Details

Autor(en) / Beteiligte

• Bouley, Julien
• Meunier, Bruno
• Chambon, Christophe
• De Smet, Stefaan
• Hocquette, Jean François
• Picard, Brigitte

Titel

Proteomic analysis of bovine skeletal muscle hypertrophy

Ist Teil von

• Proteomics (Weinheim), 2005-02, Vol.5 (2), p.490-500

Ort / Verlag

Weinheim: WILEY-VCH Verlag

Erscheinungsjahr

2005

Quelle

MEDLINE

Beschreibungen/Notizen

• Myostatin plays a major role in muscle growth and development and animals with disruption of this gene display marked increases in muscle mass. Little is known about muscle physiological adaptations in relation to this muscle hypertrophy. To provide a more comprehensive view, we analyzed bovine muscles from control, heterozygote and homozygote young Belgian blue bulls for myostatin deletion, which results in a normal level of inactive myostatin. Heterozygote and homozygote animals were characterized by a higher proportion of fast‐twitch glycolytic fibers in Semitendinosus muscle. Differential proteomic analysis of this muscle was performed using two‐dimensional gel electrophoresis followed by mass spectrometry. Thirteen proteins, corresponding to 28 protein spots, were significantly altered in response to the myostatin deletion. The observed changes in protein expression are consistent with an increased fast muscle phenotype, suggesting that myostatin negatively controls mainly fast‐twitch glycolytic fiber number. Finally, we demonstrated that differential mRNA splicing of fast troponin T is altered by the loss of myostatin function. The structure of mutually exclusive exon 16 appears predominantly expressed in muscles from heterozygote and homozygote animals. This suggests a role for exon 16 of fast troponin T in the physiological adaptation of the fast muscle phenotype.