Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Selection of candidate genes affecting meat quality and preliminary exploration of related molecular mechanisms in the Mashen pig

  • Gao, Pengfei (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Cheng, Zhimin (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Li, Meng (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Zhang, Ningfang (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Le, Baoyu (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Zhang, Wanfeng (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Song, Pengkang (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Guo, Xiaohong (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Li, Bugao (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University) ;
  • Cao, Guoqing (College of Animal Science and Veterinary Medicine, Shanxi Agricultural University)
  • Received : 2018.09.20
  • Accepted : 2019.02.07
  • Published : 2019.08.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: The aim of this study was to select the candidate genes affecting meat quality and preliminarily explore the related molecular mechanisms in the Mashen pig. Methods: The present study explored genetic factors affecting meat quality in the Mashen pig using RNA sequencing (RNA-Seq). We sequenced the transcriptomes of 180-day-old Mashen and Large White pigs using longissimus dorsi to select differentially expressed genes (DEGs). Results: The results indicated that a total of 425 genes were differentially expressed between Mashen and Large White pigs. A gene ontology enrichment analysis revealed that DEGs were mainly enriched for biological processes associated with metabolism and muscle development, while a Kyoto encyclopedia of genes and genomes analysis showed that DEGs mainly participated in signaling pathways associated with amino acid metabolism, fatty acid metabolism, and skeletal muscle differentiation. A MCODE analysis of the protein-protein interaction network indicated that the four identified subsets of genes were mainly associated with translational initiation, skeletal muscle differentiation, amino acid metabolism, and oxidative phosphorylation pathways. Conclusion: Based on the analysis results, we selected glutamic-oxaloacetic transaminase 1, malate dehydrogenase 1, pyruvate dehydrogenase 1, pyruvate dehydrogenase kinase 4, and activator protein-1 as candidate genes affecting meat quality in pigs. A discussion of the related molecular mechanisms is provided to offer a theoretical basis for future studies on the improvement of meat quality in pigs.

Keywords

References

  1. Choi YM, Kim BC. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livest Sci 2009;122:105-18. https://doi.org/10.1016/j.livsci.2008.08.015
  2. Sun L, Bai M, Xiang L, Zhang G, Ma W, Jiang H. Comparative transcriptome profiling of longissimus muscle tissues from Qianhua Mutton Merino and Small Tail Han sheep. Sci Rep 2016;6:33586. https://doi.org/10.1038/srep33586
  3. 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. http://dx.doi.org/10.1155/2016/3182746
  4. Qian X, Ba Y, Zhuang Q, Zhong G. RNA-Seq technology and its application in fish transcriptomics. OMICS 2014;18:98-110. https://doi.org/10.1089/omi.2013.0110
  5. Ayuso M, Fernandez A, Nunez Y, et al. Comparative analysis of muscle transcriptome between pig genotypes identifies genes and regulatory mechanisms associated to growth, fatness and metabolism. PLoS One 2015;10:e0145162. https://doi.org/10.1371/journal.pone.0145162
  6. Huang WL, Zhang XX, Li A, Miao XY. Identification of differentially expressed genes between subcutaneous and intramuscular adipose tissue of Large White pig using RNA-seq. Yi Chuan 2017;39:501-11. https://doi.org/10.16288/j.yczz.17-038
  7. Xu Y, Qian H, Feng X, et al. Differential proteome and transcriptome analysis of porcine skeletal muscle during development. J Proteomics 2012;75:2093-108. https://doi.org/10.1016/j.jprot.2012.01.013
  8. Larzul C, Lefaucheur L, Ecolan P, et al. Phenotypic and genetic parameters for longissimus muscle fiber characteristics in relation to growth, carcass, and meat quality traits in large white pigs. J Anim Sci 1997;75:3126-37. https://doi.org/10.2527/1997.75123126x
  9. Zhao Y, Gao P, Li W, et al. Study on the developmental expression of Lbx1 gene in longissimus dorsi of Mashen and Large White pigs. Italian J Anim Sci 2016;14:3720. https://doi.org/10.4081/ijas.2015.3720
  10. Zhao J, Li K, Yang Q, Du M, Liu X, Cao G. Enhanced adipogenesis in Mashen pigs compared with Large White pigs. Italian J Anim Sci 2017;16:217-25. https://doi.org/10.1080/1828051X.2017.1285682
  11. Li BG, Guo XH, Cao GQ, et al. Expression analysis of DECR1 gene in tissues of Mashen and Large White pig. Acta Vet Zootec Sin 2011;42:475-80.
  12. Pena RN, Quintanilla R, Manunza A, Gallardo D, Casellas J, Amills M. Application of the microarray technology to the transcriptional analysis of muscle phenotypes in pigs. Anim Genet 2014;45:311-21. https://doi.org/10.1111/age.12146
  13. Li XJ, Zhou J, Liu LQ, Qian K, Wang CL. Identification of genes in longissimus dorsi muscle differentially expressed between Wannanhua and Yorkshire pigs using RNA-sequencing. Anim Genet 2016;47:324-33. https://doi.org/10.1111/age.12421
  14. von Mering C, Jensen LJ, Snel B, et al. STRING: known and predicted protein-protein associations, integrated and transferred across organisms. Nucleic Acids Res 2005;33:D433-7. https://doi.org/10.1093/nar/gki005
  15. Matsakas A, Patel K. Skeletal muscle fibre plasticity in response to selected environmental and physiological stimuli. Histol Histopathol 2009;24:611-29. https://doi.org/10.14670/HH-24.611
  16. Schiaffino S, Reggiani C. Fiber types in mammalian skeletal muscles. Physiol Rev 2011;91:1447-531. https://doi.org/10.1152/physrev.00031.2010
  17. Guo J, Yu XF, Wu T, Ren Y, Zhu LN, Wang YZ. Different expression of different types of muscle fibers in the longissimus dorsi muscle of Jinhua pig and Changbai pig. Chinese J Anim Sci 2012;48:15-8.
  18. Otto A, Patel K. Signalling and the control of skeletal muscle size. Exp Cell Res 2010;316:3059-66. https://doi.org/10.1016/j.yexcr.2010.04.009
  19. Frontera WR, Ochala J. Skeletal muscle: a brief review of structure and function. Calcif Tissue Int 2015;96:183-95. https://doi.org/10.1007/s00223-014-9915-y
  20. Gao PF, Guo XH, Du M, et al. LncRNA profiling of skeletal muscles in Large White pigs and Mashen pigs during development. J Anim Sci 2017;95:4239-50. https://doi.org/10.2527/jas2016.1297
  21. Wagner EF. Functions of AP1 (Fos/Jun) in bone development. Ann Rheum Dis 2002;61 (Suppl 2):ii40-2. http://dx.doi.org/10.1136/ard.61.suppl_2.ii40
  22. Shaulian E, Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 2002;4:E131-E6. https://doi.org/10.1038/ncb0502-e131
  23. Thompson MR, Xu D, Williams BR. ATF3 transcription factor and its emerging roles in immunity and cancer. J Mol Med (Berl) 2009;87:1053-60. https://doi.org/10.1007/s00109-009-0520-x
  24. Han CC, Wang FS. Research progress on AP-1. Chinese J Cell Biol 2017;39:1357-62.
  25. Ishikawa H, Shozu M, Okada M, et al. Early growth response gene-1 plays a pivotal role in down-regulation of a cohort of genes in uterine leiomyoma. J Mol Endocrinol 2007;39:333-41. https://doi.org/10.1677/JME-06-0069
  26. Zhou LZ, Johnson AP, Rando TA. $NF{\kappa}B$ and AP-1 mediate transcriptional responses to oxidative stress in skeletal muscle cells. Free Radic Biol Med 2001;31:1405-16. https://doi.org/10.1016/S0891-5849(01)00719-5
  27. Toney MD. Aspartate aminotransferase: an old dog teaches new tricks. Arch Biochem Biophys 2014;544:119-27. https://doi.org/10.1016/j.abb.2013.10.002
  28. 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
  29. Birsoy K, Wang T, Chen WW, Freinkman E, Abu-Remaileh M, Sabatini DM. An essential role of the mitochondrial electron transport chain in cell proliferation is to enable aspartate synthesis. Cell 2015;162:540-51. https://doi.org/10.1016/j.cell.2015.07.016
  30. Wu MY, Cao CX, Zhang L, Xiao TF. Contents of fatty acid and amino acid in the muscles of several varieties of pigs. J Fujian Agric Forestry Univ 2009;38:166-70.
  31. Zhu QJ, Shen XL, Wang SY, Wang LP, Liu YM. Detection and analysis of volatile flavor compounds of cured meat made of Congjiangxiang pig. Guizhou Agric Sci 2006;34:19-22.
  32. Halbrook CJ, Lyssiotis CA. Employing metabolism to improve the diagnosis and treatment of pancreatic cancer. Cancer Cell 2017;31:5-19. https://doi.org/10.1016/j.ccell.2016.12.006
  33. Wiley CD, Campisi J. From ancient pathways to aging cells-connecting metabolism and cellular senescence. Cell Metab 2016;23:1013-21. https://doi.org/10.1016/j.cmet.2016.05.010
  34. Shingfield KJ, Bernard L, Leroux C, Chilliard Y. Role of trans fatty acids in the nutritional regulation of mammary lipogenesis in ruminants. Animal 2010;4:1140-66. https://doi.org/10.1017/S1751731110000510
  35. Zeng YQ, Wang GL, Wei SD, et al. Studies on carcass and meat quality performance of ccrossbred pigs with graded proportions of Laiwu Black genes. Hereditas 2005;27:65-9. https://doi.org/10.3321/j.issn:0253-9772.2005.01.013
  36. 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
  37. 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
  38. 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;105:34-43. https://doi.org/10.1016/j.ymgme.2011.09.032
  39. Rahman S. Mitochondrial disease and epilepsy. Dev Med Child Neurol 2012;54:397-406. https://doi.org/10.1111/j.1469-8749.2011.04214.x
  40. McFate T, Mohyeldin A, Lu H, et al. Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. J Biol Chem 2008;283:22700-8. https://doi.org/10.1074/jbc.M801765200

Cited by

  1. Comparative Transcriptome Analyses of Longissimus thoracis Between Pig Breeds Differing in Muscle Characteristics vol.11, 2019, https://doi.org/10.3389/fgene.2020.526309
  2. A bioinformatics investigation into the pharmacological mechanisms of the effect of the Yinchenhao decoction on hepatitis C based on network pharmacology vol.20, pp.1, 2019, https://doi.org/10.1186/s12906-020-2823-y