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MeSH Review

Pectoralis Muscles

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Disease relevance of Pectoralis Muscles

  • Body weight, pectoralis muscle weight, pectoralis protein and DNA concentration, and plasma GH and IGF-I concentrations of broiler chicks (BrBr), bantam chicks (BaBa) and reciprocal crosses between them (BaBr and BrBa) were measured between 0 and 42 days after hatching [1].
  • The peptide map obtained by electrophoresis after digestion of purified myosin heavy chains from pectoralis muscle of embryonic chicken with the Staphylococcus aureus V8 protease, produces a peptide pattern very similar but not identical to that of adult fast myosin [2].

High impact information on Pectoralis Muscles

  • It is specific for an adult fast myosin epitope that is not detected in early developing pectoralis muscle [3].
  • Monoclonal antibodies (McAbs) against the myosin heavy chain (MHC) of adult chicken pectoralis muscle have been tested for reactivity with pectoralis myosin at selected stages of chick development in vivo and in vitro [4].
  • This heterogeneity is mostly with regard to an ambiguity between adenine and guanine residues. tcRNA102 (obtained from pectoralis muscle) runs as a single band on denaturing acrylamide gels [5].
  • Brief exposure of cultured chicken pectoralis muscle cells to ionomycin or A23187 selectively increases the rate of incorporation of [35S]methionine into an 80,000-dalton protein was also observed upon cell-free translation of poly(A)-enriched RNA isolated from ionomycin-treated, as compared with control, cultures [6].
  • They show no cross-reactivity with any other myofibrillar protein of chicken pectoralis muscle, e.g. myosin, M-band proteins, titin or C-protein, nor did they exhibit a significant cross-reactivity with H-protein from rabbit [7].

Biological context of Pectoralis Muscles


Anatomical context of Pectoralis Muscles


Associations of Pectoralis Muscles with chemical compounds

  • The sequence of the NH2-terminal 808 amino acid residues of chicken pectoralis muscle myosin head was determined [18].
  • Two different C-protein variants which selectively react with either monoclonal anti-fast C-protein antibody (MF-1) or monoclonal anti-slow C-protein antibody (ALD-66) were separated from neonatal chicken pectoralis muscle by hydroxylapatite column chromatography [19].
  • Pyridoxal phosphate, the cofactor of the enzyme glycogen phosphorylase, was used as a specific label to measure the rate of degradation of the enzyme in the pectoralis muscle of growing broiler and layer chickens in vivo [20].
  • Supplementing with either methionine source resulted in significantly greater growth rate, efficiency of feed conversion, and accretion and synthesis of protein in the gastrocnemius and pectoralis muscles [21].
  • The ontogenesis of the nuclear triiodothyronine receptors was determined in the pectoralis muscle of male and female chicken at 18 days in ovo and 0, 3, 6, 14 and 35 days ex ovo [22].

Gene context of Pectoralis Muscles


Analytical, diagnostic and therapeutic context of Pectoralis Muscles


  1. Posthatching growth and pectoralis muscle development in broiler strain chickens, bantam chickens and the reciprocal crosses between them. Mitchell, R.D., Burke, W.H. Growth, development, and aging : GDA. (1995) [Pubmed]
  2. Myosin heavy chains in fast skeletal muscle of chick embryo. Dalla Libera, L. Experientia (1981) [Pubmed]
  3. Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis. Winkelmann, D.A., Lowey, S., Press, J.L. Cell (1983) [Pubmed]
  4. 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]
  5. Analysis of tcRNA102 associated with myosin heavy chain-mRNPs in control and dystrophic chick pectoralis muscle. Zezza, D.J., Heywood, S.M. J. Biol. Chem. (1986) [Pubmed]
  6. Selective stimulation of the synthesis of an 80,000-dalton protein by calcium ionophores. Wu, F.S., Park, Y.C., Roufa, D., Martonosi, A. J. Biol. Chem. (1981) [Pubmed]
  7. Novel thick filament protein of chicken pectoralis muscle: the 86 kd protein. I. Purification and characterization. Bähler, M., Eppenberger, H.M., Wallimann, T. J. Mol. Biol. (1985) [Pubmed]
  8. Structure of myosin heavy chain in avian muscular dystrophy. Huszar, G., Vigue, L., DeLucia, J., Elzinga, M., Haines, J. J. Biol. Chem. (1985) [Pubmed]
  9. Comparison of chicken genotypes: myofiber number in pectoralis muscle and myostatin ontogeny. Scheuermann, G.N., Bilgili, S.F., Tuzun, S., Mulvaney, D.R. Poult. Sci. (2004) [Pubmed]
  10. Effect of vitamin E and selenium on resistance to oxidative stress in chicken superficial pectoralis muscle. Avanzo, J.L., de Mendonça, C.X., Pugine, S.M., de Cerqueira Cesar, M. Comp. Biochem. Physiol. C Toxicol. Pharmacol. (2001) [Pubmed]
  11. Influence of experimental hypothyroidism on chick myogenesis. Bacou, F., Jallageas, M., Nougues, J., Vigneron, P. Reproduction, nutrition, development. (1980) [Pubmed]
  12. Myostatin and TGF-beta2 gene expression patterns in response to in ovo administration of rhIGF-I during chicken embryonic development. Kocamis, H., Gahr, S.A., Richter, J., Kirkpatrick-Keller, D.C., Killefer, J. Growth, development, and aging : GDA. (2002) [Pubmed]
  13. An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments. Woodhead, J.L., Lowey, S. J. Mol. Biol. (1983) [Pubmed]
  14. Expression of fast myosin heavy chain transcripts in developing and dystrophic chicken skeletal muscle. Tidyman, W.E., Moore, L.A., Bandman, E. Dev. Dyn. (1997) [Pubmed]
  15. Ultrastructural localization of acetylcholinesterase in cultured cells. III. DFP treated embryo muscle. Golder, T.K., Nieberg, P.S., Wilson, B.W. J. Histochem. Cytochem. (1978) [Pubmed]
  16. Effect of exogenous chicken growth hormone (cGH) administration on insulin-like growth factor-I (IGF-I) gene expression in domestic fowl. Rosselot, G., McMurtry, J.P., Vasilatos-Younken, R., Czerwinski, S. Mol. Cell. Endocrinol. (1995) [Pubmed]
  17. Thyroidal influence on the lactate dehydrogenase isozyme pattern in pectoralis muscle of chick embryos. Lippe, M.S., Gassman, J.I., Soltoff, S.P., King, D.B. Gen. Comp. Endocrinol. (1977) [Pubmed]
  18. The primary structure of the myosin head. Maita, T., Hayashida, M., Tanioka, Y., Komine, Y., Matsuda, G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  19. Coexistence of fast-type and slow-type C-proteins in neonatal chicken breast muscle. Obinata, T., Kitani, S., Masaki, T., Fischman, D.A. Dev. Biol. (1984) [Pubmed]
  20. Turnover of glycogen phosphorylase in the pectoralis muscle of broiler and layer chickens. Flannery, A.V., Easterby, J.S., Beynon, R.J. Biochem. J. (1992) [Pubmed]
  21. Methionine deficiency decreases protein accretion and synthesis but not tRNA acylation in muscles of chicks. Barnes, D.M., Calvert, C.C., Klasing, K.C. J. Nutr. (1995) [Pubmed]
  22. Perinatal age and sex variations of the triiodothyronine nuclear receptors in the chick pectoralis major muscle. Dainat, J., Bressot, C., Bacou, F., Rebière, A., Vigneron, P. Mol. Cell. Endocrinol. (1984) [Pubmed]
  23. IGF-I, IGF-II, and IGF-receptor-1 transcript and IGF-II protein expression in myostatin knockout mice tissues. Kocamis, H., Gahr, S.A., Batelli, L., Hubbs, A.F., Killefer, J. Muscle Nerve (2002) [Pubmed]
  24. Increased expression of cofilin in dystrophic chicken and mouse skeletal muscles. Hayakawa, K., Minami, N., Ono, S., Ogasawara, Y., Totsuka, T., Abe, H., Tanaka, T., Obinata, T. J. Biochem. (1993) [Pubmed]
  25. Skin necrosis of a pectoralis major myocutaneous flap, caused by methicillin-resistant Staphylococcus aureus. Ethunandan, M., Ansell, M., Mellor, T.K., Brennan, P.A. The British journal of oral & maxillofacial surgery. (2004) [Pubmed]
  26. Expression of phospholamban mRNA during early avian muscle morphogenesis is distinct from that of alpha-actin. Toyofuku, T., Doyle, D.D., Zak, R., Kordylewski, L. Dev. Dyn. (1993) [Pubmed]
  27. Ultrastructural localization of M-band proteins in chicken breast muscle as revealed by combined immunocytochemistry and ultramicrotomy. Strehler, E.E., Carlsson, E., Eppenberger, H.M., Thornell, L.E. J. Mol. Biol. (1983) [Pubmed]
  28. A radioimmunoassay for human serum myoglobin: method development and normal values. Rosano, T.G., Kenny, M.A. Clin. Chem. (1977) [Pubmed]
  29. Electron microscopy of C-protein molecules from chicken skeletal muscle. Swan, R.C., Fischman, D.A. J. Muscle Res. Cell. Motil. (1986) [Pubmed]
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