Ractopamine-induced changes in the proteome of post-mortem beef longissimus lumborum muscle
Kim, H.M.(University of Kentucky Department of Animal and Food Sciences) | Suman, S.P.(University of Kentucky Department of Animal and Food Sciences) | Li, S.(University of Kentucky Department of Animal and Food Sciences) | Beach, C.M.(University of Kentucky Proteomics Core Facility) | Nair, M.N.(Colorado State University Department of Animal Sciences) | Zhai, C.(Colorado State University Department of Animal Sciences) | Edenburn, B.M.(University of Illinois Department of Animal Sciences) | Felix, T.L.(University of Illinois Department of Animal Sciences) | Dilger, A.C.(University of Illinois Department of Animal Sciences) | Boler, D.D.(University of Illinois Department of Animal Sciences)
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.
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