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Publications (6)16.87 Total impact

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    ABSTRACT: In agricultural sciences, proteomics has become the new hope for analyzing the meat quality traits that are closely related to the skeletal muscle traits. 2-DE muscle maps of many species have been recently reported and used to find molecular markers of meat quality traits. However, one limitation of 2-DE based analyses is due to the limited alkaline protein separation. Considering this problem, there is a need to use recent advances that have markedly improved the 2-DE based analysis of alkaline proteins. Hence, the present study provides additional information concerning the alkaline proteome of bovine skeletal muscle by using an appropriate protocol to characterize proteins over the entire range of pH 7-11. A total of 32 distinct gene products corresponding to 60 protein spots were identified by PMF and grouped in seven categories according to their main function. This 2-D map will contribute to muscle proteome studies since a significant portion of proteins is in the alkaline pH range.
    PROTEOMICS 05/2006; 6(8):2571-5. · 4.13 Impact Factor
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    ABSTRACT: The recent development of microarray technology has led statisticians and bioinformaticians to develop new statistical methodologies for comparing different biological samples. The objective is to identify a small number of differentially expressed genes from among thousands. In quantitative proteomics, analysis of protein expression using two-dimensional gel electrophoresis shows some similarities with transcriptomic studies. Thus, the goal of this study was to evaluate different data analysis methodologies widely used in array analysis using different proteomic data sets of hundreds of proteins. Even with few replications, the significance analysis of microarrays method appeared to be more powerful than the Student's t test in truly declaring differentially expressed proteins. This procedure will avoid wasting time due to false positives and losing information with false negatives.
    Analytical Biochemistry 06/2005; 340(2):226-30. · 2.58 Impact Factor
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    ABSTRACT: 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.
    PROTEOMICS 03/2005; 5(2):490-500. · 4.13 Impact Factor
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    ABSTRACT: The large individual variation in meat quality seen both within and between animals is not fully understood. Consequently, our long-term goal is to identify reliable proteins which control or determine bovine meat quality. Using a proteomic approach, bovine skeletal muscle samples were analyzed by two-dimensional gel electrophoresis (2-DE) using an immobilized pH 4-7 gradient in the first dimension and mass spectrometry. We first tested the reproducibility of the method. These experiments showed slightly greater intersample than intrasample variability. In order to evaluate the type of visualized proteins in 2-DE, we initiated the construction of a protein reference map of bovine Semitendinosus muscle. In total, 129 protein spots corresponding to 75 different gene products were identified. Of these proteins, the largest portion is involved in metabolism (25.5%), cell structure (17%), cell defense (16%) and contractile apparatus (14.5%). One quarter of the identified proteins are represented by two or several protein spots and multiple isoforms of troponin T are present. Peptide mass fingerprint results indicate that these isoforms are partly generated by alternative splicing. The data presented here are an important step for further proteome analyses on bovine muscle. This may lead to progress in understanding the mechanisms controlling postmortem muscle metabolism and meat quality.
    PROTEOMICS 07/2004; 4(6):1811-24. · 4.13 Impact Factor
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    ABSTRACT: Mutations in the myostatin gene lead to double-muscling in cattle indicating that it is a negative regulator of the total number of muscle fibres. Myostatin expression was analysed by RT-PCR in three developing bovine muscles. It decreased during differentiation in Semitendinosus and Biceps femoris, and increased in the late differentiating Masseter during gestation. A combination of in situ hybridisation and immuno-histochemical detection of myosin heavy chains (MHC) allowed us to locate the expression in myofibres containing only developmental MHC at different stages and in fast IIA fibres at the end of gestation. In vitro, myostatin was undetectable during proliferation, peaked at the onset of fusion and decreased during terminal differentiation. It was not detected in myotubes by in situ hybridisation. The inhibition of differentiation by BrdU prevented the decrease in expression. Our results show that the peak in myostatin expression coincides with early differentiation indicating a regulatory role in cattle myogenesis.
    Reproduction Nutrition Development 01/2003; 43(6):527-42. · 1.90 Impact Factor
  • J Bouley, C Chambon, B Picard
    Sciences Des Aliments - SCI ALIMENT. 01/2003; 23(1):75-78.