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Underlying mechanisms of phosphodiesterase 10A and glutamate-ammonia ligase genes that regulate inosine monophosphate deposition and thereby affect muscle tenderness in Jingyuan chickens

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Objective: Inosine monophosphate (IMP) is a key factor that imparts of meat flavor. Differences in the IMP content in the muscles were evaluated to improve chicken meat quality. Methods: For this study, the IMP content was detected by high performance liquid chromatography. The gene expression profiles of Jingyuan chickens with different feeding patterns and different sexes were analyzed by RNA-sequencing (RNA-seq). Results: Breast muscle IMP content in free-range chickens was extremely significantly higher than that of caged chickens (p<0.01). Breast muscle IMP content in hens was also higher than that of cocks, but the difference was not significant. Correlation analysis showed that the breast muscle IMP content in caged hens and cocks was negatively correlated with the shear force, and the breast muscle IMP content in free-range hens was significantly negatively correlated with the shear force (p<0.05). The two key genes associated with IMP synthesis in chickens with different feeding patterns were glutamate-ammonia ligase (GLUL) and phosphodiesterase 10A (PDE10A). Bioinformatics analysis revealed that the GLUL and PDE10A genes are involved in glutamine biosynthesis and purine salvage pathways respectively. In addition, GLUL expression was positively correlated with the IMP content in caged and free-range chickens, and PDE10A expression was significantly positively correlated with the IMP content in caged and free-range chickens (p<0.05). Conclusion: These findings will facilitate the comprehension of the deposition of IMP in the muscles and thereby aid the process of selection and breeding of good quality local chickens.

Abstract

Objective: Inosine monophosphate (IMP) is a key factor that imparts of meat flavor. Differences in the IMP content in the muscles were evaluated to improve chicken meat quality. Methods: For this study, the IMP content was detected by high performance liquid chromatography. The gene expression profiles of Jingyuan chickens with different feeding patterns and different sexes were analyzed by RNA-sequencing (RNA-seq). Results: Breast muscle IMP content in free-range chickens was extremely significantly higher than that of caged chickens (p<0.01). Breast muscle IMP content in hens was also higher than that of cocks, but the difference was not significant. Correlation analysis showed that the breast muscle IMP content in caged hens and cocks was negatively correlated with the shear force, and the breast muscle IMP content in free-range hens was significantly negatively correlated with the shear force (p<0.05). The two key genes associated with IMP synthesis in chickens with different feeding patterns were glutamate-ammonia ligase (GLUL) and phosphodiesterase 10A (PDE10A). Bioinformatics analysis revealed that the GLUL and PDE10A genes are involved in glutamine biosynthesis and purine salvage pathways respectively. In addition, GLUL expression was positively correlated with the IMP content in caged and free-range chickens, and PDE10A expression was significantly positively correlated with the IMP content in caged and free-range chickens (p<0.05). Conclusion: These findings will facilitate the comprehension of the deposition of IMP in the muscles and thereby aid the process of selection and breeding of good quality local chickens.

참고문헌 (35)

  1. Magdelaine P, "Poultry meat consumption trends in europe", World Poult Sci J, 64, pp.53~56 (2008)[DOI]
  2. Kearney J, "Food consumption trends and drivers", Philos Trans R Soc Lond B Biol Sci, 365, pp.2793~2807 (2010)[DOI]
  3. Godfray HCJ, "Food security : the challenge of feeding 9 billion people", Science, 327, pp.812~818 (2010)[DOI]
  4. Toomer OT, "Meat quality and sensory attributes of meat produced from broiler chickens fed a high oleic peanut diet", Poult Sci, 98, pp.5188~5197 (2019)[DOI]
  5. Kuttappan VA, "White striping and woody breast myopathies in the modern poultry industry : a review", Poult Sci, 95, pp.2724~2733 (2016)[DOI]
  6. Zhang J, "Correlation analysis between AK1 mRNA expression and inosine monophosphate deposition in Jingyuan chickens", Animals, 10, pp.439~ (2020)[DOI]
  7. Jung S, "Carnosine, anserine, creatine, and inosine 5'-monophosphate contents in breast and thigh meats from 5 lines of Korean native chicken", Poult Sci, 92, pp.3275~3282 (2013)[DOI]
  8. Zhang T, "Specific expression pattern of IMP metabolism related-genes in chicken muscle between cage and free range conditions", Plos One, 13, pp.e0201736~ (2018)[DOI]
  9. Zhou XJ, "Effect of breed, age and feeding method on inosinic acid and intramuscular fat content of chicken meat", Chin J Anim Nutr, 22, pp.1251~1256 (2010)
  10. Sun YJ, "Influence of different feeding methods on muscle flavor substances of Beijing You chicken", Chin Anim Husband Veteri Medic, 41, pp.89~94 (2014)
  11. Chen YB, "Study on the relationship between the change rule of IMP content and correlation of related", pp.2021
  12. Dalgaard LB, "Classification of wooden breast myopathy in chicken pectoralis major by a standardised method and association with conventional quality assessments", Int J Food Sci Technol, 53, pp.1744~1752 (2018)[DOI]
  13. Chen L, "Prediction and analysis of essential genes using the enrichments of gene ontology and KEGG pathways", Plos One, 12, pp.e0184129~ (2017)[DOI]
  14. Szklarczyk D, "STRING v11 : proteinprotein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets", Nucleic Acids Res, 47, pp.D607-13~ (2019)[DOI]
  15. Jassal B, "The reactome pathway knowledgebase", Nucleic Acids Res, 48, pp.D498~D503 (2020)[DOI]
  16. Livak KJ, "Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method", Methods, 25, pp.402~408 (2001)[DOI]
  17. Yan JS, "Effects of exogenous inosine monophosphate on growth performance, flavor compounds, enzyme activity, and gene expression of muscle tissues in chicken", Poult Sci, 97, pp.1229~1237 (2018)[DOI]
  18. Küçüközet AO, "Cooking loss, tenderness, and sensory evaluation of chicken meat roasted after wrapping with edible films", Food Sci Technol Int, 24, pp.576~584 (2018)[DOI]
  19. Musundire MT, "Physical and chemical properties of meat from scavenging chickens and helmeted guinea fowls in response to age and sex", Br Poult Sci, 58, pp.390~396 (2017)[DOI]
  20. Liu Y, "Correlation between the content of inosine acid and meat quality of adult Daweishan mini chicken", Chin Poult, 39, pp.11~16 (2017)[DOI]
  21. Xiao J, "Study on slaughter performance and meat quality of Haikang chickens", Jiangsu Agric Sci, 47, pp.196~200 (2019)[DOI]
  22. Wang YW, "Effects of gender and muscle location on meat components of Pingwu red chicken", Jiangsu Agric Sci, 46, pp.179~182 (2018)[DOI]
  23. Li Q, "Comparison of postmortem changes in atp-related compounds, protein degradation and endogenous enzyme activity of white muscle and dark muscle from common carp(cyprinus carpio)stored at 4°C", LWT-Food Sci Technol, 78, pp.317~324 (2017)[DOI]
  24. BønsdorffT, "Mapping of the bovine genes of the de novo AMP synthesis pathway", Anim Genet, 35, pp.438~444 (2004)[DOI]
  25. Epstein PM, "Ontogenetic changes in adenylate cyclase, cyclic AMP phosphodiesterase and calmodulin in chick ventricular myocardium", Biochem J, 243, pp.525~531 (1987)[DOI]
  26. Dennison CS, "Age-dependent changes in amino acid phenotype and the role of glutamate release from hypothalamic proopiomelanocortin neurons", J Comp Neurol, 524, pp.1222~1235 (2016)[DOI]
  27. Keravis T, "Cyclic nucleotide phosphodiesterases(PDE)and peptide motifs", Curr Pharm Des, 16, pp.1114~1125 (2010)[DOI]
  28. Fujishige K, "Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A)", J Biol Chem, 274, pp.18438~18445 (1999)[DOI]
  29. Loughney K, "Isolation and characterization of PDE10A, a novel human 3’, 5’-cyclic nucleotide phosphodiesterase", Gene, 234, pp.109~117 (1999)[DOI]
  30. Beaumont V, "Phosphodiesterase 10A inhibition improves cortico-basal ganglia function in Huntington's disease models", Neuron, 92, pp.1220~1237 (2016)[DOI]
  31. Kumada Y, "Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes", Proc Natl Acad Sci USA, 90, pp.3009~3013 (1993)[DOI]
  32. He YJ, "Glutamine synthetase is essential in early mouse embryogenesis", Dev Dyn, 236, pp.1865~1875 (2007)[DOI]
  33. Spodenkiewicz M, "Minireview on glutamine synthetase deficiency, an ultra-rare inborn error of amino acid biosynthesis", Biology, 5, pp.40~ (2016)[DOI]
  34. Weber G, "Multi-enzyme-targeted chemotherapy by acivicin and actinomycin", Adv Enzyme Regul, 20, pp.75~96 (1982)[DOI]
  35. Cox AG, "Yap reprograms glutamine metabolism to increase nucleotide biosynthesis and enable liver growth", Nat Cell Biol, 18, pp.886~896 (2016)[DOI]

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