Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development

Abstract

Embryonic growth and development of skeletal muscle is a major determinant of muscle mass, and has a significant effect on meat production in chicken. To assess the protein expression profiles during embryonic skeletal muscle development, we performed a proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) in leg muscle tissues of female Xinghua chicken at embryonic age (E) 11, E16, and 1-day post hatch (D1). We identified 3,240 proteins in chicken embryonic muscle and 491 of them were differentially expressed (fold change ≥ 1.5 or ≤ 0.666 and p < 0.05). There were 19 up- and 32 down-regulated proteins in E11 vs. E16 group, 238 up- and 227 down-regulated proteins in E11 vs. D1 group, and 13 up- and 5 down-regulated proteins in E16 vs. D1 group. Protein interaction network analyses indicated that these differentially expressed proteins were mainly involved in the pathway of protein synthesis, muscle contraction, and oxidative phosphorylation. Integrative analysis of proteome and our previous transcriptome data found 189 differentially expressed proteins that correlated with their mRNA level. The interactions between these proteins were also involved in muscle contraction and oxidative phosphorylation pathways. The lncRNA-protein interaction network found four proteins DMD, MYL3, TNNI2, and TNNT3 that are all involved in muscle contraction and may be lncRNA regulated. These results provide several candidate genes for further investigation into the molecular mechanisms of chicken embryonic muscle development, and enable us to better understanding their regulation networks and biochemical pathways.

Sarcomeric TPM3α in developing chicken

“…The results alone suggest that embryonic skeletal muscles express higher TPM3α transcripts than the 15‐day post‐hatch animals and still higher than muscles from adult chicken. Our finding on the expression of TPM3a transcripts in embryonic chicken skeletal muscles is in agreement with the findings of Ouyang et al (). These authors performed proteomic analysis of chicken skeletal muscle during embryonic development and found the elevated amount of TPM3 expression in embryonic (E11) vs. D1 or developed chicken.…”

“…Sarcomeric TPM3 isoform has long been known to play a critical role in muscle contraction in slow skeletal muscle in vertebrates. However, no sarcomeric TPM3 protein or its cDNA clone has been reported until June 3, 2017 (variant 4; NM_001352041.1) (Ouyang et al, 2017), while we were submitting our TPM3a sequence in GenBank (submission id: MF347378). Interestingly, the nucleotide as well as deduced amino acid sequences of a low molecular weight TPM3 isoform (TPM3b) was reported by MacLeod (1982) .…”

Enhanced Immune Responses with Serum Proteomic Analysis of Hu Sheep to Foot-and-Mouth Disease Vaccine Emulsified in a Vegetable Oil Adjuvant

“…This study suggested that the adjuvant properties of SO-VE-GS may be attributed to activation of immune-related genes and pathways [32]. This proteomic technology [56] is based on isotopic labeling and has been applied in several aspects, including production mechanisms [57], growth performance [44], and disease resistance of animals [58][59][60]. However, few studies have looked at its use in vaccine adjuvant research.…”

“…To explore the protein-protein interaction networks, STRING software [44] was adopted. In the SO-VE-GS vs. control comparison, 23 differentially expressed proteins were analyzed and 16 of them constituted an interaction network with 23 nodes and 23 edges.…”

Proteomic analyses of sheep (ovis aries) embryonic skeletal muscle

“…The embryonic phase is important for skeletal muscle development and growth 18 . During this phase, the muscle fibres are formed and proliferated at early embryonic stage and hypertrophic at late stage 19,20 , which has great influence on production of meat mass 21 .…”