, Rossman R, Nunez L, Stitt TN, Yancopoulos GD, Glass DJ. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI (3) K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol. 2001;3:1009–13.
LeBrasseur NK, Walsh K, Arany Z. Metabolic benefits of resistance training and fast glycolytic skeletal muscle. Am J Physiol Endocrinol Metab. 2011;300:E3–E10.
Sandri M, Sandri C, Gilbert A, Skurk C, Calabria E, Picard A, Walsh K, Schiaffino S, Lecker SH, Goldberg AL. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell. 2004;117:399–412.
Akasaki Y, Ouchi N, Izumiya Y, Bernardo BL, Lebrasseur NK, Walsh K. Glycolytic fast-twitch muscle fiber restoration counters adverse age-related changes in body composition and metabolism. Aging Cell. 2014;13:80–91.
Hanatani S, Izumiya Y, Araki S, Rokutanda T, Kimura Y, Walsh K, Ogawa H. Akt1-mediated fast/glycolytic skeletal muscle growth attenuates renal damage in experimental kidney disease. J Am Soc Nephrol. 2014;25:2800–11.
Araki S, Izumiya Y, Hanatani S, Rokutanda T, Usuku H, Akasaki Y, Takeo T, Nakagata N, Walsh K, Ogawa H. Akt1-mediated skeletal muscle growth attenuates cardiac dysfunction and remodeling after experimental myocardial infarction. Circ Heart Fail. 2012;5:116–25.
Kim MH, Kay DI, Rudra RT, Chen BM, Hsu N, Izumiya Y, Martinez L, Spencer MJ, Walsh K, Grinnell AD, et al. Myogenic Akt signaling attenuates muscular degeneration, promotes myofiber regeneration and improves muscle function in dystrophin-deficient mdx mice. Hum Mol Genet. 2011;20:1324–38.
Peter AK, Ko CY, Kim MH, Hsu N, Ouchi N, Rhie S, Izumiya Y, Zeng L, Walsh K, Crosbie RH. Myogenic Akt signaling upregulates the utrophin-glycoprotein complex and promotes sarcolemma stability in muscular dystrophy. Hum Mol Genet. 2009;18:318–27.
Walsh K. Adipokines, myokines and cardiovascular disease. Circ J. 2009;73:13–8.
Pedersen BK. Muscles and their myokines. J Exp Biol. 2011;214:337–46.
Catoire M, Kersten S. The search for exercise factors in humans. FASEB J. 2015;29:1615–28.
Besse-Patin A, Montastier E, Vinel C, Castan-Laurell I, Louche K, Dray C, Daviaud D, Mir L, Marques MA, Thalamas C, et al. Effect of endurance training on skeletal muscle myokine expression in obese men: identification of apelin as a novel myokine. Int J Obes (Lond). 2014;38:707–13.
Raschke S, Eckardt K, Bjorklund Holven K, Jensen J, Eckel J. Identification and validation of novel contraction-regulated myokines released from primary human skeletal muscle cells. PLoS ONE. 2013;8, e62008.
Deshmukh AS, Cox J, Jensen LJ, Meissner F, Mann M. Secretome Analysis of Lipid-Induced Insulin Resistance in Skeletal Muscle Cells by a Combined Experimental and Bioinformatics Workflow. J Proteome Res. 2015;14:4885–95.
Grill MA, Bales MA, Fought AN, Rosburg KC, Munger SJ, Antin PB. Tetracycline-inducible system for regulation of skeletal muscle-specific gene expression in transgenic mice. Transgenic Res. 2003;12:33–43.
Shiojima I, Sato K, Izumiya Y, Schiekofer S, Ito M, Liao R, Colucci WS, Walsh K. Disruption of coordinated cardiac hypertrophy and angiogenesis contributes to the transition to heart failure. J Clin Invest. 2005;115:2108–18.
Li B, Dewey CN. RSEM: accurate transcript quantification from RNA-Seq data with or without a reference genome. BMC Bioinformatics. 2011;12:323.
Yuan M, Breitkopf SB, Yang X, Asara JM. A positive/negative ion-switching, targeted mass spectrometry-based metabolomics platform for bodily fluids, cells, and fresh and fixed tissue. Nat Protoc. 2012;7:872–81.
Horton P, Park KJ, Obayashi T, Fujita N, Harada H, Adams-Collier CJ, Nakai K. WoLF PSORT: protein localization predictor. Nucleic Acids Res. 2007;35:W585–7.
Park S, Brisson BK, Liu M, Spinazzola JM, Barton ER. Mature IGF-I excels in promoting functional muscle recovery from disuse atrophy compared with pro-IGF-IA. J Appl Physiol. 2014;116:797–806.
Gorgens SW, Raschke S, Holven KB, Jensen J, Eckardt K, Eckel J. Regulation of follistatin-like protein 1 expression and secretion in primary human skeletal muscle cells. Arch Physiol Biochem. 2013;119:75–80.
Rao RR, Long JZ, White JP, Svensson KJ, Lou J, Lokurkar I, Jedrychowski MP, Ruas JL, Wrann CD, Lo JC, et al. Meteorin-like is a hormone that regulates immune-adipose interactions to increase beige fat thermogenesis. Cell. 2014;157:1279–91.
Matthews VB, Astrom MB, Chan MH, Bruce CR, Krabbe KS, Prelovsek O, Akerstrom T, Yfanti C, Broholm C, Mortensen OH, et al. Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase. Diabetologia. 2009;52:1409–18.
Zanuso S, Jimenez A, Pugliese G, Corigliano G, Balducci S. Exercise for the management of type 2 diabetes: a review of the evidence. Acta Diabetol. 2010;47:15–22.
Bodine SC, Stitt TN, Gonzalez M, Kline WO, Stover GL, Bauerlein R, Zlotchenko E, Scrimgeour A, Lawrence JC, Glass DJ, et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol. 2001;3:1014–9.
Lane AN, Fan TW. Regulation of mammalian nucleotide metabolism and biosynthesis. Nucleic Acids Res. 2015;43:2466–85.
Wagle A, Jivraj S, Garlock GL, Stapleton SR. Insulin regulation of glucose-6-phosphate dehydrogenase gene expression is rapamycin-sensitive and requires phosphatidylinositol 3-kinase. J Biol Chem. 1998;273:14968–74.
Wagner KR, Kauffman FC, Max SR. The pentose phosphate pathway in regenerating skeletal muscle. Biochem J. 1978;170:17–22.
Nair KS, Schwartz RG, Welle S. Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. Am J Physiol. 1992;263:E928–34.
Blomstrand E, Saltin B. BCAA intake affects protein metabolism in muscle after but not during exercise in humans. Am J Physiol Endocrinol Metab. 2001;281:E365–74.
Chaillou T, Lee JD, England JH, Esser KA, McCarthy JJ. Time course of gene expression during mouse skeletal muscle hypertrophy. J Appl Physiol. 2013;115:1065–74.
Jang C, Oh SF, Wada S, Rowe GC, Liu L, Chan MC, Rhee J, Hoshino A, Kim B, Ibrahim A, et al. A branched-chain amino acid metabolite drives vascular fatty acid transport and causes insulin resistance. Nat Med. 2016;22:421–6.
Petrella JK, Kim JS, Mayhew DL, Cross JM, Bamman MM. Potent myofiber hypertrophy during resistance training in humans is associated with satellite cell-mediated myonuclear addition: a cluster analysis. J Appl Physiol. 2008;104:1736–42.
Kadi F, Schjerling P, Andersen LL, Charifi N, Madsen JL, Christensen LR, Andersen JL. The effects of heavy resistance training and detraining on satellite cells in human skeletal muscles. J Physiol. 2004;558:1005–12.
Kadi F, Thornell LE. Concomitant increases in myonuclear and satellite cell content in female trapezius muscle following strength training. Histochem Cell Biol. 2000;113:99–103.
Rodgers JT, King KY, Brett JO, Cromie MJ, Charville GW, Maguire KK, Brunson C, Mastey N, Liu L, Tsai CR, et al. mTORC1 controls the adaptive transition of quiescent stem cells from G0 to G (Alert). Nature. 2014;510:393–6.
Zhang P, Liang X, Shan T, Jiang Q, Deng C, Zheng R, Kuang S. mTOR is necessary for proper satellite cell activity and skeletal muscle regeneration. Biochem Biophys Res Commun. 2015;463:102–8.
Cao Y, Yao Z, Sarkar D, Lawrence M, Sanchez GJ, Parker MH, MacQuarrie KL, Davison J, Morgan MT, Ruzzo WL, et al. Genome-wide MyoD binding in skeletal muscle cells: a potential for broad cellular reprogramming. Dev Cell. 2010;18:662–74.
Wilson EM, Rotwein P. Selective control of skeletal muscle differentiation by Akt1. J Biol Chem. 2007;282:5106–10.
Bernard K, Logsdon NJ, Ravi S, Xie N, Persons BP, Rangarajan S, Zmijewski JW, Mitra K, Liu G, Darley-Usmar VM, et al. Metabolic Reprogramming Is Required for Myofibroblast Contractility and Differentiation. J Biol Chem. 2015;290:25427–38.
Taegtmeyer H, Sen S, Vela D. Return to the fetal gene program: a suggested metabolic link to gene expression in the heart. Ann N Y Acad Sci. 2010;1188:191–8.
Ryall JG, Dell’Orso S, Derfoul A, Juan A, Zare H, Feng X, Clermont D, Koulnis M, Gutierrez-Cruz G, Fulco M, et al. The NAD (+)-dependent SIRT1 deacetylase translates a metabolic switch into regulatory epigenetics in skeletal muscle stem cells. Cell Stem Cell. 2015;16:171–83.
Fukada S, Uezumi A, Ikemoto M, Masuda S, Segawa M, Tanimura N, Yamamoto H, Miyagoe-Suzuki Y, Takeda S. Molecular signature of quiescent satellite cells in adult skeletal muscle. Stem Cells. 2007;25:2448–59.
Fulco M, Cen Y, Zhao P, Hoffman EP, McBurney MW, Sauve AA, Sartorelli V. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev Cell. 2008;14:661–73.
Blaauw B, Canato M, Agatea L, Toniolo L, Mammucari C, Masiero E, Abraham R, Sandri M, Schiaffino S, Reggiani C. Inducible activation of Akt increases skeletal muscle mass and force without satellite cell activation. FASEB J. 2009;23:3896–905.
Mason S, Wadley GD. Skeletal muscle reactive oxygen species: a target of good cop/bad cop for exercise and disease. Redox Rep. 2014;19:97–106.
Mahadev K, Zilbering A, Zhu L, Goldstein BJ. Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J Biol Chem. 2001;276:21938–42.
Loh K, Deng H, Fukushima A, Cai X, Boivin B, Galic S, Bruce C, Shields BJ, Skiba B, Ooms LM, et al. Reactive oxygen species enhance insulin sensitivity. Cell Metab. 2009;10:260–72.
Tidball JG, Wehling-Henricks M. Macrophages promote muscle membrane repair and muscle fibre growth and regeneration during modified muscle loading in mice in vivo. J Physiol. 2007;578:327–36.
Arnold L, Henry A, Poron F, Baba-Amer Y, Van Rooijen N, Plonquet A, Gherardi RK, Chazaud B. Inflammatory monocytes recruited after skeletal muscle injury switch into antiinflammatory macrophages to support myogenesis. J Exp Med. 2007;204:1057–69.
Barton-Davis ER, Shoturma DI, Sweeney HL. Contribution of satellite cells to IGF-I induced hypertrophy of skeletal muscle. Acta Physiol Scand. 1999;167:301–5.
Carroll PV, Christ ER, Umpleby AM, Gowrie I, Jackson N, Bowes SB, Hovorka R, Croos P, Sonksen PH, Russell-Jones DL. IGF-I treatment in adults with type 1 diabetes: effects on glucose and protein metabolism in the fasting state and during a hyperinsulinemic-euglycemic amino acid clamp. Diabetes. 2000;49:789–96.
Cusi K, DeFronzo R. Recombinant human insulin-like growth factor I treatment for 1 week improves metabolic control in type 2 diabetes by ameliorating hepatic and muscle insulin resistance. J Clin Endocrinol Metab. 2000;85:3077–84.
Broholm C, Laye MJ, Brandt C, Vadalasetty R, Pilegaard H, Pedersen BK, Scheele C. LIF is a contraction-induced myokine stimulating human myocyte proliferation. J Appl Physiol. 2011;111:251–9.
Brandt N, O’Neill HM, Kleinert M, Schjerling P, Vernet E, Steinberg GR, Richter EA, Jorgensen SB. Leukemia inhibitory factor increases glucose uptake in mouse skeletal muscle. Am J Physiol Endocrinol Metab. 2015;309:E142–53.
Spangenburg EE, Booth FW. Leukemia inhibitory factor restores the hypertrophic response to increased loading in the LIF (-/-) mouse. Cytokine. 2006;34:125–30.
Schiaffino S, Dyar KA, Ciciliot S, Blaauw B, Sandri M. Mechanisms regulating skeletal muscle growth and atrophy. FEBS J. 2013;280:4294–314.
Raue U, Slivka D, Jemiolo B, Hollon C, Trappe S. Myogenic gene expression at rest and after a bout of resistance exercise in young (18–30 yr) and old (80–89 yr) women. J Appl Physiol. 2006;101:53–9.
Kimura H, Kwan KM, Zhang Z, Deng JM, Darnay BG, Behringer RR, Nakamura T, De Crombrugghe B, Akiyama H. Cthrc1 is a positive regulator of osteoblastic bone formation. PLoS ONE. 2008;3, e3174.
Stohn JP, Perreault NG, Wang Q, Liaw L, Lindner V. Cthrc1, a novel circulating hormone regulating metabolism. PLoS ONE. 2012;7, e47142.
Stohn JP, Wang Q, Siviski ME, Kennedy K, Jin YR, Kacer D, DeMambro V, Liaw L, Vary CP, Rosen CJ, et al. Cthrc1 controls adipose tissue formation, body composition, and physical activity. Obesity (Silver Spring). 2015;23:1633–42.
Xu T, Bianco P, Fisher LW, Longenecker G, Smith E, Goldstein S, Bonadio J, Boskey A, Heegaard AM, Sommer B, et al. Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice. Nat Genet. 1998;20:78–82.
Myren M, Kirby DJ, Noonan ML, Maeda A, Owens RT, Ricard-Blum S, Kram V, Kilts TM, Young MF. Biglycan potentially regulates angiogenesis during fracture repair by altering expression and function of endostatin. Matrix Biol. 2016;52-54:141–50.
Lechner BE, Lim JH, Mercado ML, Fallon JR. Developmental regulation of biglycan expression in muscle and tendon. Muscle Nerve. 2006;34:347–55.
Grandoch M, Kohlmorgen C, Melchior-Becker A, Feldmann K, Homann S, Muller J, Kiene LS, Zeng-Brouwers J, Schmitz F, Nagy N, et al. Loss of Biglycan Enhances Thrombin Generation in Apolipoprotein E-Deficient Mice: Implications for Inflammation and Atherosclerosis. Arterioscler Thromb Vasc Biol. 2016;36:e41–50.
Izumiya Y, Bina HA, Ouchi N, Akasaki Y, Kharitonenkov A, Walsh K. FGF21 is an Akt-regulated myokine. FEBS Lett. 2008;582:3805–10.
Kharitonenkov A, DiMarchi R. FGF21 Revolutions: Recent Advances Illuminating FGF21 Biology and Medicinal Properties. Trends in endocrinology and metabolism: TEM. 2015;26:608–17.
Lee P, Linderman JD, Smith S, Brychta RJ, Wang J, Idelson C, Perron RM, Werner CD, Phan GQ, Kammula US, et al. Irisin and FGF21 are cold-induced endocrine activators of brown fat function in humans. Cell Metab. 2014;19:302–9.
Schlein C, Talukdar S, Heine M, Fischer AW, Krott LM, Nilsson SK, Brenner MB, Heeren J, Scheja L. FGF21 Lowers Plasma Triglycerides by Accelerating Lipoprotein Catabolism in White and Brown Adipose Tissues. Cell Metab. 2016;23:441–53.
Planavila A, Redondo I, Hondares E, Vinciguerra M, Munts C, Iglesias R, Gabrielli LA, Sitges M, Giralt M, Van Bilsen M, et al. Fibroblast growth factor 21 protects against cardiac hypertrophy in mice. Nat Commun. 2013;4:2019.
Kim KH, Kim SH, Min YK, Yang HM, Lee JB, Lee MS. Acute exercise induces FGF21 expression in mice and in healthy humans. PLoS ONE. 2013;8, e63517.
Mou Z, Hyde TM, Lipska BK, Martinowich K, Wei P, Ong CJ, Hunter LA, Palaguachi GI, Morgun E, Teng R, et al. Human Obesity Associated with an Intronic SNP in the Brain-Derived Neurotrophic Factor Locus. Cell Rep. 2015;13:1073–80.
Pelleymounter MA, Cullen MJ, Wellman CL. Characteristics of BDNF-induced weight loss. Exp Neurol. 1995;131:229–38.
Rothman SM, Griffioen KJ, Wan R, Mattson MP. Brain-derived neurotrophic factor as a regulator of systemic and brain energy metabolism and cardiovascular health. Ann N Y Acad Sci. 2012;1264:49–63.
Bostrom P, Wu J, Jedrychowski MP, Korde A, Ye L, Lo JC, Rasbach KA, Bostrom EA, Choi JH, Long JZ, et al. A PGC1-alpha-dependent myokine that drives brown-fat-like development of white fat and thermogenesis. Nature. 2012;481:463–8.
Wrann CD, White JP, Salogiannnis J, Laznik-Bogoslavski D, Wu J, Ma D, Lin JD, Greenberg ME, Spiegelman BM. Exercise induces hippocampal BDNF through a PGC-1alpha/FNDC5 pathway. Cell Metab. 2013;18:649–59.
Norheim F, Raastad T, Thiede B, Rustan AC, Drevon CA, Haugen F. Proteomic identification of secreted proteins from human skeletal muscle cells and expression in response to strength training. Am J Physiol Endocrinol Metab. 2011;301:E1013–21.
Oshima Y, Ouchi N, Sato K, Izumiya Y, Pimentel DR, Walsh K. Follistatin-like 1 is an Akt-regulated cardioprotective factor that is secreted by the heart. Circulation. 2008;117:3099–108.
Gruppo Italiano per lo Studio della Sopravvivenza nell’Infarto Miocardico. GISSI-2: a factorial randomised trial of alteplase versus streptokinase and heparin versus no heparin among 12,490 patients with acute myocardial infarction. Lancet. 1990;336:65–71.
Kupchak BR, Creighton BC, Aristizabal JC, Dunn-Lewis C, Volk BM, Ballard KD, Comstock BA, Maresh CM, Kraemer WJ, Volek JS. Beneficial effects of habitual resistance exercise training on coagulation and fibrinolytic responses. Thromb Res. 2013;131:e227–34.
Festoff BW, Hantai D, Soria J, Thomaidis A, Soria C. Plasminogen activator in mammalian skeletal muscle: characteristics of effect of denervation on urokinase-like and tissue activator. J Cell Biol. 1986;103:1415–21.