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AMHC1  -  myosin heavy chain

Gallus gallus

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Disease relevance of AMHC1


High impact information on AMHC1


Chemical compound and disease context of AMHC1


Biological context of AMHC1


Anatomical context of AMHC1

  • AMHC1 is first activated in the posterior segment of the heart when these myocytes initially differentiate (Hamburger and Hamilton stage 9+) [11].
  • The early activation of AMHC1 expression in the posterior cardiac myocytes suggests that the heart cells are diversified when they differentiate initially and that the anterior heart progenitors differ from the posterior heart progenitors in their myosin isoform gene expression [11].
  • Messenger RNA which stimilates the synthesis of myosin heavy chain in a reticulocyte lysate has been isolated from single myogenic cell cultures [14].
  • Lower concentrations of diazepam allow cell fusion to occur, but inhibit the synthesis and accumulation of myosin heavy chain, implying that cell fusion does not obligate myoblasts to synthesize and accumulate large quantities of muscle specific protein [15].
  • Furthermore, if mature cultures that reacted with the neonatal antibody were placed into high [K+] medium, neonatal MHC disappeared from virtually all myotubes within 3 d [16].

Associations of AMHC1 with chemical compounds

  • Embryos treated with retinoic acid prior to the initiation of fusion of the heart primordia express AMHC1 throughout the entire heart-forming region and fusion of the heart primordia is inhibited [11].
  • The guanidine denatured myosin heavy chain fragments were either dialyzed or diluted into renaturation buffer and reformed dimers which were electrophoretically indistinguishable from native rods [17].
  • In contrast, no change in creatine phosphokinase activity, myosin heavy chain content, or [35S] methionine incorporation into total cellular protein was observed during cholera toxin treatment [18].
  • The MHC CNBr peptides were analyzed by one-dimensional and two-dimensional isoelectric focusing/sodium dodecyl sulfate gradient gels and by amino acid sequencing [2].
  • MHC was alkylated with N-ethylmaleimide, purified by Sepharose-4B chromatography, and cleaved with cyanogen bromide [2].

Physical interactions of AMHC1


Regulatory relationships of AMHC1

  • Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains [21].

Other interactions of AMHC1


Analytical, diagnostic and therapeutic context of AMHC1


  1. Developmental modulation of myosin expression by thyroid hormone in avian skeletal muscle. Gardahaut, M.F., Fontaine-Perus, J., Rouaud, T., Bandman, E., Ferrand, R. Development (1992) [Pubmed]
  2. Structure of myosin heavy chain in avian muscular dystrophy. Huszar, G., Vigue, L., DeLucia, J., Elzinga, M., Haines, J. J. Biol. Chem. (1985) [Pubmed]
  3. Functional consequences of mutations in the smooth muscle myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy. Yamashita, H., Tyska, M.J., Warshaw, D.M., Lowey, S., Trybus, K.M. J. Biol. Chem. (2000) [Pubmed]
  4. Segregated assembly of muscle myosin expressed in nonmuscle cells. Moncman, C.L., Rindt, H., Robbins, J., Winkelmann, D.A. Mol. Biol. Cell (1993) [Pubmed]
  5. Ventricular myosin light chain 1 is developmentally regulated and does not change in hypertension. McNally, E.M., Buttrick, P.M., Leinwand, L.A. Nucleic Acids Res. (1989) [Pubmed]
  6. Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Soldati, T., Perriard, J.C. Cell (1991) [Pubmed]
  7. Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis. Winkelmann, D.A., Lowey, S., Press, J.L. Cell (1983) [Pubmed]
  8. Myosin heavy chains from two different adult fast-twitch muscles have different peptide maps but identical mRNAs. Bandman, E., Matsuda, R., Strohman, R.C. Cell (1982) [Pubmed]
  9. The genes and mRNA coding for the heavy chains of chick embryonic skeletal myosin. Patrinou-Georgoulas, M., John, H.A. Cell (1977) [Pubmed]
  10. A monoclonal antibody to the embryonic myosin heavy chain of rat skeletal muscle. Gambke, B., Rubinstein, N.A. J. Biol. Chem. (1984) [Pubmed]
  11. Expression of the atrial-specific myosin heavy chain AMHC1 and the establishment of anteroposterior polarity in the developing chicken heart. Yutzey, K.E., Rhee, J.T., Bader, D. Development (1994) [Pubmed]
  12. Molecular characterization of a novel atrial-specific myosin heavy-chain gene expressed in the chick embryo. Oana, S., Matsuoka, R., Nakajima, H., Hiratsuka, E., Furutani, Y., Takao, A., Momma, K. Eur. J. Cell Biol. (1995) [Pubmed]
  13. The essential light chains constitute part of the active site of smooth muscle myosin. Okamoto, Y., Sekine, T., Grammer, J., Yount, R.G. Nature (1986) [Pubmed]
  14. Messenger RNA for myosin polypeptides: isolation from single myogenic cell cultures. Strohman, R.C., Moss, P.S., Micou-Eastwood, J., Spector, D., Przybyla, A., Paterson, B. Cell (1977) [Pubmed]
  15. Diazepam inhibits myoblast fusion and expression of muscle specific protein synthesis. Bandman, E., Walker, C.R., Strohman, R.C. Science (1978) [Pubmed]
  16. Contractile activity is required for the expression of neonatal myosin heavy chain in embryonic chick pectoral muscle cultures. Cerny, L.C., Bandman, E. J. Cell Biol. (1986) [Pubmed]
  17. Assembly of avian skeletal muscle myosins: evidence that homodimers of the heavy chain subunit are the thermodynamically stable form. Kerwin, B., Bandman, E. J. Cell Biol. (1991) [Pubmed]
  18. Regulation of acetylcholine receptor by cyclic AMP. Blosser, J.C., Appel, S.H. J. Biol. Chem. (1980) [Pubmed]
  19. Axial arrangement of the myosin rod in vertebrate thick filaments: immunoelectron microscopy with a monoclonal antibody to light meromyosin. Shimizu, T., Dennis, J.E., Masaki, T., Fischman, D.A. J. Cell Biol. (1985) [Pubmed]
  20. An M-CAT binding factor and an RSRF-related A-rich binding factor positively regulate expression of the alpha-cardiac myosin heavy-chain gene in vivo. Molkentin, J.D., Markham, B.E. Mol. Cell. Biol. (1994) [Pubmed]
  21. Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains. Katsuragawa, Y., Yanagisawa, M., Inoue, A., Masaki, T. Eur. J. Biochem. (1989) [Pubmed]
  22. Differentiation of cardiac Purkinje fibers requires precise spatiotemporal regulation of Nkx2-5 expression. Harris, B.S., Spruill, L., Edmonson, A.M., Rackley, M.S., Benson, D.W., O'Brien, T.X., Gourdie, R.G. Dev. Dyn. (2006) [Pubmed]
  23. Ectopic insulin-like growth factor I expression in avian skeletal muscle prevents expression of CMD4, a novel inhibitor of differentiation. Winner, D.G., Ealy, A.D., Hannon, K., Johnson, S.E. Domest. Anim. Endocrinol. (2006) [Pubmed]
  24. Slow and fast myosin heavy chain content defines three types of myotubes in early muscle cell cultures. Miller, J.B., Crow, M.T., Stockdale, F.E. J. Cell Biol. (1985) [Pubmed]
  25. Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms. Matsuda, R., Spector, D.H., Strohman, R.C. Dev. Biol. (1983) [Pubmed]
  26. Developmentally regulated slow troponin C messenger RNA in chicken skeletal and cardiac muscles. Berezowsky, C., Bag, J. Biochem. Cell Biol. (1988) [Pubmed]
  27. Continued expression of neonatal myosin heavy chain in adult dystrophic skeletal muscle. Bandman, E. Science (1985) [Pubmed]
  28. Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro. Bader, D., Masaki, T., Fischman, D.A. J. Cell Biol. (1982) [Pubmed]
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