Abstract
Meat quality is a complex trait influenced by many factors, including genetics, nutrition, feeding environment, animal handling, and their interactions. To elucidate relevant factors affecting pork quality associated with oxidative stress and muscle development, we analyzed protein expression in high quality longissimus dorsi muscles (HQLD) and low quality longissimus dorsi muscles (LQLD) from Duroc pigs by liquid chromatographytandem mass spectrometry (LC-MS/MS)–based proteomic analysis. Between HQLD (n = 20) and LQLD (n = 20) Duroc pigs, 24 differentially expressed proteins were identified by LC-MS/MS. A total of 10 and 14 proteins were highly expressed in HQLD and LQLD, respectively. The 24 proteins have putative functions in the following seven categories: catalytic activity (31%), ATPase activity (19%), oxidoreductase activity (13%), cytoskeletal protein binding (13%), actin binding (12%), calcium ion binding (6%), and structural constituent of muscle (6%). Silver-stained image analysis revealed significant differential expression of lactate dehydrogenase A (LDHA) between HQLD and LQLD Duroc pigs. LDHA was subjected to in vitro study of myogenesis under oxidative stress conditions and LDH activity assay to verification its role in oxidative stress. No significant difference of mRNA expression level of LDHA was found between normal and oxidative stress condition. However, LDH activity was significantly higher under oxidative stress condition than at normal condition using in vitro model of myogenesis. The highly expressed LDHA was positively correlated with LQLD. Moreover, LDHA activity increased by oxidative stress was reduced by antioxidant resveratrol. This paper emphasizes the importance of differential expression patterns of proteins and their interaction for the development of meat quality traits. Our proteome data provides valuable information on important factors which might aid in the regulation of muscle development and the improvement of meat quality in longissimus dorsi muscles of Duroc pigs under oxidative stress conditions.
Highlights
Variation in meat quality traits is a well-known problem
Some previous studies have indicated that meat sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), protein spots were visualized using protocols quality is determined by postmortem muscle metabolism described in PlusOne Silver staining kit (GE Healthcare (Pette, 2002; Spangenburg and Booth, 2003)
We focus on its use in the study of livestock muscle development and meat quality with a focus on the differential expression patterns of proteins and their interactions for the development of meat quality traits
Summary
Some previous studies have indicated that meat SDS-PAGE, protein spots were visualized using protocols quality is determined by postmortem muscle metabolism described in PlusOne Silver staining kit (GE Healthcare (Pette, 2002; Spangenburg and Booth, 2003). This lack of oxygen results in a shift to was modified so that glutaraldehyde was omitted from the glycolytic (anaerobic) metabolism and a buildup of lactic sensitization step and formaldehyde was omitted from the acid, causing a drop in muscle pH (Frisby et al, 2005). The underlying Liquid chromatography-tandem mass spectrometry mechanisms of many different meat quality traits are far. Peptides were bound to the trapping column for 10 min with 2% (vol/vol) aqueous acetonitrile containing 0.1% (vol/vol) formic acid.
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