Acknowledgement
This work was supported by grants from the Individual Basic Science & Engineering Research Program (2017R1D1A1B03036432), the National Research Foundation of Korea, and the Next-Generation BioGreen 21 Program (Project No. PJ01325701), Rural Development Administration, Republic of Korea. Finally, we would like to thank the Writing Center at Jeonbuk National University for their language assistance, which we think readers will agree has greatly enhanced the readability of the manuscript.
References
- Kim H, Lee T, Park W, et al. Peeling back the evolutionary layers of molecular mechanisms responsive to exercise-stress in the skeletal muscle of the racing horse. DNA Res 2013;20:287-98. https://doi.org/10.1093/dnares/dst010
- Park KD, Park J, Ko J, et al. Whole transcriptome analyses of six thoroughbred horses before and after exercise using RNA-Seq. BMC Genomics 2012;13:473. https://doi.org/10.1186/1471-2164-13-473
- Capomaccio S, Cappelli K, Barrey E, Felicetti M, Silvestrelli M, Verini-Supplizi A. Microarray analysis after strenuous exercise in peripheral blood mononuclear cells of endurance horses. Anim Genet 2010;41:166-75. https://doi.org/10.1111/j.1365-2052.2010.02129.x
- Eivers SS, McGivney BA, Fonseca RG, et al. Alterations in oxidative gene expression in equine skeletal muscle following exercise and training. Physiol Genomics 2010;40:83-93. https://doi.org/10.1152/physiolgenomics.00041.2009
- Park JW, Song KD, Kim NY, et al. Molecular analysis of alternative transcripts of equine AXL receptor tyrosine kinase gene. Asian-Australas J Anim Sci 2017;30:1471-7. https://doi.org/10.5713/ajas.17.0409
- Cho HW, Shin S, Park JW, et al. Molecular characterization and expression analysis of the peroxisome proliferator activated receptor delta (PPARδ) gene before and after exercise in horse. Asian-Australas J Anim Sci 2015;28:697-702. https://doi.org/10.5713/ajas.14.0575
- Park JW, Choi JY, Hong SA, et al. Exercise induced upregulation of glutamate-cysteine ligase catalytic subunit and glutamate-cysteine ligase modifier subunit gene expression in Thoroughbred horses. Asian-Australas J Anim Sci 2017;30:728-35. https://doi.org/10.5713/ajas.16.0776
- Piccinini AM, Midwood KS. DAMPening inflammation by modulating TLR signalling. Mediators Inflamm 2010;2010:Article ID 672395. https://doi.org/10.1155/2010/672395
- Hindi SM, Kumar A. Toll-like receptor signalling in regenerative myogenesis: friend and foe. J Pathol 2016;239:125-8. https://doi.org/10.1002/path.4714
- Lee HG, Choi JY, Park JW, et al. Effects of exercise on myokine gene expression in horse skeletal muscles. Asian-Australas J Anim Sci 2019;32:350-6. https://doi.org/10.5713/ajas.18.0375
- Lee HG, Khummuang S, Youn HH, et al. The effect of heat stress on frame switch splicing of X-box binding protein 1 gene in horse. Asian-Australas J Anim Sci 2019;32:1095-103. https://doi.org/10.5713/ajas.18.0757
- Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. Methods 2001;25:402-8. https://doi.org/10.1006/meth.2001.1262
- Kim DH, Lee HG, Nipin Sp, et al. Validation of exercise-response genes in skeletal muscle cells of Thoroughbred racing horses. Anim Biosci 2021;34:134-142. https://doi.org/10.5713/ajas.18.0749
- Catoire M, Mensink M, Kalkhoven E, Schrauwen P, Kersten S. Identification of human exercise-induced myokines using secretome analysis. Physiol Genomics 2014;46:256-67. https://doi.org/10.1152/physiolgenomics.00174.2013
- Pourteymour S, Eckardt K, Holen T, et al. Global mRNA sequencing of human skeletal muscle: search for novel exercise-regulated myokines. Mol Metab 2017;6:352-65. https://doi.org/10.1016/j.molmet.2017.01.007
- Martin SJ. Cell death and inflammation: the case for IL-1 family cytokines as the canonical DAMPs of the immune system. FEBS J 2016;283:2599-615. https://doi.org/10.1111/febs.13775
- Schaefer L. Complexity of danger: the diverse nature of damage-associated molecular patterns. J Biol Chem 2014;289:35237-45. https://doi.org/10.1074/jbc.R114.619304
- Zhang X, Mosser DM. Macrophage activation by endogenous danger signals. J Pathol 2008;214:161-78. https://doi.org/10.1002/path.2284
- Cristi MC, Sanchez CP, Veneroso C, Cuevas MJ, Gonzalez-Gallego J. Effect of an acute exercise bout on toll-like receptor 4 and inflammatory mechanisms in rat heart. Rev Med Chile 2012;140:1282-8. https://doi.org/10.4067/s0034-98872012001000007
- Fernandez-Verdejo R, Vanwynsberghe AM, Essaghir A, et al. Activating transcription factor 3 attenuates chemokine and cytokine expression in mouse skeletal muscle after exercise and facilitates molecular adaptation to endurance training. FASEB J 2017;31:840-51. https://doi.org/10.1096/fj.201600 987R
- Kerst B, Mennerich D, Schuelke M, et al. Heterozygous myogenic factor 6 mutation associated with myopathy and severe course of Becker muscular dystrophy. Neuromuscul Disord 2000;10:572-7. https://doi.org/10.1016/S0960-8966(00)00150-4
- Miner JH, Wold B. Herculin, a fourth member of the MyoD family of myogenic regulatory genes. Proc Natl Acad Sci USA 1990;87:1089-93. https://doi.org/10.1073/pnas.87.3.1089
- Kim SY, Choi YJ, Joung SM, Lee BH, Jung YS, Lee JY. Hypoxic stress up-regulates the expression of Toll-like receptor 4 in macrophages via hypoxia-inducible factor. Immunology 2010;129:516-24. https://doi.org/10.1111/j.1365-2567.2009.03203.x
- Imai Y, Kuba K, Neely GG, et al. Identification of oxidative stress and toll-like receptor 4 signaling as a key pathway of acute lung injury. Cell 2008;133:235-49. https://doi.org/10.1016/j.cell.2008.02.043
- Zou J, An H, Xu H, Liu S, Cao X. Heat shock up-regulates expression of toll-like receptor-2 and toll-like receptor-4 in human monocytes via p38 kinase signal pathway. Immunology 2005;114:522-30. https://doi.org/10.1111/j.1365-2567.2004.02112.x
- Ju XH, Xu HJ, Yong YH, An LL, Jiao PR, Liao M. Heat stress upregulation of Toll-like receptors 2/4 and acute inflammatory cytokines in peripheral blood mononuclear cell (PBMC) of Bama miniature pigs: an in vivo and in vitro study. Animal 2014;8:1462-8. https://doi.org/10.1017/S1751731114001268
- Janeway JCA, Medzhitov R. Innate immune recognition. Annu Rev Immunol 2002;20:197-216. https://doi.org/10.1146/annurev.immunol.20.083001.084359
- Takeda K, Kaisho T, Akira S. Toll-like receptors. Annu Rev Immunol 2003;21:335-76. https://doi.org/10.1146/annurev.immunol.21.120601.141126
- Gilchrist M, Thorsson V, Li B, et al. Systems biology approaches identify ATF3 as a negative regulator of toll-like receptor 4. Nature 2006;441:173-8. https://doi.org/10.1038/nature04768
- Hai TW, Liu F, Coukos WJ, Green MR. Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers. Genes dev 1989;3:2083-90. https://doi.org/10.1101/gad.3.12b.2083
- Hsu JC, Laz T, Mohn KL, Taub R. Identification of LRF-1, a leucine-zipper protein that is rapidly and highly induced in regenerating liver. Proc Natl Acad Sci USA 1991;88:3511-5. https://doi.org/10.1073/pnas.88.9.3511
- Hai T, Wolfgang CD, Marsee DK, et al. ATF3 and stress responses. Gene Expr 1999;7:321-35.
- Hai T, Hartman MG. The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis. Gene 2001;273:1-11. https://doi.org/10.1016/S0378-1119(01)00551-0
- Shtil AA, Mandlekar S, Yu R, et al. Differential regulation of mitogen-activated protein kinases by microtubule-binding agents in human breast cancer cells. Oncogene 1999;18:377-84. https://doi.org/10.1038/sj.onc.1202305
- Zimmermann J, Erdmann D, Lalande I, Grossenbacher R, Noorani M, Furst P. Proteasome inhibitor induced gene expression profiles reveal overexpression of transcriptional regulators ATF3, GADD153 and MAD1. Oncogene 2000;19:2913-20. https://doi.org/10.1038/sj.onc.1203606
- Chen BP, Liang G, Whelan J, Hai T. ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms. J Biol Chem 1994;269:15819-26. https://doi.org/10.1016/S0021-9258(17)40754-X
- Iyer VR, Eisen MB, Ross DT, et al. The transcriptional program in the response of human fibroblasts to serum. Science 1999;283:83-7. https://doi.org/10.1126/science.283.5398.83
- Sp N, Kang DY, Kim DH, et al. Methylsulfonylmethane inhibits cortisol-induced stress through p53-mediated SDHA/HPRT1 expression in racehorse skeletal muscle cells: a primary step against exercise stress. Exp Ther Med 2020;19:214-22. https://doi.org/10.3892/etm.2019.8196
- Bleul CC, Fuhlbrigge RC, Casasnovas JM, Aiuti A, Springer TA. A highly efficacious lymphocyte chemoattractant, stromal cell-derived factor 1 (SDF-1). J Exp Med 1996;184:1101-9. https://doi.org/10.1084/jem.184.3.1101
- Loetscher M, Gerber B, Loetscher P, et al. Chemokine receptor specific for IP10 and mig: structure, function, and expression in activated T-lymphocytes. J Exp Med 1996;184:963-9. https://doi.org/10.1084/jem.184.3.963
- Weber M, Uguccioni M, Ochensberger B, Baggiolini M, Clark-Lewis I, Dahinden CA. Monocyte chemotactic protein MCP-2 activates human basophil and eosinophil leukocytes similar to MCP-3. J Immunol 1995;154:4166-72.
- Robertson TA, Maley MAL, Grounds MD, Papadimitriou JM. The role of macrophages in skeletal muscle regeneration with particular reference to chemotaxis. Exp Cell Res 1993;207:321-31. https://doi.org/10.1006/excr.1993.1199
- Pimkhaokham A, Shimada Y, Fukuda Y, et al. Nonrandom chromosomal imbalances in esophageal squamous cell carcinoma cell lines: possible involvement of the ATF3 and CENPF genes in the 1q32 amplicon. Jpn J Cancer Res 2000;91:1126-3. https://doi.org/10.1111/j.1349-7006.2000.tb00895.x