7 research outputs found

    Ractopamine-induced changes in sarcoplasmic proteome profile of post-rigor pork semimembranosus muscle

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    Ractopamine is a beta-adrenergic agonist that increases leanness and carcass weight in finishing pigs. Our previous study observed that dietary ractopamine increased the abundance of several glycolytic enzymes in the sarcoplasmic proteome of post-rigor pork longissimus thoracis muscle. Pork semimembranosus is an economically important muscle and demonstrates differences in biochemistry compared with longissimus thoracis. Nonetheless, the effects of ractopamine on sarcoplasmic proteome of semimembranosus have not been evaluated yet. Therefore, this study examined the influence of ractopamine on sarcoplasmic proteome of post-rigor pork semimembranosus. Analyses of sarcoplasmic proteome of semimembranosus muscles from control (CON; diet without ractopamine) and ractopamine-fed (RAC; 7.4 mg/kg for 14 days followed by 10.0 mg/kg for 14 days) barrows revealed that haemoglobin subunit beta, alpha-crystallin B, and titin fragments were over-abundant in CON. In contrast, myosin light chain 1/3 and tripartite motif-containing protein 72 were over-abundant in RAC. The low abundance of haemoglobin subunit beta and alpha crystallin B in RAC could be attributed to fibre type shift (from oxidative to glycolytic) in response to ractopamine. The over-abundance of MLC 1/3 and tripartite motif-containing protein 72 in RAC could be due to the increased myofibrillar protein synthesis and muscle mass in ractopamine-fed pigs. Dietary ractopamine decreased the abundance of sarcoplasmic proteins involved in oxygen transport and chaperone activity, but increased the abundance of proteins involved in muscle contraction and plasma membrane repair in pork semimembranosus muscle.Keywords: Pork, ractopamine, sarcoplasmic proteome, semimembranosu

    Supranutritional supplementation of vitamin E influences mitochondrial proteome profile of post-mortem longissimus lumborum from feedlot heifers

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    Supplementation of vitamin E improves beef colour stability by minimizing lipid oxidation-induced myoglobin oxidation. Mitochondria affect myoglobin redox stability, and dietary vitamin E influences mitochondrial functionality in skeletal muscles. Nonetheless, the influence of vitamin E on the mitochondrial proteome of beef skeletal muscles has yet to be  investigated. Therefore, the objective of this study was to examine the effect of dietary vitamin E on mitochondrial proteome of post-mortem beef longissimus lumborum (LL) muscle. Beef LL muscle samples (24 hours post-mortem) were obtained from the carcasses of nine (n = 9) vitamin E-fed (VITE) (1000 IU vitamin E for 89 days) and nine (n = 9) control (CONT) (diet without supplemental vitamin E) heifers. The mitochondrial proteome was analysed using two-dimensional gel electrophoresis and mass spectrometry, and nine differentially abundant spots were identified. All the differentially abundant spots were over-abundant in CONT, and the proteins were electron transport chain enzymes (NADH dehydrogenase iron-sulphur protein 8, NADH dehydrogenase flavoprotein 2, and cytochrome c oxidase subunit 5B), metabolic enzymes (succinate-CoA ligase (ADP-forming) subunit beta; dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; pyruvate dehydrogenase protein X component), and enzymes involved in ATP regeneration (creatine kinase S-type). The low abundance of these proteins in VITE may decrease mitochondrial activity, resulting in low oxidative activity. These findings suggest that the strong antioxidant activity of vitamin E leads to less expression of mitochondrial oxidative enzymes in beef skeletal muscles.Keywords: Beef colour, lipid oxidation, mitochondrial enzyme

    Ractopamine-induced changes in the proteome of post-mortem beef longissimus lumborum muscle

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    Ractopamine is a beta-adrenergic agonist that is approved for use in beef cattle, pigs and turkeys as a repartitioning agent to increase lean muscle deposition and decrease lipogenesis. Although the effects of dietary ractopamine on the proteome profile of post-mortem pork muscles have been examined, its influence on beef muscle proteome has not been studied. Therefore, the objective of this study was to examine the effect of ractopamine on the proteome profile of post-mortem beef longissimus lumborum (LL) muscle. LL muscle samples were obtained from the carcasses of six (n = 6) steers fed ractopamine (RAC; 400 mg ractopamine hydrochloride for 28 days) and six (n = 6) steers fed no ractopamine (CON). The muscle proteome was analysed using two-dimensional gel electrophoresis and tandem mass spectrometry. Five differentially abundant spots were identified, and all the spots were over-abundant in RAC. The identified proteins were involved in muscle structure development (F-actin-capping protein subunit beta-2; PDZ and LIM domain protein-3), chaperone activity (heat shock protein beta-1), oxygen transport (myoglobin), and glycolysis (L-lactate dehydrogenase A chain). These results suggested that dietary ractopamine could influence the abundance of enzymes associated with muscle development and muscle fibre type shift in beef LL muscle.Keywords: growth promotants, meat quality, proteomic
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