Arginine induces skeletal muscle fiber type conversion by upregulating Akirin2 and AMPK/PGC-1α in mice
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We have previously reported that arginine promotes slow myosin heavy chain expression in cell culture via Akirin2 and the AMP-activated protein kinase (AMPK) signaling pathway. Our goal in the present study was to investigate whether arginine has similar functions and molecular mechanisms in vivo. Kunming mice were fed a diet supplemented with arginine and actively immunized with Akirin2. The study lasted for 40 d. Tibialis anterior (TA) muscle was harvested for analysis. We found that Kunming mice supplemented with arginine significantly increased the oxidative fibers expression and decreased the expression of glycolytic fiber. Expressions of peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α) and AMPK were increased in the TA muscle of arginine-treated Kunming mice. We also find that dietary supplementation of arginine increased the succinate dehydrogenase and malate dehydrogenase activities and decreased the lactate dehydrogenase activity. But active immunization against Akirin2 got opposite results. These results indicated that arginine induced muscle fiber transition from type II to type I, which may be mediated by Akirin2 and AMPK//PGC-1α signaling pathway.
KeywordsArginine muscle fiber type conversion mice Akirin2 AMPK/PGC-1α signaling
AMP-activated protein kinase
peroxisome proliferator activated receptor-γ coactivator-1α
myosin heavy chain
phosphate buffer saline.
This work was supported by the Sichuan Youth Science and Technology Foundation (No. 2017JQ0008), the National Natural Science Foundation of China (No. 31472108), and the Specific Research Supporting Program for Discipline Construction in Sichuan Agricultural University.
Compliance with ethical standards
Conflict of Interest
All authors declare that they have no conflict of interest.
All animal procedures were performed in compliance with the experimental protocols approved by the Animal Care and Use Committee of the Animal Nutrition Institute of Sichuan Agricultural University.
- Chen XL, Guo YF, Jia G, Zhao H, Liu GM, Huang ZQ (2018a) Arginine promotes slow myosin heavy chain expression via Akirin2 and the AMP-activated protein kinase signaling pathway in porcine skeletal muscle satellite cells. J Agric Food Chem 66:4734–4740. https://doi.org/10.1021/acs.jafc.8b00775 CrossRefGoogle Scholar
- Chen XL, Guo YF, Jia G, Zhao H, Liu GM, Huang ZQ (2018b) Effects of active immunization against Akirin2 on muscle fiber-type composition in pigs. Anim Biotechnol. https://doi.org/10.1080/10495398.2017.1390475
- Goto A, Matsushita K, Gesellchen V, El Chamy L, Kuttenkeuler D, Takeuchi O, Hoffmann JA, Akira S, Boutros M, Reichhart JM (2008) Akirins are highly conserved nuclear proteins required for NF-kappaB-dependent gene expression in drosophila and mice. Nat Immunol. 9:97–104. https://doi.org/10.1038/ni1543 CrossRefGoogle Scholar
- Tartey S, Matsushita K, Vandenbon A, Ori D, Imamura T, Mino T, Standley DM, Hoffmann JA, Reichhart JM, Akira S, Takeuchi O (2014) Akirin2 is critical for inducing inflammatory genes by bridging IκB-ζ and the SWI/SNF complex. EMBO J 33:2332–2348. https://doi.org/10.15252/embj.201488447 CrossRefGoogle Scholar
- Wang L, Jia Y, Rogers H, Suzuki N, Gassmann M, Wang Q, McPherron AC, Kopp JB, Yamamoto M, Noguchi CT (2013) Erythropoietin contributes to slow oxidative muscle fiber specification via PGC-1α and AMPK activation. Int J Biochem Cell Biol 45:1155–1164. https://doi.org/10.1016/j.biocel.2013.03.007 CrossRefGoogle Scholar
- Wang L, Wang Z, Yang K, Shu G, Wang S, Gao P, Zhu X, Xi Q, Zhang Y, Jiang Q (2016) Epigallocatechin gallate reduces slow-twitch muscle fiber formation and mitochondrial biosynthesis in C2C12 cells by repressing AMPK Activity and PGC-1α expression. J Agr Food Chem 64:6517–6523. https://doi.org/10.1021/acs.jafc.6b02193 CrossRefGoogle Scholar
- Zhang C, Luo J, Yu B, Zheng P, Huang ZQ, Mao XB, He J, Yu J, Chen JL, Chen DW (2015) Dietary resveratrol supplementation improves meat quality of finishing pigs through changing muscle fiber characteristics and antioxidative status. Meat Sci 102:15–21. https://doi.org/10.1016/j.meatsci.2014.11.014 CrossRefGoogle Scholar