title: Proteome Analysis Using Isobaric Tags for Relative and Absolute Analysis Quantitation (iTRAQ) Reveals Alterations in Stress-Induced Dysfunctional Chicken Muscle.
abstract: The current study was designed to investigate changes in the protein profiles of pale, soft, and exudative (PSE)-like muscles of broilers subjected to transportation under high-temperature conditions, using isobaric tags for relative and absolute analysis quantitation (iTRAQ). Arbor Acres chickens (n = 112) were randomly divided into two treatments: unstressed control (CON) and 0.5 h of transport (T). Birds were transported according to a designed protocol. Pectoralis major (PM) muscle samples in the T group were collected and classified as normal (T-NOR) or PSE-like (T-PSE). Plasma activities of stress indicators, muscle microstructure, and proteome were measured. Results indicated that broilers in the T-PSE group exhibited higher activities of plasma stress indicators. The microstructure of T-PSE group showed a looser network and larger intercellular spaces in comparison to the other groups. Proteomic analysis, based on iTRAQ, revealed 29 differentially expressed proteins in the T-NOR and T-PSE groups that were involved in protein turnover, signal transduction, stress and defense, calcium handling, cell structure, and metabolism. In particular, proteins relating to the glycolysis pathway, calcium signaling, and molecular chaperones exhibited significant differences that may contribute to the inferior post-mortem meat quality. Overall, the proteomic results provide a further understanding of the mechanism of meat quality changes in response to stress.
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University , Nanjing 210095, China.
authors.forename: Tong
authors.identifier: http://orcid.org/0000-0003-1561-4614
authors.initials: T
authors.lastname: Xing
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University , Nanjing 210095, China.
authors.forename: Chong
authors.initials: C
authors.lastname: Wang
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University , Nanjing 210095, China.
authors.forename: Xue
authors.initials: X
authors.lastname: Zhao
authors.affiliation: Experimental Teaching Center of Life Science, Nanjing Agricultural University , Nanjing 210095, People's Republic of China.
authors.forename: Chen
authors.initials: C
authors.lastname: Dai
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University , Nanjing 210095, China.
authors.forename: Guanghong
authors.initials: G
authors.lastname: Zhou
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University , Nanjing 210095, China.
authors.forename: Xinglian
authors.initials: X
authors.lastname: Xu
mesh_terms: D000818:Animals; D030161:Avian Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002645:Chickens / Q000235:genetics / Q000502:physiology*; D005260:Female; D006358:Hot Temperature; D008297:Male; D008460:Meat / Q000032:analysis; D018482:Muscle, Skeletal / Q000737:chemistry / Q000378:metabolism; D020543:Proteome / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D013312:Stress, Physiological
chemical_list: D030161:Avian Proteins; D020543:Proteome
keywords: broiler; calcium signaling; glycolysis; molecular chaperone; proteome; stress