Location: Quality and Safety Assessment Research Unit
Title: Proteomic analyses on chicken breast meat with white striping myopathyAuthor
Kong, Byungwhi | |
OWENS, CASEY - University Of Arkansas | |
BOTTJE, WALTER - University Of Arkansas | |
SHAKERI, MAJID - Oak Ridge Institute For Science And Education (ORISE) | |
CHOI, JANGHAN - Oak Ridge Institute For Science And Education (ORISE) | |
Zhuang, Hong | |
Bowker, Brian |
Submitted to: Poultry Science
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 3/18/2024 Publication Date: 3/22/2024 Citation: Kong, B.C., Owens, C., Bottje, W., Shakeri, M., Choi, J., Zhuang, H., Bowker, B.C. 2024. Proteomic analyses on chicken breast meat with white striping myopathy. Poultry Science. http://doi.org/10.1016/j.psj.2024.103682. DOI: https://doi.org/10.1016/j.psj.2024.103682 Interpretive Summary: Quality defects in chicken breast meat including the white striping (WS) condition have caused substantial economic losses to the global poultry industry. This study was conducted to identify proteins that differentially exist in WS meat compared with normal meat. Results provide insights into potential biochemical and physiological mechanisms in the development of the WS condition and will contribute to improving poultry productivity through myopathy prevention. Technical Abstract: White striping (WS) is an emerging myopathy that results in significant economic losses to the global poultry industry. WS is detected as the occurrence of white lines on raw poultry meat. The exact etiologies for WS are still unclear. Proteomic analyses of co-expressed WS and woody breast phenotypes previously demonstrated dysfunctions in carbohydrate metabolism, protein synthesis, and calcium buffering capabilities in muscle cells. In this study, we conducted shotgun proteomics on chicken breast fillets exhibiting only WS that were collected at approximately 6 h postmortem. After determining WS severity, protein extractions were conducted from severe WS meat with no woody breast (WB) condition (n=5) and normal non-affected (no WS) control meat (n=5). Shotgun proteomics was conducted by Orbitrap Lumos, tandem mass tag (TMT) analysis. As results, 148 differentially abundant proteins (|fold change|>1.4; p-value < 0.05) were identified in the WS meats compared with controls. The significant canonical pathways included BAG2 signaling pathway, glycogen degradation II, Isoleucine degradation I, aldosterone signaling in epithelial cells, and valine degradation I. The potential upstream regulators include LIPE, UCP1, ATP5IF1, and DMD. The results of this study provide additional insights into the cellular mechanisms on the WS myopathy and meat quality. |