Animal Bioscience

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
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Glutamic-oxaloacetic transaminase 1 regulates adipocyte differentiation by altering nicotinamide adenine dinucleotide phosphate content

  • Yang, Yang (College of Animal Science, Shanxi Agricultural University) ;
  • Cheng, Zhimin (College of Animal Science, Shanxi Agricultural University) ;
  • Zhang, Wanfeng (College of Animal Science, Shanxi Agricultural University) ;
  • Hei, Wei (College of Animal Science, Shanxi Agricultural University) ;
  • Lu, Chang (College of Animal Science, Shanxi Agricultural University) ;
  • Cai, Chunbo (College of Animal Science, Shanxi Agricultural University) ;
  • Zhao, Yan (College of Animal Science, Shanxi Agricultural University) ;
  • Gao, Pengfei (College of Animal Science, Shanxi Agricultural University) ;
  • Guo, Xiaohong (College of Animal Science, Shanxi Agricultural University) ;
  • Cao, Guoqing (College of Animal Science, Shanxi Agricultural University) ;
  • Li, Bugao (College of Animal Science, Shanxi Agricultural University)
  • Received : 2021.04.14
  • Accepted : 2021.07.27
  • Published : 2022.02.01
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Abstract

Objective: This study was performed to examine whether the porcine glutamic-oxaloacetic transaminase 1 (GOT1) gene has important functions in regulating adipocyte differentiation. Methods: Porcine GOT1 knockout and overexpression vectors were constructed and transfected into the mouse adipogenic 3T3-L1 cells. Lipid droplets levels were measured after 8 days of differentiation. The mechanisms through which GOT1 participated in lipid deposition were examined by measuring the expression of malate dehydrogenase 1 (MDH1) and malic enzyme (ME1) and the cellular nicotinamide adenine dinucleotide phosphate (NADPH) content. Results: GOT1 knockout significantly decreased lipid deposition in the 3T3-L1 cells (p<0.01), whereas GOT1 overexpression significantly increased lipid accumulation (p<0.01). At the same time, GOT1 knockout significantly decreased the NADPH content and the expression of MDH1 and ME1 in the 3T3-L1 cells. Overexpression of GOT1 significantly increased the NADPH content and the expression of MDH1 and ME1, suggesting that GOT1 regulated adipocyte differentiation by altering the NADPH content. Conclusion: The results preliminarily revealed the effector mechanisms of GOT1 in regulating adipose differentiation. Thus, a theoretical basis is provided for improving the quality of pork and studies on diseases associated with lipid metabolism.

Keywords

Acknowledgement

This work was supported by National Natural Science Foundation of China (31872336), Special Funds for Scholars Support Program of Shanxi Province (2016; 2017), Basic Research Project of Shanxi Province (201901D211376; 201901D211369).

References

  1. Spurlock ME, Gabler NK. The development of porcine models of obesity and the metabolic syndrome. J Nutr 2008;138:397-402. https://doi.org/10.1093/jn/138.2.397
  2. Squillaro T, Peluso G, Galderisi U, Di Bernardo G. Long noncoding RNAs in regulation of adipogenesis and adipose tissue function. Elife 2020;9:e59053. https://doi.org/10.7554/eLife.59053
  3. Song T, Yang Y, Jiang S, Peng J. Novel Insights into adipogenesis from the perspective of transcriptional and RNA N6-methyladenosine-mediated post-transcriptional regulation. Adv Sci 2020;7:2001563. https://doi.org/10.1002/advs.202001563
  4. Listrat A, Lebret B, Louveau I, et al. How muscle structure and composition influence meat and flesh quality. Sci World J 2016;2016:Article ID 3182746. https://doi.org/10.1155/2016/3182746
  5. Bishop CA, Schulze MB, Klaus S, Weitkunat K. The branched-chain amino acids valine and leucine have differential effects on hepatic lipid metabolism. FASEB J 2020;34:9727-39. https://doi.org/10.1096/fj.202000195R
  6. Zhao JX, Li K, Yang QY, Du M, Liu XD, Cao GQ. Enhanced adipogenesis in Mashen pigs compared with Large White pigs. Ita J Anim Sci 2017;16:217-25. https://doi.org/10.1080/1828051x.2017.1285682
  7. Gao P, Cheng Z, Li M, et al. Selection of candidate genes affecting meat quality and preliminary exploration of related molecular mechanisms in the mashen pig. Asian-Australas J Anim Sci 2019;32:1084-94. https://doi.org/10.5713/ajas.18.0718
  8. Hirotsu K, Goto M, Okamoto A, Miyahara I. Dual substrate recognition of aminotransferases. Chem Rec 2005;5:160-72. https://doi.org/10.1002/tcr.20042
  9. Zhou X, Liu K, Cui J, et al. Circ-MBOAT2 knockdown represses tumor progression and glutamine catabolism by miR-433-3p/GOT1 axis in pancreatic cancer. J Exp Clin Cancer Res 2021;40:124. https://doi.org/10.1186/s13046-021-01894-x
  10. Wiley CD, Velarde MC, Lecot P, et al. Mitochondrial dysfunction induces senescence with a distinct secretory phenotype. Cell Metab 2016;23:303-14. https://doi.org/10.1016/j.cmet.2015.11.011
  11. Qing GL, Li B, Vu A, et al. ATF4 regulates MYC-Mediated neuroblastoma cell death upon glutamine deprivation. Cancer Cell 2012;22:631-44. https://doi.org/10.1016/j.ccr.2012.09.021
  12. Son J, Lyssiotis CA, Ying H, et al. Glutamine supports pancreatic cancer growth through a KRAS-regulated metabolic pathway. Nature 2013;496:101-5. https://doi.org/10.1038/nature12040
  13. Alfaia CM, Lopes PA, Madeira MS, et al. Current feeding strategies to improve pork intramuscular fat content and its nutritional quality. Adv Food Nutr Res 2019;89:53-94. http://doi.org/10.1016/bs.afnr.2019.03.006
  14. Cannata S, Engle TE, Moeller SJ, et al. Effect of visual marbling on sensory properties and quality traits of pork loin. Meat Sci 2010;85:428-34. https://doi.org/10.1016/j.meatsci.2010.02.011
  15. Madeira MS, Costa P, Alfaia CM, et al. The increased intramuscular fat promoted by dietary lysine restriction in lean but not in fatty pig genotypes improves pork sensory attributes. J Anim Sci 2013;91:3177-87. https://doi.org/10.2527/jas.2012-5424
  16. Hocquette JF, Gondret F, Baeza E, Medale F, Jurie C, Pethick DW. Intramuscular fat content in meat-producing animals: development, genetic and nutritional control, and identification of putative markers. Animal 2010;4:303-19. https://doi.org/10.1017/S1751731109991091
  17. Sen U, Sirin E, Ensoy U, Aksoy Y, Ulutas Z, Kuran M. The effect of maternal nutrition level during mid-gestation on postnatal muscle fibre composition and meat quality in lambs. Anim Prod Sci 2016;56:834-43. https://doi.org/10.1071/An14663
  18. Joo ST, Kim GD, Hwang YH, Ryu YC. Control of fresh meat quality through manipulation of muscle fiber characteristics. Meat Sci 2013;95:828-36. https://doi.org/10.1016/j.meatsci.2013.04.044
  19. Cho IC, Park HB, Ahn JS, et al. A functional regulatory variant of MYH3 influences muscle fiber-type composition and intramuscular fat content in pigs. PLoS Genet 2019;15:e1008279. https://doi.org/10.1371/journal.pgen.1008279
  20. Zhou X, Liu Y, Zhang L, Kong X, Li F. Serine-to-glycine ratios in low-protein diets regulate intramuscular fat by affecting lipid metabolism and myofiber type transition in the skeletal muscle of growing-finishing pigs. Anim Nutr 2021;7:384-92. https://doi.org/10.1016/j.aninu.2020.08.011
  21. Cong L, Ran FA, Cox D, et al. Multiplex genome engineering using CRISPR/Cas systems. Science 2013;339:819-23. https://doi.org/10.1126/science.1231143
  22. Zhou X, Xin J, Fan N, et al. Generation of CRISPR/Cas9-mediated gene-targeted pigs via somatic cell nuclear transfer. Cell Mol Life Sci 2015;72:1175-84. https://doi.org/10.1007/s00018-014-1744-7
  23. Zhan T, Rindtorff N, Betge J, Ebert MP, Boutros M. CRISPR/Cas9 for cancer research and therapy. Semin Cancer Biol 2019;55:106-19. https://doi.org/10.1016/j.semcancer.2018.04.001
  24. Kim EY, Kim WK, Kang HJ, et al. Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity. J Lipid Res 2012;53:1864-76. https://doi.org/10.1194/jlr.M026567
  25. Yu X, Hiromasa Y, Tsen H, Stoops JK, Roche TE, Zhou ZH. Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains. Structure 2008;16:104-14. https://doi.org/10.1016/j.str.2007.10.024
  26. Patel KP, O'brien TW, Subramony SH, Shuster J, Stacpoole PW. The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients. Mol Genet Metab 2012;106:385-94. https://doi.org/10.1016/j.ymgme.2012.03.017
  27. Gardan D, Gondret F, Louveau I. Lipid metabolism and secretory function of porcine intramuscular adipocytes compared with subcutaneous and perirenal adipocytes. Am J Physiol Endocrinol Metab 2006;291:E372-80. https//doi.org/10.1152/ajpendo.00482.2005
  28. Wang YP, Zhou LS, Zhao YZ, et al. Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress. EMBO J 2014;33:1304-20. https//doi.org/10.1002/embj.201387224
  29. Fell DA, Small JR. Fat synthesis in adipose tissue. an examination of stoichiometric constraints. Biochem J 1986;238:781-6. https://doi.org/10.1042/bj2380781
  30. Kim EY, Kim WK, Kang HJ, et al. Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity. J Lipid Res 2012;53:1864-76. https://doi.org/10.1194/jlr.M026567