Abstract
Chronological age is one of the important factors influencing muscle development and meat quality in chickens. To evaluate the protein expression profiles during skeletal muscle development, we performed a tandem mass tag (TMT)-based quantitative proteomic strategy in pectoralis major (breast muscle) of Beijing-You chicken (BYC) at the chronological age of 90, 120, and 150 days. Each chronological age contained 3 pooling samples or 15 birds (five birds per pooling sample). A total of 1,413 proteins were identified in chicken breast muscle with FDR < 1% and 197 of them were differentially expressed (fold change ≥1.2 or ≤0.83 and p < 0.05). There were 110 up- and 71 down-regulated proteins in 120 d vs 90 d group, 13 up- and 10 down-regulated proteins in 150 d vs 120 d group. The proteomic profiles of BYC at 120 d were very similar to those at 150 d and highly different from those at 90 d, suggesting that 120 d might be an important chronological age for BYC. Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses indicated that these differentially expressed proteins were mainly involved in the pathway of glycolysis/gluconeogenesis, adrenergic signaling in cardiomyocytes, focal adhesion, oocyte meiosis and phagosome. Furthermore, some DEPs were quantified using parallel reaction monitoring (PRM) to validate the results from TMT analysis. In summary, these results provided some candidate protein-coding genes for further functional validation and contribute to a comprehensive understanding of muscle development and age-dependent meat quality regulation by proteins in chickens.
Highlights
Muscle development and meat quality are traits that are comprehensively affected by age, gender, nutrition, and species (López et al, 2011; Díaz et al, 2012; Umaya, 2014; Tasoniero et al, 2018)
The results showed that Llactate dehydrogenase A chain (LDHA), beta-enolase (ENO3), and fructose-bisphosphate aldolase (ALDOC) were enriched in the glycolysis/gluconeogenesis pathway, while myosin regulatory light chain 2 (MYLPF) and myosin heavy chain (P13538) were derived from the tight junction pathway and tropomyosin alpha1 chain (TPM1) was derived from the adrenergic signaling in cardiomyocytes pathway
Proteomic analysis was known as a powerful technique for studying the protein expression patterns, and has been widely carried out in identifying proteome changes of skeletal muscle at different development stages in chickens (Doherty et al, 2004; Teltathum and Mekchay, 2009; Liu et al, 2016; Ouyang et al, 2017)
Summary
Muscle development and meat quality are traits that are comprehensively affected by age, gender, nutrition, and species (López et al, 2011; Díaz et al, 2012; Umaya, 2014; Tasoniero et al, 2018). In another work, Cai et al (2018) characterized the whole muscle proteome and indicated that eight proteins were differentially expressed between normal and woody breast meat samples using two-dimensional gel electrophoresis. Most of these studies were limited to gel-based proteomic approaches. Early studies mainly focused on commercial broilers and layers, but an understanding of the molecular mechanisms underlying muscle development and meat quality due to Chinese indigenous chickens remains lacking
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