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Home / Equine Research Bank / Br J Nutr / Characterisation of equine satellite cell transcriptomic pro...
The British journal of nutrition2016; 116(8); 1315-1325; doi: 10.1017/S000711451600324X

Characterisation of equine satellite cell transcriptomic profile response to β-hydroxy-β-methylbutyrate (HMB).

Abstract: β-Hydroxy-β-methylbutyrate (HMB) is a popular ergogenic aid used by human athletes and as a supplement to sport horses, because of its ability to aid muscle recovery, improve performance and body composition. Recent findings suggest that HMB may stimulate satellite cells and affect expressions of genes regulating skeletal muscle cell growth. Despite the scientific data showing benefits of HMB supplementation in horses, no previous study has explained the mechanism of action of HMB in this species. The aim of this study was to reveal the molecular background of HMB action on equine skeletal muscle by investigating the transcriptomic profile changes induced by HMB in equine satellite cells in vitro. Upon isolation from the semitendinosus muscle, equine satellite cells were cultured until the 2nd day of differentiation. Differentiating cells were incubated with HMB for 24 h. Total cellular RNA was isolated, amplified, labelled and hybridised to microarray slides. Microarray data validation was performed with real-time quantitative PCR. HMB induced differential expressions of 361 genes. Functional analysis revealed that the main biological processes influenced by HMB in equine satellite cells were related to muscle organ development, protein metabolism, energy homoeostasis and lipid metabolism. In conclusion, this study demonstrated for the first time that HMB has the potential to influence equine satellite cells by controlling global gene expression. Genes and biological processes targeted by HMB in equine satellite cells may support HMB utility in improving growth and regeneration of equine skeletal muscle; however, the overall role of HMB in horses remains equivocal and requires further proteomic, biochemical and pharmacokinetic studies.
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Publication Date: 2016-10-03 PubMed ID: 27691998PubMed Central: PMC5082287DOI: 10.1017/S000711451600324XGoogle Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigated how the popular athletic supplement β-Hydroxy-β-methylbutyrate (HMB) influences gene expression in horse muscle cells, with results offering insights into its potential to improve muscle growth and recovery in horses.

Objective of the Study

The aim of this study was to understand the molecular mechanism of HMB’s action on equine skeletal muscle. The researchers were particularly interested in studying the changes in the transcriptomic profile caused by HMB in horse muscle cells. Prior to this research, the mechanism of HMB action on horse muscles had not been investigated.

Research Methodology

  • The researchers isolated satellite cells (a type of muscle stem cell) from the semitendinosus muscle of horses.
  • The isolated cells were then cultured until the 2nd day of differentiation, a process where the satellite cells change into specialized muscle cells. On this day, the cells were treated with HMB for 24 hours.
  • After the treatment, total cellular RNA was isolated from the cells. This RNA was amplified, labelled, and hybridised to microarray slides, which enables the study of gene expression on a large scale.
  • The microarray data was validated with real-time quantitative PCR, a laboratory technique used to amplify and simultaneously quantify a targeted DNA molecule.

Results and Findings

The researchers found that HMB exposure led to differential expression of 361 genes. The primary biological processes affected by HMB in equine satellite cells were related to muscle organ development, protein metabolism, energy homeostasis, and lipid metabolism.

Conclusions and Implications

The study demonstrated, for the first time, that HMB can influence equine satellite cells by controlling global gene expression – altering how genes are selectively converted into functional protein molecules. The genes and biological processes targeted by HMB in horse muscle cells could potentially enhance the growth and regeneration of horse skeletal muscle. However, the study concludes that further research, including proteomic, biochemical and pharmacokinetic studies, is necessary to fully understand HMB’s role in horses.

Cite This Article

APA
Szcześniak KA, Ciecierska A, Ostaszewski P, Sadkowski T. (2016). Characterisation of equine satellite cell transcriptomic profile response to β-hydroxy-β-methylbutyrate (HMB). Br J Nutr, 116(8), 1315-1325. https://doi.org/10.1017/S000711451600324X

Publication

The British journal of nutrition
ISSN: 1475-2662
NlmUniqueID: 0372547
Country: England
Language: English
Volume: 116
Issue: 8
Pages: 1315-1325

Researcher Affiliations

Szcześniak, Katarzyna A
  • Department of Physiological Sciences, Faculty of Veterinary Medicine,Warsaw University of Life Science - SGGW,Nowoursynowska 159, 02-776 Warsaw,Poland.
Ciecierska, Anna
  • Department of Physiological Sciences, Faculty of Veterinary Medicine,Warsaw University of Life Science - SGGW,Nowoursynowska 159, 02-776 Warsaw,Poland.
Ostaszewski, Piotr
  • Department of Physiological Sciences, Faculty of Veterinary Medicine,Warsaw University of Life Science - SGGW,Nowoursynowska 159, 02-776 Warsaw,Poland.
Sadkowski, Tomasz
  • Department of Physiological Sciences, Faculty of Veterinary Medicine,Warsaw University of Life Science - SGGW,Nowoursynowska 159, 02-776 Warsaw,Poland.

MeSH Terms

  • Animals
  • Apoptosis
  • Cell Differentiation
  • Cell Proliferation
  • Cells, Cultured
  • Dietary Supplements
  • Energy Metabolism
  • Gene Expression Profiling
  • Gene Expression Regulation, Developmental
  • Gene Ontology
  • Hamstring Muscles / cytology
  • Hamstring Muscles / growth & development
  • Hamstring Muscles / metabolism
  • Horses
  • Male
  • Muscle Development
  • Muscle Proteins / genetics
  • Muscle Proteins / metabolism
  • Performance-Enhancing Substances / metabolism
  • RNA, Messenger / metabolism
  • Satellite Cells, Skeletal Muscle / cytology
  • Satellite Cells, Skeletal Muscle / metabolism
  • Transcriptome
  • Valerates / metabolism

References

This article includes 63 references
  1. Waller AP, Lindinger MI. Nutritional aspects of post exercise skeletal muscle glycogen synthesis in horses: a comparative review.. Equine Vet J 2010 Apr;42(3):274-81.
    pubmed: 20486986doi: 10.2746/042516409x479603google scholar: lookup
  2. Harris PA, Harris RC. Ergogenic potential of nutritional strategies and substances in the horse. Livest Prod Sci 2005;92:147–165.
  3. Wilson JM, Fitschen PJ, Campbell B, Wilson GJ, Zanchi N, Taylor L, Wilborn C, Kalman DS, Stout JR, Hoffman JR, Ziegenfuss TN, Lopez HL, Kreider RB, Smith-Ryan AE, Antonio J. International Society of Sports Nutrition Position Stand: beta-hydroxy-beta-methylbutyrate (HMB).. J Int Soc Sports Nutr 2013 Feb 2;10(1):6.
    pmc: PMC3568064pubmed: 23374455doi: 10.1186/1550-2783-10-6google scholar: lookup
  4. Szcześniak KA, Ostaszewski P, Fuller JC Jr, Ciecierska A, Sadkowski T. Dietary supplementation of β-hydroxy-β-methylbutyrate in animals - a review.. J Anim Physiol Anim Nutr (Berl) 2015 Jun;99(3):405-17.
    pubmed: 25099672doi: 10.1111/jpn.12234google scholar: lookup
  5. Ostaszewski P, Kostiuk S, Balasinska B. The leucine metabolite 3-hydroxy-3-methylbutyrate (HMB) modifies protein turnover in muscles of laboratory rats and domestic chickens in vitro. J Anim Physiol Anim Nutr 2000;84:1–8.
  6. Smith HJ, Mukerji P, Tisdale MJ. Attenuation of proteasome-induced proteolysis in skeletal muscle by {beta}-hydroxy-{beta}-methylbutyrate in cancer-induced muscle loss.. Cancer Res 2005 Jan 1;65(1):277-83.
    pubmed: 15665304
  7. Nissen SL, Abumrad NN. Nutritional role of the leucine metabolite bhydroxy-b-methylbutyrate (HMB). J Nutr Biochem 1997;8:300–311.
  8. Kornasio R, Riederer I, Butler-Browne G, Mouly V, Uni Z, Halevy O. Beta-hydroxy-beta-methylbutyrate (HMB) stimulates myogenic cell proliferation, differentiation and survival via the MAPK/ERK and PI3K/Akt pathways.. Biochim Biophys Acta 2009 May;1793(5):755-63.
    pubmed: 19211028doi: 10.1016/j.bbamcr.2008.12.017google scholar: lookup
  9. Tatara MR. Neonatal programming of skeletal development in sheep is mediated by somatotrophic axis function.. Exp Physiol 2008 Jun;93(6):763-72.
    pubmed: 18263656doi: 10.1113/expphysiol.2007.041145google scholar: lookup
  10. Fernyhough ME, Helterline Dl, Vierck Jl. Myogenic satellite cell proliferative and differentiative responses to components of common oral ergogenic supplements. Res Sport Med 2004;12:161–190.
  11. Vukovich MD, Dreifort GD. Effect of beta-hydroxy beta-methylbutyrate on the onset of blood lactate accumulation and V(O)(2) peak in endurance-trained cyclists.. J Strength Cond Res 2001 Nov;15(4):491-7.
    pubmed: 11726262
  12. Bruckbauer A, Zemel MB, Thorpe T, Akula MR, Stuckey AC, Osborne D, Martin EB, Kennel S, Wall JS. Synergistic effects of leucine and resveratrol on insulin sensitivity and fat metabolism in adipocytes and mice.. Nutr Metab (Lond) 2012 Aug 22;9(1):77.
    pmc: PMC3506499pubmed: 22913271doi: 10.1186/1743-7075-9-77google scholar: lookup
  13. Ostaszewski P, Kowalska A, Szarska E. Effects of β-hydroxy-β-methylbutyrate and γ-oryzanol on blood biochemical markers in exercising thoroughbred race horses. J Equine Vet Sci 2012;32:542–551.
  14. Miller P, Sandberg L, Fuller JC Jr. The effects of supplemental β-hydroxy-β-methylbutyrate (HMB) on training and racing thoroughbreds. Assoc Equine Sports Med Proc 1998;1:23–24.
  15. MAURO A. Satellite cell of skeletal muscle fibers.. J Biophys Biochem Cytol 1961 Feb;9(2):493-5.
    pmc: PMC2225012pubmed: 13768451doi: 10.1083/jcb.9.2.493google scholar: lookup
  16. Alway SE, Pereira SL, Edens NK, Hao Y, Bennett BT. β-Hydroxy-β-methylbutyrate (HMB) enhances the proliferation of satellite cells in fast muscles of aged rats during recovery from disuse atrophy.. Exp Gerontol 2013 Sep;48(9):973-84.
    pubmed: 23832076doi: 10.1016/j.exger.2013.06.005google scholar: lookup
  17. Kao M, Columbus DA, Suryawan A, Steinhoff-Wagner J, Hernandez-Garcia A, Nguyen HV, Fiorotto ML, Davis TA. Enteral β-hydroxy-β-methylbutyrate supplementation increases protein synthesis in skeletal muscle of neonatal pigs.. Am J Physiol Endocrinol Metab 2016 Jun 1;310(11):E1072-84.
    pmc: PMC4935142pubmed: 27143558doi: 10.1152/ajpendo.00520.2015google scholar: lookup
  18. Szcześniak KA, Ciecierska A, Ostaszewski P, Sadkowski T. Transcriptomic profile adaptations following exposure of equine satellite cells to nutriactive phytochemical gamma-oryzanol.. Genes Nutr 2016;11:5.
    pmc: PMC4959553pubmed: 27482297doi: 10.1186/s12263-016-0523-5google scholar: lookup
  19. Brazma A, Hingamp P, Quackenbush J, Sherlock G, Spellman P, Stoeckert C, Aach J, Ansorge W, Ball CA, Causton HC, Gaasterland T, Glenisson P, Holstege FC, Kim IF, Markowitz V, Matese JC, Parkinson H, Robinson A, Sarkans U, Schulze-Kremer S, Stewart J, Taylor R, Vilo J, Vingron M. Minimum information about a microarray experiment (MIAME)-toward standards for microarray data.. Nat Genet 2001 Dec;29(4):365-71.
    pubmed: 11726920doi: 10.1038/ng1201-365google scholar: lookup
  20. Edgar R, Domrachev M, Lash AE. Gene Expression Omnibus: NCBI gene expression and hybridization array data repository.. Nucleic Acids Res 2002 Jan 1;30(1):207-10.
    pmc: PMC99122pubmed: 11752295doi: 10.1093/nar/30.1.207google scholar: lookup
  21. Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method.. Methods 2001 Dec;25(4):402-8.
    pubmed: 11846609doi: 10.1006/meth.2001.1262google scholar: lookup
  22. Bustin SA, Benes V, Garson JA, Hellemans J, Huggett J, Kubista M, Mueller R, Nolan T, Pfaffl MW, Shipley GL, Vandesompele J, Wittwer CT. The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments.. Clin Chem 2009 Apr;55(4):611-22.
    pubmed: 19246619doi: 10.1373/clinchem.2008.112797google scholar: lookup
  23. Huang da W, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources.. Nat Protoc 2009;4(1):44-57.
    pubmed: 19131956doi: 10.1038/nprot.2008.211google scholar: lookup
  24. Asakura A, Komaki M, Rudnicki M. Muscle satellite cells are multipotential stem cells that exhibit myogenic, osteogenic, and adipogenic differentiation.. Differentiation 2001 Oct;68(4-5):245-53.
    pubmed: 11776477doi: 10.1046/j.1432-0436.2001.680412.xgoogle scholar: lookup
  25. Sacco A, Doyonnas R, Kraft P, Vitorovic S, Blau HM. Self-renewal and expansion of single transplanted muscle stem cells.. Nature 2008 Nov 27;456(7221):502-6.
    pmc: PMC2919355pubmed: 18806774doi: 10.1038/nature07384google scholar: lookup
  26. Ono Y, Boldrin L, Knopp P, Morgan JE, Zammit PS. Muscle satellite cells are a functionally heterogeneous population in both somite-derived and branchiomeric muscles.. Dev Biol 2010 Jan 1;337(1):29-41.
    pmc: PMC2806517pubmed: 19835858doi: 10.1016/j.ydbio.2009.10.005google scholar: lookup
  27. Motohashi N, Asakura A. Muscle satellite cell heterogeneity and self-renewal.. Front Cell Dev Biol 2014;2:1.
    pmc: PMC4206996pubmed: 25364710doi: 10.3389/fcell.2014.00001google scholar: lookup
  28. Manzano R, Toivonen JM, Calvo AC, Miana-Mena FJ, Zaragoza P, Muñoz MJ, Montarras D, Osta R. Sex, fiber-type, and age dependent in vitro proliferation of mouse muscle satellite cells.. J Cell Biochem 2011 Oct;112(10):2825-36.
    pubmed: 21608019doi: 10.1002/jcb.23197google scholar: lookup
  29. Yada E, Yamanouchi K, Nishihara M. Adipogenic potential of satellite cells from distinct skeletal muscle origins in the rat.. J Vet Med Sci 2006 May;68(5):479-86.
    pubmed: 16757891doi: 10.1292/jvms.68.479google scholar: lookup
  30. Essén B, Lindholm A, Thornton J. Histochemical properties of muscle fibres types and enzyme activities in skeletal muscles of Standardbred trotters of different ages.. Equine Vet J 1980 Oct;12(4):175-80.
    pubmed: 6449365doi: 10.1111/j.2042-3306.1980.tb03420.xgoogle scholar: lookup
  31. Bröhl D, Vasyutina E, Czajkowski MT, Griger J, Rassek C, Rahn HP, Purfürst B, Wende H, Birchmeier C. Colonization of the satellite cell niche by skeletal muscle progenitor cells depends on Notch signals.. Dev Cell 2012 Sep 11;23(3):469-81.
    pubmed: 22940113doi: 10.1016/j.devcel.2012.07.014google scholar: lookup
  32. Bischoff R. Interaction between satellite cells and skeletal muscle fibers.. Development 1990 Aug;109(4):943-52.
    pubmed: 2226207doi: 10.1242/dev.109.4.943google scholar: lookup
  33. Stelzer G, Dalah I, Stein TI, Satanower Y, Rosen N, Nativ N, Oz-Levi D, Olender T, Belinky F, Bahir I, Krug H, Perco P, Mayer B, Kolker E, Safran M, Lancet D. In-silico human genomics with GeneCards.. Hum Genomics 2011 Oct;5(6):709-17.
    pmc: PMC3525253pubmed: 22155609doi: 10.1186/1479-7364-5-6-709google scholar: lookup
  34. Jones NC, Tyner KJ, Nibarger L, Stanley HM, Cornelison DD, Fedorov YV, Olwin BB. The p38alpha/beta MAPK functions as a molecular switch to activate the quiescent satellite cell.. J Cell Biol 2005 Apr 11;169(1):105-16.
    pmc: PMC2171902pubmed: 15824134doi: 10.1083/jcb.200408066google scholar: lookup
  35. Troy A, Cadwallader AB, Fedorov Y, Tyner K, Tanaka KK, Olwin BB. Coordination of satellite cell activation and self-renewal by Par-complex-dependent asymmetric activation of p38α/β MAPK.. Cell Stem Cell 2012 Oct 5;11(4):541-53.
    pmc: PMC4077199pubmed: 23040480doi: 10.1016/j.stem.2012.05.025google scholar: lookup
  36. Perdiguero E, Ruiz-Bonilla V, Gresh L, Hui L, Ballestar E, Sousa-Victor P, Baeza-Raja B, Jardí M, Bosch-Comas A, Esteller M, Caelles C, Serrano AL, Wagner EF, Muñoz-Cánoves P. Genetic analysis of p38 MAP kinases in myogenesis: fundamental role of p38alpha in abrogating myoblast proliferation.. EMBO J 2007 Mar 7;26(5):1245-56.
    pmc: PMC1817635pubmed: 17304211doi: 10.1038/sj.emboj.7601587google scholar: lookup
  37. Wang J, Walsh K. Resistance to apoptosis conferred by Cdk inhibitors during myocyte differentiation.. Science 1996 Jul 19;273(5273):359-61.
    pmc: PMC3641673pubmed: 8662523doi: 10.1126/science.273.5273.359google scholar: lookup
  38. Wang Y, Huang S, Sah VP, Ross J Jr, Brown JH, Han J, Chien KR. Cardiac muscle cell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated protein kinase family.. J Biol Chem 1998 Jan 23;273(4):2161-8.
    pubmed: 9442057doi: 10.1074/jbc.273.4.2161google scholar: lookup
  39. Aversa Z, Alamdari N, Castillero E, Muscaritoli M, Rossi Fanelli F, Hasselgren PO. β-Hydroxy-β-methylbutyrate (HMB) prevents dexamethasone-induced myotube atrophy.. Biochem Biophys Res Commun 2012 Jul 13;423(4):739-43.
    pmc: PMC3399026pubmed: 22705301doi: 10.1016/j.bbrc.2012.06.029google scholar: lookup
  40. Kan W, Zhao KS, Jiang Y, Yan W, Huang Q, Wang J, Qin Q, Huang X, Wang S. Lung, spleen, and kidney are the major places for inducible nitric oxide synthase expression in endotoxic shock: role of p38 mitogen-activated protein kinase in signal transduction of inducible nitric oxide synthase expression.. Shock 2004 Mar;21(3):281-7.
    pubmed: 14770043doi: 10.1097/01.shk.0000113314.37747.55google scholar: lookup
  41. Mitsutaka Y, Sumito O, Hidetaka O. Beta-hydroxy-beta-methylbutyrate inhibits lipopolysaccharide-induced interleukin-6 expression by increasing protein phosphatase-1α expression. RNA Transcription 2015;1:1–5.
  42. Cuenda A, Cohen P. Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis.. J Biol Chem 1999 Feb 12;274(7):4341-6.
    pubmed: 9933636doi: 10.1074/jbc.274.7.4341google scholar: lookup
  43. Han J, Molkentin JD. Regulation of MEF2 by p38 MAPK and its implication in cardiomyocyte biology.. Trends Cardiovasc Med 2000 Jan;10(1):19-22.
    pubmed: 11150724doi: 10.1016/s1050-1738(00)00039-6google scholar: lookup
  44. Pawlinski R, Tencati M, Hampton CR, Shishido T, Bullard TA, Casey LM, Andrade-Gordon P, Kotzsch M, Spring D, Luther T, Abe J, Pohlman TH, Verrier ED, Blaxall BC, Mackman N. Protease-activated receptor-1 contributes to cardiac remodeling and hypertrophy.. Circulation 2007 Nov 13;116(20):2298-306.
    pmc: PMC2848478pubmed: 17967980doi: 10.1161/circulationaha.107.692764google scholar: lookup
  45. Chevessier F, Hantaï D, Verdière-Sahuqué M. Expression of the thrombin receptor (PAR-1) during rat skeletal muscle differentiation.. J Cell Physiol 2001 Nov;189(2):152-61.
    pubmed: 11598900doi: 10.1002/jcp.10009google scholar: lookup
  46. Bentzinger CF, Wang YX, Rudnicki MA. Building muscle: molecular regulation of myogenesis.. Cold Spring Harb Perspect Biol 2012 Feb 1;4(2).
    pmc: PMC3281568pubmed: 22300977doi: 10.1101/cshperspect.a008342google scholar: lookup
  47. Hansen A. Myostatin mRNA expression in cultured equine satellite cells. 2014.
  48. de Mello F, Streit DP Jr, Sabin N, Gabillard JC. Dynamic expression of tgf-β2, tgf-β3 and inhibin βA during muscle growth resumption and satellite cell differentiation in rainbow trout (Oncorhynchus mykiss).. Gen Comp Endocrinol 2015 Jan 1;210:23-9.
    pubmed: 25449661doi: 10.1016/j.ygcen.2014.10.011google scholar: lookup
  49. García-Pelagio KP, Bloch RJ, Ortega A, González-Serratos H. Biomechanics of the sarcolemma and costameres in single skeletal muscle fibers from normal and dystrophin-null mice.. J Muscle Res Cell Motil 2011 Mar;31(5-6):323-36.
    pmc: PMC4326082pubmed: 21312057doi: 10.1007/s10974-011-9238-9google scholar: lookup
  50. Kuang W, Xu H, Vilquin JT, Engvall E. Activation of the lama2 gene in muscle regeneration: abortive regeneration in laminin alpha2-deficiency.. Lab Invest 1999 Dec;79(12):1601-13.
    pubmed: 10616210
  51. Gupta VA, Beggs AH. Kelch proteins: emerging roles in skeletal muscle development and diseases.. Skelet Muscle 2014;4:11.
    pmc: PMC4067060pubmed: 24959344doi: 10.1186/2044-5040-4-11google scholar: lookup
  52. Eddins MJ, Marblestone JG, Suresh Kumar KG, Leach CA, Sterner DE, Mattern MR, Nicholson B. Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy.. Cell Biochem Biophys 2011 Jun;60(1-2):113-8.
    pubmed: 21448668doi: 10.1007/s12013-011-9175-7google scholar: lookup
  53. Rittig N, Bach E, Thomsen HH, Møller AB, Hansen J, Johannsen M, Jensen E, Serena A, Jørgensen JO, Richelsen B, Jessen N, Møller N. Anabolic effects of leucine-rich whey protein, carbohydrate, and soy protein with and without β-hydroxy-β-methylbutyrate (HMB) during fasting-induced catabolism: A human randomized crossover trial.. Clin Nutr 2017 Jun;36(3):697-705.
    pubmed: 27265181doi: 10.1016/j.clnu.2016.05.004google scholar: lookup
  54. Pimentel GD, Rosa JC, Lira FS, Zanchi NE, Ropelle ER, Oyama LM, Oller do Nascimento CM, de Mello MT, Tufik S, Santos RV. β-Hydroxy-β-methylbutyrate (HMβ) supplementation stimulates skeletal muscle hypertrophy in rats via the mTOR pathway.. Nutr Metab (Lond) 2011 Feb 23;8(1):11.
    pmc: PMC3048483pubmed: 21345206doi: 10.1186/1743-7075-8-11google scholar: lookup
  55. Somwar R, Perreault M, Kapur S, Taha C, Sweeney G, Ramlal T, Kim DY, Keen J, Côte CH, Klip A, Marette A. Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.. Diabetes 2000 Nov;49(11):1794-800.
    pubmed: 11078445doi: 10.2337/diabetes.49.11.1794google scholar: lookup
  56. Cao W, Collins QF, Becker TC, Robidoux J, Lupo EG Jr, Xiong Y, Daniel KW, Floering L, Collins S. p38 Mitogen-activated protein kinase plays a stimulatory role in hepatic gluconeogenesis.. J Biol Chem 2005 Dec 30;280(52):42731-7.
    pubmed: 16272151doi: 10.1074/jbc.m506223200google scholar: lookup
  57. Huss JM, Torra IP, Staels B, Giguère V, Kelly DP. Estrogen-related receptor alpha directs peroxisome proliferator-activated receptor alpha signaling in the transcriptional control of energy metabolism in cardiac and skeletal muscle.. Mol Cell Biol 2004 Oct;24(20):9079-91.
    pmc: PMC517878pubmed: 15456881doi: 10.1128/mcb.24.20.9079-9091.2004google scholar: lookup
  58. Shao D, Liu Y, Liu X, Zhu L, Cui Y, Cui A, Qiao A, Kong X, Liu Y, Chen Q, Gupta N, Fang F, Chang Y. PGC-1 beta-regulated mitochondrial biogenesis and function in myotubes is mediated by NRF-1 and ERR alpha.. Mitochondrion 2010 Aug;10(5):516-27.
    pubmed: 20561910doi: 10.1016/j.mito.2010.05.012google scholar: lookup
  59. Towler MC, Hardie DG. AMP-activated protein kinase in metabolic control and insulin signaling.. Circ Res 2007 Feb 16;100(3):328-41.
    pubmed: 17307971doi: 10.1161/01.res.0000256090.42690.05google scholar: lookup
  60. Sanders MA, Madoux F, Mladenovic L, Zhang H, Ye X, Angrish M, Mottillo EP, Caruso JA, Halvorsen G, Roush WR, Chase P, Hodder P, Granneman JG. Endogenous and Synthetic ABHD5 Ligands Regulate ABHD5-Perilipin Interactions and Lipolysis in Fat and Muscle.. Cell Metab 2015 Nov 3;22(5):851-60.
    pmc: PMC4862007pubmed: 26411340doi: 10.1016/j.cmet.2015.08.023google scholar: lookup
  61. Ghanbari-Niaki A. Treadmill exercise training enhances ATP-binding cassette protein-A1 (ABCA1) expression in male rats’ heart and gastrocnemius muscles. Int J Endocrinol Metab 2010;8:206–210.
  62. Blondelle J, Ohno Y, Gache V, Guyot S, Storck S, Blanchard-Gutton N, Barthélémy I, Walmsley G, Rahier A, Gadin S, Maurer M, Guillaud L, Prola A, Ferry A, Aubin-Houzelstein G, Demarquoy J, Relaix F, Piercy RJ, Blot S, Kihara A, Tiret L, Pilot-Storck F. HACD1, a regulator of membrane composition and fluidity, promotes myoblast fusion and skeletal muscle growth.. J Mol Cell Biol 2015 Oct;7(5):429-40.
    pmc: PMC4589950pubmed: 26160855doi: 10.1093/jmcb/mjv049google scholar: lookup
  63. Cambron LD, Leskawa KC. Glycosphingolipids during skeletal muscle cell differentiation: comparison of normal and fusion-defective myoblasts.. Mol Cell Biochem 1994 Jan 26;130(2):173-85.
    pubmed: 8028596doi: 10.1007/bf01457398google scholar: lookup

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    doi: 10.3390/biomedicines11082329pubmed: 37626825google scholar: lookup
  2. Singh SS, Kumar A, Welch N, Sekar J, Mishra S, Bellar A, Gangadhariah M, Attaway A, Al Khafaji H, Wu X, Pathak V, Agrawal V, McMullen MR, Hornberger TA, Nagy LE, Davuluri G, Dasarathy S. Multiomics-Identified Intervention to Restore Ethanol-Induced Dysregulated Proteostasis and Secondary Sarcopenia in Alcoholic Liver Disease.. Cell Physiol Biochem 2021 Feb 6;55(1):91-116.
    doi: 10.33594/000000327pubmed: 33543862google scholar: lookup
  3. Rugowska A, Starosta A, Konieczny P. Epigenetic modifications in muscle regeneration and progression of Duchenne muscular dystrophy.. Clin Epigenetics 2021 Jan 19;13(1):13.
    doi: 10.1186/s13148-021-01001-zpubmed: 33468200google scholar: lookup
  4. Ciecierska A, Motyl T, Sadkowski T. Transcriptomic Profile of Primary Culture of Skeletal Muscle Cells Isolated from Semitendinosus Muscle of Beef and Dairy Bulls.. Int J Mol Sci 2020 Jul 7;21(13).
    doi: 10.3390/ijms21134794pubmed: 32645861google scholar: lookup
  5. Ogura J, Sato T, Higuchi K, Bhutia YD, Babu E, Masuda M, Miyauchi S, Rueda R, Pereira SL, Ganapathy V. Transport Mechanisms for the Nutritional Supplement β-Hydroxy-β-Methylbutyrate (HMB) in Mammalian Cells.. Pharm Res 2019 Apr 17;36(6):84.
    doi: 10.1007/s11095-019-2626-3pubmed: 30997560google scholar: lookup
  6. Chodkowska KA, Ciecierska A, Majchrzak K, Ostaszewski P, Sadkowski T. Effect of β-hydroxy-β-methylbutyrate on miRNA expression in differentiating equine satellite cells exposed to hydrogen peroxide.. Genes Nutr 2018;13:10.
    doi: 10.1186/s12263-018-0598-2pubmed: 29662554google scholar: lookup
  7. Sadkowski T, Ciecierska A, Oprządek J, Balcerek E. Breed-dependent microRNA expression in the primary culture of skeletal muscle cells subjected to myogenic differentiation.. BMC Genomics 2018 Jan 31;19(1):109.
    doi: 10.1186/s12864-018-4492-5pubmed: 29390965google scholar: lookup
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