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ARS Home » Southeast Area » Athens, Georgia » U.S. National Poultry Research Center » Quality and Safety Assessment Research Unit » Research » Publications at this Location » Publication #416211
Research Project: Assessment of Quality Attributes of Poultry Products, Grain, Seed, Nuts, and Feed

Location: Quality and Safety Assessment Research Unit

Title: Proteomic analysis suggests mitochondria disorders and cell death lead to spaghetti meat myopathy

Author
item SHAKERI, MAJID - US Department Of Energy
item CHOI, JANGHAN - US Department Of Energy
item Kong, Byungwhi
item Zhuang, Hong
item Bowker, Brian

Submitted to: Meat and Muscle Biology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 9/14/2024
Publication Date: 9/15/2024
Citation: Shakeri, M., Choi, J., Kong, B.C., Zhuang, H., Bowker, B.C. 2024. Proteomic analysis suggests mitochondria disorders and cell death lead to spaghetti meat myopathy. Meat and Muscle Biology. 8(1): 18205, 1–7. https://doi.org/10.22175/mmb.18205.
DOI: https://doi.org/10.22175/mmb.18205

Interpretive Summary: Spaghetti meat (SM) is a myopathy that affects the structural integrity of breast muscle in broilers and reduces meat quality. Unfortunately, the cause of SM is unknown making it difficult to develop effective preventative measures. Different nutritional and management strategies have been examined to reduce the incidence of SM. However, none of the strategies have identified a promising solution to overcome the issue. A better understanding of the underlying mechanisms is needed to make it possible to develop effective strategies to cope with the issue. In this study, proteomics analysis was utilized to investigate alterations in muscle composition related to SM. Results suggested that SM impaired energy production and mitochondria function and elevated cell death in the affected muscle tissue.

Technical Abstract: Spaghetti meat (SM) is a myopathy that affects the structural integrity of Pectoralis major muscles in broilers and accounts for decreased meat acceptability and significant economic losses for the industry. The causative mechanisms have not been as extensively investigated as other myopathies such as wooden breast. A novel method to investigate alterations in muscle composition is proteomics analysis. The aim of this study was to investigate proteins related to mitochondria function in SM using proteomics analysis. Severe SM and normal (N) pectoralis major were collected from a broiler processing plant. The analysis identified 1903 proteins. Results suggested that SM exhibited greater cellular stress and cell death as evidenced by increased N-myc downstream-regulated gene 1, Plastin 3, ribosomal protein L10 and calnexin (FDR<0.05 for all). Increased cell stress potentially impacted nonsense meditated decade pathway (eliminates mRNAs containing premature translation termination codons). The SM myopathy downregulated several composites related to mitochondria function and glucose metabolism pathways including basic leucine zipper and w2 domains 2, eukaryotic translation initiation factor 3 subunit B, pyruvate kinase L/R, thioredoxin-dependent peroxide reductase mitochondrial, enolase 3, creatine kinase mitochondrial 2, succinate-CoA ligase GDP/ADP-forming subunit alpha1, calcium voltage-gated channel auxiliary subunit alpha2delta 1 and complement 1q binding protein C (FDR<0.05 for all) indicating a disruption in energy production and cell health. Current results suggested that SM impaired energy production and mitochondria function and elevated cell death. Although this study provides valuable information regarding possible mechanisms involved in the SM myopathy, further investigations are required to fully understand the mechanisms and their connections to other vital pathways.