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Proteomic analysis of bovine skeletal muscle hypertrophy
Author(s) -
Bouley Julien,
Meunier Bruno,
Chambon Christophe,
De Smet Stefaan,
Hocquette Jean François,
Picard Brigitte
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200400925
Subject(s) - myostatin , heterozygote advantage , muscle hypertrophy , myokine , biology , medicine , skeletal muscle , endocrinology , exon , semitendinosus muscle , phenotype , gene , genetics , genotype
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.