Electrophoretic separation of bovine muscle myosin heavy chain isoforms

Picard, Brigitte; Barboiron, Christiane; Duris, M.P.; Gagnière, Hélène; Jurie, Catherine; Geay, Y.

doi:10.1016/s0309-1740(99)00021-2

Cited by 41 publications

(42 citation statements)

References 32 publications

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“…A third band in the fast isoforms, namely MyHC IIb, sometimes described in bovine muscle (Picard et al, 1999), has not been revealed in these samples. At 8 months of age, cloned heifers had a greater proportion of MyHC I and MyHC IIa isoforms (13.9% v. 6.9% P 5 0.0008 and 27.9% v. 16.3% P , 0.0001, respectively) and a lower proportion of the MyHC IIx isoform (58.2% v. 76.8% P , 0.0001) compared with control heifers (Figure 2).…”

Section: Contractile Characteristicsmentioning

confidence: 67%

“…Chikuni et al (2004) demonstrated that the MyHC IIb gene is present in bovine genome but not expressed. This indicates that fibres classified IIB by conventional histochemical (Picard et al, 1999). During early postnatal growth (up to about 6 months of age), there is a conversion in fibre types, namely from fast oxido-glycolytic fibres (type FOG or IIA) into fast glycolytic fibres (type FG or IIX), which indicates a modification of muscle metabolism (Jurie et al, 1995;Wegner et al, 2000).…”

Section: Discussionmentioning

confidence: 95%

“…The contractile muscle type was determined in all samples by quantifying the different myosin heavy chain (MyHC) isoforms that were separated by electrophoresis SDS-PAGE according to the method of Picard et al (1999). Each well of gel was loaded with 3 mg of myofibrillar protein.…”

Section: Contractile Characteristicsmentioning

confidence: 99%

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Comparison of cloned and non-cloned Holstein heifers in muscle contractile and metabolic characteristics

Jurie

Picard

Heyman

et al. 2009

Animal

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Muscle contractile and metabolic characteristics were studied on nine cloned and eight non-cloned (control) heifers. The animals were submitted to repeated biopsies of the semitendinosus (ST) muscle at the ages of 8, 12, 18 and 24 months. The contractile type was determined from the proportion of the different myosin heavy chain (MyHC) isoforms separated by electrophoresis. Glycolytic metabolism was assessed by lactate dehydrogenase (LDH) activity, and oxidative metabolism was assessed by isocitrate dehydrogenase (ICDH), cytochrome-c oxidase (COX) and b-hydroxyacyl-CoA dehydrogenase (HAD) activities. In cloned heifers at 8 months of age, there was a greater proportion of MyHC I (slow oxidative isoform) and MyHC IIa (fast oxido-glycolytic isoform), a lower proportion of MyHC IIx (fast glycolytic isoform), greater COX and HAD activity and a lower LDH/ICDH ratio compared with control heifers. Thus, young cloned heifers had slower muscle types associated with a more oxidative muscular metabolism than control heifers. From 12 months of age onwards, no significant differences were observed between cloned and control heifers. A delay in muscle differentiation and maturation in cloned heifers is hypothesised and discussed.

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Section: Contractile Characteristicsmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 95%

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Comparison of cloned and non-cloned Holstein heifers in muscle contractile and metabolic characteristics

Jurie

Picard

Heyman

et al. 2009

Animal

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“…The young bulls were slaughtered at 17 months of age on average and the steers at 30 months of age on average at the INRA experimental slaughterhouse in compliance with current ethical guidelines for animal welfare. Muscle samples from the Longissimus thoracis (LT; fast oxido-glycolytic with 25% of myosins of heavy chains I (MyHC-I), 62% of MyHC-IIa and 13% of MyHC-IIx in our experiment by electrophoresis (Picard et al, 1999), and in accordance with Jurie et al (1995Jurie et al ( , 2007 in bovine) and Semitendinosus (ST; fast glycolytic with 11% of MyHC-I, 24% of MyHC-IIa and 66% of MyHC-IIx in our experiment, and in accordance with Schreurs et al (2008) in bovine) muscles were excised for each animal within 15 min after slaughter. Muscle samples were immediately frozen in liquid nitrogen and stored at 2808C until protein extraction.…”

Section: Animals and Samplesmentioning

confidence: 99%

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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Some proteins have been revealed as biomarkers for beef tenderness by previous studies. These markers could be used in immunological tests to predict beef tenderness, in living animals as well as in carcasses. It is well known that rearing practices modify the amounts of mRNA and proteins. Therefore, the reliability of protein tests could be affected by livestock and biological effects such as production systems, breed, muscle and animal type. This study analysed the effects of animal and muscle type on 24 proteins. The animals studied were 67 young bulls and 44 steers of the Charolais breed, and muscles were Longissimus thoracis and Semitendinosus. Protein amounts were determined by Dot blot, an immunological technique. Results showed that expressions of 20 proteins were influenced by animal and/or muscle type. These results could lead to modifications and adaptations of prediction tests according to rearing practice, bovine breed and beef cut.

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“…Llama also expressed three fast MyHC isoforms, judging from protein analysis (Graziotti et al , 2001). However, the bovine muscle showed no MyHC-2b expression through the RT-PCR analysis (Chikuni et al , 2004), although the presence of three bands for the fast MyHC isoforms was reported on the SDS-PAGE experiment (Picard et al ., 1999). Equine skeletal muscle did not express the MyHC-2b isoform at the protein level (Rivero et al , 1999), and there is no evidence at the DNA level.…”

Section: Introductionmentioning

confidence: 99%

Absence of the Functional Myosin Heavy Chain 2b Isoform in Equine Skeletal Muscles

2004

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Electrophoretic separation of bovine muscle myosin heavy chain isoforms

Cited by 41 publications

References 32 publications

Comparison of cloned and non-cloned Holstein heifers in muscle contractile and metabolic characteristics

Comparison of cloned and non-cloned Holstein heifers in muscle contractile and metabolic characteristics

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Absence of the Functional Myosin Heavy Chain 2b Isoform in Equine Skeletal Muscles

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