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Gene Review

Myog  -  myogenin

Rattus norvegicus

Synonyms: Myogenin
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Disease relevance of Myog

  • Because of the initial increase of immediate early gene c-fos mRNA and the subsequent increase of myogenic transcription factor myogenin mRNA, it appears that repetitive muscle stretch induces sequential progression of gene transcription toward muscle hypertrophy [1].
  • Together, our results suggest that the transformed and undifferentiated phenotype of BA-Han-1C rhabdomyosarcoma cells is associated with the inactivation of the myogenic factor MyoD1 as well as lack of myogenin expression [2].
  • EXPERIMENTAL DESIGN: To clarify the primary events in myogenic precursor cell activation, the expression of myogenin was examined in rats 1 to 48 hours after either a contusion injury to the gastrocnemius or after toxic injury to the soleus muscle [3].
  • However, as revealed by changes in the expression levels of these two regulatory factors under conditions of hypothyroidism and chronic low-frequency stimulation (CLFS), MyoD and myogenin did not seem to be strictly correlated with fast and slow myosins, respectively [4].
  • The unaltered levels of transcripts of myogenin, SkM2 of Na+ channels and gamma-subunit of AChR, confirm that there is no denervation-like prejunctional (nerve-related) component to explain the muscle weakness or the upregulation of AChRs at sites distant from burns [5].

Psychiatry related information on Myog

  • It is likely that this maintained level of increased Id expression, in conjunction with the returning levels of myogenin and MRF4 expression, account for the reduced level of embryonic receptors in long-term denervated muscle [6].

High impact information on Myog

  • Our data suggest that activation of myogenin gene expression and the establishment of the differentiated phenotype may require functional Myf-5 [7].
  • The present investigation provides evidence that E1a interferes with the expression of myogenin and the activity of Myf-5, the two myogenic helix-loop-helix (HLH) proteins that are expressed in L6 muscle cells [7].
  • The same inhibition by E1a can be shown for the other myogenic HLH proteins, MyoD, myogenin, and MRF4/Myf-6, that have been expressed in 10T1/2 fibroblasts [7].
  • The Pan/E12,E47 proteins also show structural similarity with the Drosophila daughterless protein, MyoD, Myogenin, and Myf-5 [8].
  • The virus converted cultured cardiac fibroblasts to skeletal muscle, indicated by expression of myogenin and skeletal myosin heavy chains (MHCs) [9].

Chemical compound and disease context of Myog


Biological context of Myog


Anatomical context of Myog

  • Myogenin is a member of the recently discovered family of muscle determination genes that have been shown to induce myogenic differentiation in nonmuscle cells and to be closely correlated with terminal differentiation in myoblasts [15].
  • Jun, Fos, MyoD1, and myogenin proteins are increased in skeletal muscle fiber nuclei after denervation [16].
  • Fos, MyoD1, and Myogenin immunoreactivity was mostly confined to muscle cell nuclei, whereas Jun antibodies stained muscle cell and some interstitial cell nuclei [16].
  • After 16 days of spaceflight, tibialis anterior, plantaris, medial gastrocnemius, and soleus muscles were removed from the hindlimb musculature and examined for the expression of MyoD-family transcription factors such as MyoD, myogenin, and MRF4 [17].
  • This growth inhibitory response is followed by cell commitment to terminal differentiation with elevated expression of myogenin muscle determination genes, induction of muscle-specific proteins, and formation of multinucleated myotubes [18].

Associations of Myog with chemical compounds


Regulatory relationships of Myog


Other interactions of Myog


Analytical, diagnostic and therapeutic context of Myog


  1. Repetitive stretch induces c-fos and myogenin mRNA within several hours in skeletal muscle removed from rats. Ikeda, S., Yoshida, A., Matayoshi, S., Tanaka, N. Archives of physical medicine and rehabilitation. (2003) [Pubmed]
  2. Retinoic acid induces myogenin synthesis and myogenic differentiation in the rat rhabdomyosarcoma cell line BA-Han-1C. Arnold, H.H., Gerharz, C.D., Gabbert, H.E., Salminen, A. J. Cell Biol. (1992) [Pubmed]
  3. Satellite cell proliferation and the expression of myogenin and desmin in regenerating skeletal muscle: evidence for two different populations of satellite cells. Rantanen, J., Hurme, T., Lukka, R., Heino, J., Kalimo, H. Lab. Invest. (1995) [Pubmed]
  4. Quantification of MyoD, myogenin, MRF4 and Id-1 by reverse-transcriptase polymerase chain reaction in rat muscles--effects of hypothyroidism and chronic low-frequency stimulation. Kraus, B., Pette, D. Eur. J. Biochem. (1997) [Pubmed]
  5. Na+ channel and acetylcholine receptor changes in muscle at sites distant from burns do not simulate denervation. Nosek, M.T., Martyn, J.A. J. Appl. Physiol. (1997) [Pubmed]
  6. Adaptation of nicotinic acetylcholine receptor, myogenin, and MRF4 gene expression to long-term muscle denervation. Adams, L., Carlson, B.M., Henderson, L., Goldman, D. J. Cell Biol. (1995) [Pubmed]
  7. Inhibition of muscle differentiation by the adenovirus E1a protein: repression of the transcriptional activating function of the HLH protein Myf-5. Braun, T., Bober, E., Arnold, H.H. Genes Dev. (1992) [Pubmed]
  8. Pan: a transcriptional regulator that binds chymotrypsin, insulin, and AP-4 enhancer motifs. Nelson, C., Shen, L.P., Meister, A., Fodor, E., Rutter, W.J. Genes Dev. (1990) [Pubmed]
  9. Muscle differentiation during repair of myocardial necrosis in rats via gene transfer with MyoD. Murry, C.E., Kay, M.A., Bartosek, T., Hauschka, S.D., Schwartz, S.M. J. Clin. Invest. (1996) [Pubmed]
  10. Myogenin, MyoD, and myosin expression after pharmacologically and surgically induced hypertrophy. Mozdziak, P.E., Greaser, M.L., Schultz, E. J. Appl. Physiol. (1998) [Pubmed]
  11. Gender related and dexamethasone induced differences in the mRNA levels of the MRF genes in rat anterior tibial skeletal muscle. te Pas, M.F., de Jong, P.R., Verburg, F.J., Duin, M., Henning, R.H. Mol. Biol. Rep. (1999) [Pubmed]
  12. Insulin-like growth factor-I stimulates terminal myogenic differentiation by induction of myogenin gene expression. Florini, J.R., Ewton, D.Z., Roof, S.L. Mol. Endocrinol. (1991) [Pubmed]
  13. Akt phosphorylation is not sufficient for insulin-like growth factor-stimulated myogenin expression but must be accompanied by down-regulation of mitogen-activated protein kinase/extracellular signal-regulated kinase phosphorylation. Tiffin, N., Adi, S., Stokoe, D., Wu, N.Y., Rosenthal, S.M. Endocrinology (2004) [Pubmed]
  14. Nerve activity-independent regulation of skeletal muscle atrophy: role of MyoD and myogenin in satellite cells and myonuclei. Hyatt, J.P., Roy, R.R., Baldwin, K.M., Edgerton, V.R. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  15. Highly specific inhibition of IGF-I-stimulated differentiation by an antisense oligodeoxyribonucleotide to myogenin mRNA. No effects on other actions of IGF-T. Florini, J.R., Ewton, D.Z. J. Biol. Chem. (1990) [Pubmed]
  16. Jun, Fos, MyoD1, and myogenin proteins are increased in skeletal muscle fiber nuclei after denervation. Weis, J. Acta Neuropathol. (1994) [Pubmed]
  17. Effects of microgravity on myogenic factor expressions during postnatal development of rat skeletal muscle. Inobe, M., Inobe, I., Adams, G.R., Baldwin, K.M., Takeda, S. J. Appl. Physiol. (2002) [Pubmed]
  18. Transforming growth factor beta induces myoblast differentiation in the presence of mitogens. Zentella, A., Massagué, J. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  19. Maturation of the myogenic program is induced by postmitotic expression of insulin-like growth factor I. Musarò, A., Rosenthal, N. Mol. Cell. Biol. (1999) [Pubmed]
  20. Phosphatidylinositol 3-kinase inhibitors block differentiation of skeletal muscle cells. Kaliman, P., Viñals, F., Testar, X., Palacín, M., Zorzano, A. J. Biol. Chem. (1996) [Pubmed]
  21. Alteration of the C-terminal amino acid of tubulin specifically inhibits myogenic differentiation. Chang, W., Webster, D.R., Salam, A.A., Gruber, D., Prasad, A., Eiserich, J.P., Bulinski, J.C. J. Biol. Chem. (2002) [Pubmed]
  22. Myogenic signaling by lithium in cardiomyoblasts is Akt independent but requires activation of the beta-catenin-Tcf/Lef pathway. Kashour, T., Burton, T., Dibrov, A., Amara, F. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  23. Cell adhesion to collagen and decreased myogenic gene expression implicated in the control of myogenesis by transforming growth factor beta. Heino, J., Massagué, J. J. Biol. Chem. (1990) [Pubmed]
  24. Activation of the skeletal alpha-actin promoter during muscle regeneration. Marsh, D.R., Carson, J.A., Stewart, L.N., Booth, F.W. J. Muscle Res. Cell. Motil. (1998) [Pubmed]
  25. Overexpression of calpastatin inhibits L8 myoblast fusion. Barnoy, S., Maki, M., Kosower, N.S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  26. Protein kinase C and calcium/calmodulin-activated protein kinase II (CaMK II) suppress nicotinic acetylcholine receptor gene expression in mammalian muscle. A specific role for CaMK II in activity-dependent gene expression. Macpherson, P., Kostrominova, T., Tang, H., Goldman, D. J. Biol. Chem. (2002) [Pubmed]
  27. Insulin-like growth factors require phosphatidylinositol 3-kinase to signal myogenesis: dominant negative p85 expression blocks differentiation of L6E9 muscle cells. Kaliman, P., Canicio, J., Shepherd, P.R., Beeton, C.A., Testar, X., Palacín, M., Zorzano, A. Mol. Endocrinol. (1998) [Pubmed]
  28. Fibroblast growth factor receptors display both common and distinct signaling pathways. Shaoul, E., Reich-Slotky, R., Berman, B., Ron, D. Oncogene (1995) [Pubmed]
  29. Myogenin and oxidative enzyme gene expression levels are elevated in rat soleus muscles after endurance training. Siu, P.M., Donley, D.A., Bryner, R.W., Alway, S.E. J. Appl. Physiol. (2004) [Pubmed]
  30. Vascular smooth muscle cells spontaneously adopt a skeletal muscle phenotype: a unique Myf5(-)/MyoD(+) myogenic program. Graves, D.C., Yablonka-Reuveni, Z. J. Histochem. Cytochem. (2000) [Pubmed]
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