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

• We have also examined the amino acid sequence of a 3-methyl-histidine-containing peptide which originates from the 20-kDa fragment of pectoralis muscle MHC in dystrophic chicks: Val-Leu-Asn-Ala-Ser-Ala-Ile-Pro-Glu-Gly-*Gln-Phe-*Ile-Asp-Ser-Lys-Lys- Ala-Ser-Leu-Gln-Lys-Leu-Gly-Ser-Ile-Asp-Val-(Asp, 3-methylhistidine, Gln) [8].
• Comparison of chicken genotypes: myofiber number in pectoralis muscle and myostatin ontogeny [9].
• Effect of vitamin E and selenium on resistance to oxidative stress in chicken superficial pectoralis muscle [10].
• Aldolase (glycolytic) and NADP isocitrate dehydrogenase (tricarboxylic acid cycle) activities, measured on the adductor and pectoralis muscles, showed a similar developmental pattern in control and treated animals, but was retarded in the latter due to a 5-day delay in hatching [11].
• TGF-beta2 gene expression from in ovo rhIGF-I treated pectoralis muscles dramatically increased at E 13 (approximately 2.5 fold), in contrast to E 14 from control pectoralis muscle, and gradually declined through E 16 [12].

Anatomical context of Pectoralis Muscles

• We have isolated and purified these proteins from adult chicken pectoralis muscle, and have studied their in vitro interactions with myosin, heavy meromyosin, light meromyosin and subfragment-2 in order to obtain a fuller understanding of the role these proteins play in the M-band of skeletal muscle [13].
• The expression of MyHC genes was also studied in muscle cell cultures derived from 12-day embryonic pectoralis muscles [14].
• In normal 10 day cultures of embryo pectoralis muscles AChE is localized in the nuclear envelope, perinuclear sarcoplasm, sarcotubular system, subsurface vesicles and bound outside the cells [15].
• Steady-state IGF-I mRNA abundance was determined by a solution hybridization nuclease protection assay using total cellular RNA obtained from liver, heart, kidney, spleen, epiphyseal growth plate cartilage, gastrocnemius and pectoralis muscles [16].
• Thyroidal influence on the lactate dehydrogenase isozyme pattern in pectoralis muscle of chick embryos [17].

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

• IGF-R1 mRNA levels from control mice heart (P <.05) and kidney (P <.01) were significantly higher than in myostatin knockout mice, whereas levels were lower in pectoralis muscle of control mice than knockout mice (P <.01) [23].
• Since cofilin expression is down-regulated during normal postnatal development of skeletal muscles [Abe et al. (1989) J. Biochem. 106, 696-702], cofilin was detected in the breast (pectoralis) muscle of normal adult chicken and the leg (femoris and tibialis anterior) muscles of normal mice only at a low level [24].
• A case of MRSA-induced skin necrosis of part of a pectoralis muscle flap is described [25].
• Moreover, no phospholamban mRNA was detected in primary cultures derived from pectoralis muscle of the same age [26].
• Northern blot analysis of embryonic day 11 chick fast pectoralis muscle showed that phospholamban mRNA was not detected in vivo while alpha-cardiac actin mRNA was [26].

Analytical, diagnostic and therapeutic context of Pectoralis Muscles

• Cryo-ultramicrotomy and "conventional" plastic sectioning have been used in combination with extraction and immunolabeling techniques to determine the location of the two M-band proteins characterized to date, MM-creatine kinase (MM-CK: Mr, 80,000) and M-protein "myomesin" (Mr, 165,000) within the M-region of chicken pectoralis muscle [27].
• Myoglobin isolated from human pectoralis muscle was purified by (NH4)2SO4 fractionation and Sephadex gel filtration and injected into rabbits to elicit antisera [28].
• C-protein from chicken pectoralis muscle has been purified by sequential DEAE-Sephadex and hydroxyapatite chromatography and examined by transmission electron microscopy after spraying in glycerol onto mica and replicating by rotary shadowing with platinum [29].

References