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ANIMAL GROWTH, PHYSIOLOGY, AND REPRODUCTION |





* Unité Qualité des Produits Animaux, INRA, 63122 St-Genès-Champanelle, France;
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Plateforme protéomique, INRA, 63122 St-Genès-Champanelle, France;
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Station dAmélioration Génétique des Animaux, INRA, 31326 Castanet-Tolosan, France;
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Unité de Génétique Moléculaire Animale, INRA-Université de Limoges, 87060 Limoges, France;
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# Département de Génétique, Faculté de Médicine Vétérinaire, Université de Liège, 43400 Liège, Belgium; and
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|| Institute of Animal Science, 2232 Kostinbrod, Bulgaria
2 Corresponding author: elaville{at}clermont.inra.fr
Two-dimensional electrophoresis was used to investigate the effects of a QTL for muscle hypertrophy on sarcoplasmic protein expression in ovine muscles. In the Belgian Texel breed, the QTL for muscle hypertrophy is localized in the myostatin-encoding gene. Based on microsatellite markers flanking the myostatin gene, we compared the hypertrophied genotype with the normal genotype. The average age of the sheep was 3 mo. Among the 4 muscles studied, in the hypertrophied genotype only the vastus medialis was normal, whereas the semimembranosus, tensor fasciae latae, and LM were hypertrophied. In the hypertrophied genotype, these muscles showed upregulation of enzymes involved in glycolytic metabolism together with oxidative metabolism in LM. Certain chaperone proteins, including glutathione S-transferase-Pi, heat shock protein-27, and heat shock cognate-70, were also more highly expressed, probably due to increased use of energetic pathways. Expression of the iron transport protein transferrin was increased. Alpha-1-antitrypsin was the only protein showing a similar pattern of expression (i.e., less expressed) in all 4 muscles of the hypertrophied genotype. It is suggested that transferrin and alpha-1-antitrypsin may interact to reinforce myogenic proliferative signaling.
Key Words:
1-antitrypsin myostatin sheep skeletal muscle sarcoplasmic protein transferrin
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