Insights from proteome to phosphorylated proteome: deciphering different regulatory mechanisms in goat muscles with high‐ and low‐meat quality

Abstract

SUMMARYTo investigate the inner mechanisms of meat quality differences between high‐quality (HQ) and low‐quality (LQ), a comparative quantitative study between longissimus thoracis and external intercostals of goat muscle was performed from proteome to phosphorylated proteome using RP‐HPLC in combination with the ‘isobaric tag’ for relative and absolute quantitation (iTRAQ) labelling strategy. Altogether, 1441 proteins were identified in our study, of which 673 were phosphoproteins, and a total of twenty were common differentially expressed proteins. Myosin, carbonic anhydrase, and phosphoglucomutase could be used as proteins marker for HQ and LQ meat. Bioinformatics analysis showed that these proteins exhibited different rates for glycolysis and oxidative phosphorylation reaction, thus causing the different pH and NADH change rates, and resulting in better colour, tenderness, and water retention in HQ meat. The release of Ca2+ and adenosine triphosphate changed the meat quality through calcium signalling. Our finding provides a comprehensive view of proteome changes and their phosphorylation levels in goat muscle, involved in producing meats of different muscle parts. It also gives a better understanding of the regulation of protein on various biological processes that determine the final meat quality attributes.