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Gene Review

MYOG  -  myogenin (myogenic factor 4)

Sus scrofa

 
 
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Disease relevance of myog

  • Variation at the myogenin locus explained 4% of the total phenotypic variation in birth weight, growth rate, and carcass weight, and 5.8% of the total variation in lean weight [1].
 

High impact information on myog

  • The inhibition by TNFalpha of IGF-I-induced protein synthesis and expression of myogenin is not due to direct killing of myoblasts by TNFalpha [2].
  • The simultaneous decrease in IGFBP-3 mRNA and protein that accompanies IGF-I-induced myogenin expression suggests that differentiation of myogenic cells may be preceded or accompanied by decreased production of IGFBP-3 [3].
  • These newly formed myofibers maintained their Mb skeletal muscle origin as evidenced by their capacity to express myogenin and fast skeletal myosin [4].
  • Development of muscle fibers is regulated by the MyoD gene family consisting of MyoD1, myf-5, myf-6, and myogenin [5].
  • Backfat thickness was negatively related to myogenin expression in the F-line [6].
 

Biological context of myog

 

Anatomical context of myog

  • Myogenin has a central position within the MyoD gene family because myogenin expression abrogates myoblast proliferation potential and regulates the differentiation of single nucleated myoblasts into multinucleated myofibers [1].
  • Thus, myogenin genotype could be related to variation in the number of muscle fibers formed, leading to variation in muscle mass and, thus, lean weight [1].
 

Associations of myog with chemical compounds

  • The PEM isolated from sows fed L-carnitine had decreased IGF-II (P = 0.02), IGFBP-3 (P = 0.03), and myogenin (P = 0.04; 61, 59, and 67%, respectively) mRNA abundance compared with controls [9].
 

Other interactions of myog

References

  1. Influences of myogenin genotypes on birth weight, growth rate, carcass weight, backfat thickness, and lean weight of pigs. te Pas, M.F., Soumillion, A., Harders, F.L., Verburg, F.J., van den Bosch, T.J., Galesloot, P., Meuwissen, T.H. J. Anim. Sci. (1999) [Pubmed]
  2. Cytokine-hormone interactions: tumor necrosis factor alpha impairs biologic activity and downstream activation signals of the insulin-like growth factor I receptor in myoblasts. Broussard, S.R., McCusker, R.H., Novakofski, J.E., Strle, K., Shen, W.H., Johnson, R.W., Freund, G.G., Dantzer, R., Kelley, K.W. Endocrinology (2003) [Pubmed]
  3. Effect of insulin-like growth factor (IGF)-I and Des (1-3) IGF-I on the level of IGF binding protein-3 and IGF binding protein-3 mRNA in cultured porcine embryonic muscle cells. Yang, F., Johnson, B.J., White, M.E., Hathaway, M.R., Dayton, W.R. J. Cell. Physiol. (1999) [Pubmed]
  4. Cell transplantation for treatment of acute myocardial infarction: unique capacity for repair by skeletal muscle satellite cells. Horackova, M., Arora, R., Chen, R., Armour, J.A., Cattini, P.A., Livingston, R., Byczko, Z. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
  5. Genetic variation at the porcine MYF-5 gene locus. Lack Of association with meat production traits. te Pas, M.F., Harders, F.L., Soumillion, A., Born, L., Buist, W., Meuwissen, T.H. Mamm. Genome (1999) [Pubmed]
  6. Messenger ribonucleic acid expression of the MyoD gene family in muscle tissue at slaughter in relation to selection for porcine growth rate. te Pas, M.F., Verburg, F.J., Gerritsen, C.L., de Greef, K.H. J. Anim. Sci. (2000) [Pubmed]
  7. Rapid communication: myogenin (MYOG) physically maps to porcine chromosome 9q2.1-q2.6. Ernst, C.W., Mendez, E.A., Robic, A., Rothschild, M.F. J. Anim. Sci. (1998) [Pubmed]
  8. Rapid communication: MspI restriction fragment length polymorphism at the swine myogenin locus. Ernst, C.W., Vaske, D.A., Larson, R.G., Rothschild, M.F. J. Anim. Sci. (1993) [Pubmed]
  9. Effects of L-carnitine on fetal growth and the IGF system in pigs. Waylan, A.T., Kayser, J.P., Gnad, D.P., Higgins, J.J., Starkey, J.D., Sissom, E.K., Woodworth, J.C., Johnson, B.J. J. Anim. Sci. (2005) [Pubmed]
 
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