Advertisement

Journal of Applied Genetics

, Volume 51, Issue 1, pp 51–57 | Cite as

Association of 3 polymorphisms in porcine troponin I genes (TNNI1 andTNNI2) with meat quality traits

  • H. Yang
  • Z. Y. Xu
  • M. G. Lei
  • F. E. Li
  • C. Y. Deng
  • Y. Z. Xiong
  • B. Zuo
Original Article

Abstract

The contractile protein troponin I (TnI), a constituent protein of the troponin complex located on the thin filaments of striated muscle, is involved in inhibition of calcium-induced myosin AT Pase activity (and thus contraction). TnI-slow (slow-twitch skeletal muscle isoform, named TNNI1) and TnI-fast (fast-twitch skeletal muscle isoform, named TNNI2) are muscle-fiber-type-specific proteins, and expression of their genes may affect the composition of muscle fiber, thereby influencing the meat quality traits. Thus, the TnI genes are potential candidate genes for traits related to meat quality in animals. Association of 2 SNPs (EU743939:g.5174T>C in intron 4, and EU743939:g.8350C>A in intron 7) of theTNNI1 gene and a SNP (EU696779:g.1167C>T in intron 3) of theTNNI2 gene with 11 meat quality traits were studied on 334 Large White × Meishan F2 pigs. In theTNNI1 gene, g.5174T>C and g.8350C>A were found to be significantly associated with intramuscular fat content and meat color value of biceps femoris. The g.5174T>C also showed significant effects on meat color value and marbling score of longissimus dorsi, as well as pH of longissimus dorsi and semispinalis capitis. The g.1167C>T polymorphism in theTNNI2 gene affected significantly the pH of longissimus dorsi, meat color value of longissimus dorsi and semispinalis capitis, marbling score of longissimus dorsi, and intramuscular fat.

Keywords

meat quality pigs polymorphisms TnI-slow TnI-fast troponin I 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Benjamini Y, Hochberg Y, 1995. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Roy Statistical Society B 57: 289–300.Google Scholar
  2. Bottinelli R, Reggiani C, 2000. Human skeletal muscle fibres: molecular and functional diversity. Prog Biophys Mol Biol 73: 195–262.CrossRefPubMedGoogle Scholar
  3. Calkins CR, Duston TR, Smith GC, Carpenter ZL, Davis GW, 1981. Relationship of fiber type composition to marbling and tenderness of bovine muscle. J Food Sci 46: 708–715.CrossRefGoogle Scholar
  4. Choe JH, Choi YM, Lee SH, Shin HG, Ryu YC, Hong KC, Kim BC, 2008. The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality. Meat Sci 80: 355–362.CrossRefGoogle Scholar
  5. Clark KA, McElhinny AS, Beckerle MC, Gregorio CC, 2002. Striated muscle cytoarchitecture: an intricate web of form and function. Annu Rev Cell Dev Biol 18: 637–706.CrossRefPubMedGoogle Scholar
  6. Corin SJ, Juhasz O, Zhu L, Conley P, Kedes L, Wade R, 1994. Structure and expression of the human slow twitch skeletal muscle troponin I gene. J Biol Chem 269: 10651–10659.PubMedGoogle Scholar
  7. Mullen AJ, Barton PJ, 2000. Structural characterization of the human fast skeletal muscle troponin I gene (TNNI2). Gene 242: 313–320.CrossRefPubMedGoogle Scholar
  8. Ovilo C, Fernandez A, Rodriguez MC, Nieto M, Silio L, 2006. Association ofMC4R gene variants with growth, fatness, carcass composition and meat and fat quality traits in heavy pigs. Meat Sci 73: 42–47.CrossRefGoogle Scholar
  9. Pette D, Staron RS, 1997. Mammalian skeletal muscle fiber type transitions. Int Rev Cytol 170: 143–223.CrossRefPubMedGoogle Scholar
  10. Picard B, Lefaucheur L, Berri C, Duclos MJ, 2002. Muscle fibre ontogenesis in farm animal species. Reprod Nutr Dev 42: 415–431.CrossRefPubMedGoogle Scholar
  11. Polly P, Haddadi LM, Issa LL, Subramaniam N, Palmer SJ, Tay ESE, Hardeman EC, 2003. hMus TRD1α1 represses MEF2 activation of the troponin I slow enhancer. J Biol Chem 278: 36603–36610.CrossRefPubMedGoogle Scholar
  12. Ryu YC, Kim BC, 2005. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci 71: 351–357.CrossRefGoogle Scholar
  13. Ryu YC, Kim BC, 2006. Comparison of histochemical characteristics in various pork groups categorized by postmortem metabolic rate and pork quality. J Anim Sci 84: 894–901.PubMedGoogle Scholar
  14. Schiaffino S, Reggiani C, 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev 76: 371–423.PubMedGoogle Scholar
  15. Varona L, Gomez-Raya L, Rauw WM, Noguera JL, 2005. A simulation study on the detection of causal mutations from F2 experiments. J Anim Breed Genet 122: 30–36.CrossRefPubMedGoogle Scholar
  16. Xiong YZ, Deng CY, 1999. Principle and method of swine testing. Chinese Agricultural Press, Beijing.Google Scholar
  17. Zuo B, Yang H, Lei MG, Li FE, Deng CY, Jiang SW, Xiong YZ, 2007. Association of the polymorphism inGYS1 andACOX1 gene with meat quality traits in pigs. Animal 1: 1243–1248.CrossRefGoogle Scholar

Copyright information

© Institute of Plant Genetics, Polish Academy of Sciences, Poznan 2010

Authors and Affiliations

  • H. Yang
    • 1
    • 2
  • Z. Y. Xu
    • 1
  • M. G. Lei
    • 1
  • F. E. Li
    • 1
  • C. Y. Deng
    • 1
  • Y. Z. Xiong
    • 1
  • B. Zuo
    • 1
  1. 1.Key Laboratory of Swine Genetics and Breeding, Ministry of Agriculture & Key Laboratory of Agricultural Animal Genetics and Breeding, Ministry of Education, College of Animal Science and Veterinary MedicineHuazhong Agricultural UniversityWuhanP. R. China
  2. 2.Livestock and Poultry Breeding Center of Hubei ProvinceWuhanP. R. China

Personalised recommendations