Denervation of Chicken Skeletal Muscle Causes an Increase in Acetylcholinesterase mRNA Synthesis

cDNA encoding Ca2+-ATPase was cloned from a chicken skeletal muscle library. The cDNA (termed FCa) comprised 3,239 base pairs, including an open reading frame encoding 994 amino acids which showed the highest degree of homology with the adult rabbit fast-twitch Ca2+-ATPase isoform (C. J. Brandl, S. de Leon, D. R. Martin, and D. H. MacLennan, J. Biol. Chem. 262:3768-3774, 1987). Radiolabeled FCa hybridized to a 3.2-kilobase transcript in chicken skeletal muscle RNA but not to cardiac muscle RNA, which confirmed its identity as encoding the fast Ca2+-ATPase isoenzyme. FCa was transfected into the mouse myogenic line C2C12, from which a protein of 100 kilodaltons was immunopurified by using a monoclonal antibody specific for the avian fast Ca2+-ATPase. Immunofluorescence microscopy of a line (designated C2FCa2) stably expressing the avian Ca2+-ATPase localized the protein to the nuclear envelope and a population of cytoplasmic vesicles. A similar pattern was observed when C2FCa2 cells were stained with DiOC6(3), a cyanine dye that labels endoplasmic reticulum and mitochondria (M. Terasaki, J. Song, J. R. Wong, M. J. Weiss, and L. B. Chen, Cell 38:101-108, 1984). We conclude that the avian Ca2+-ATPase fast isoform is expressed and correctly targeted to the endoplasmic reticulum in mouse C2C12 cells.

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The chicken skeletal muscle alpha-actin promoter is tissue specific in transgenic mice

Molecular and Cellular Biology ◽

10.1128/mcb.9.9.3785-3792.1989 ◽

1989 ◽

Vol 9 (9) ◽

pp. 3785-3792

Author(s):

C J Petropoulos ◽

M P Rosenberg ◽

N A Jenkins ◽

N G Copeland ◽

S H Hughes

Keyword(s):

Skeletal Muscle ◽

Transgenic Mice ◽

Striated Muscle ◽

Transcriptional Start Site ◽

Actin Gene ◽

Tissue Specific ◽

Adult Mice ◽

Transgenic Lines ◽

Alpha Actin ◽

Chicken Skeletal Muscle

We have generated transgenic mouse lines that carry the promoter region of the chicken skeletal muscle alpha (alpha sk) actin gene linked to the bacterial chloramphenicol acetyltransferase (CAT) gene. In adult mice, the pattern of transgene expression resembled that of the endogenous alpha sk actin gene. In most of the transgenic lines, high levels of CAT activity were detected in striated muscle (skeletal and cardiac) but not in the other tissues tested. In striated muscle, transcription of the transgene was initiated at the normal transcriptional start site of the chicken alpha sk actin gene. The region from nucleotides -191 to +27 of the chicken alpha sk actin gene was sufficient to direct the expression of CAT in striated muscle of transgenic mice. These observations suggest that the mechanism of tissue-specific actin gene expression is well conserved in higher vertebrate species.

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Mitochondrial Oxidative Damage in Chicken Skeletal Muscle Induced by Acute Heat Stress

The Journal of Poultry Science ◽

10.2141/jpsa.44.439 ◽

2007 ◽

Vol 44 (4) ◽

pp. 439-445 ◽

Cited By ~ 99

Author(s):

Ahmad Mujahid ◽

Neil R. Pumford ◽

Walter Bottje ◽

Kiyotaka Nakagawa ◽

Teruo Miyazawa ◽

...

Keyword(s):

Skeletal Muscle ◽

Heat Stress ◽

Oxidative Damage ◽

Acute Heat Stress ◽

Mitochondrial Oxidative Damage ◽

Chicken Skeletal Muscle

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The complete amino acid sequence of chicken skeletal-muscle enolase

Biochemical Journal ◽

10.1042/bj2360115 ◽

1986 ◽

Vol 236 (1) ◽

pp. 115-126 ◽

Cited By ~ 17

Author(s):

G A Russell ◽

B Dunbar ◽

L A Fothergill-Gilmore

Keyword(s):

Skeletal Muscle ◽

Amino Acid ◽

Amino Acid Sequence ◽

Peptide Bond ◽

Peptide Bonds ◽

Complete Amino Acid Sequence ◽

Arginine Residues ◽

Cnbr Cleavage ◽

Yeast Enolase ◽

Chicken Skeletal Muscle

The complete amino acid sequence of chicken skeletal-muscle enolase, comprising 433 residues, was determined. The sequence was deduced by automated sequencing of hydroxylamine-cleavage, CNBr-cleavage, o-iodosobenzoic acid-cleavage, clostripain-digest and staphylococcal-proteinase-digest fragments. The presence of several acid-labile peptide bonds and the tenacious aggregation of most CNBr-cleavage fragments meant that a commonly used sequencing strategy involving initial CNBr cleavage was unproductive. Cleavage at the single Asn-Gly peptide bond with hydroxylamine proved to be particularly useful. Comparison of the sequence of chicken enolase with the two yeast enolase isoenzyme sequences shows that the enzyme is strongly conserved, with 60% of the residues identical. The histidine and arginine residues implicated as being important for the activity of yeast enolase are conserved in the chicken enzyme. Secondary-structure predictions are analysed in an accompanying paper [Sawyer, Fothergill-Gilmore & Russell (1986) Biochem. J. 236, 127-130].

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