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http://dx.doi.org/10.5713/ab.21.0134

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

Wang, Weizhen (Agriculture School, Ningxia University)
Zhang, Juan (Agriculture School, Ningxia University)
Hu, Honghong (Agriculture School, Ningxia University)
Yu, Baojun (Agriculture School, Ningxia University)
He, Jintong (Agriculture School, Ningxia University)
Yao, Tingting (Agriculture School, Ningxia University)
Gu, Yaling (Agriculture School, Ningxia University)
Cai, Zhengyun (Agriculture School, Ningxia University)
Xin, Guosheng (Ningxia Feed Engineering Technology Research Center, School of Life Sciences, Ningxia University)
Publication Information
Animal Bioscience / v.35, no.11, 2022 , pp. 1771-1786 More about this Journal
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.
Keywords
Glutamate-ammonia Ligase (GLUL); Inosine Monophosphate; Jingyuan Chicken; Phosphodiesterase 10A (PDE10A); RNA-seq;
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1 Jung S, Bae YS, Kim HJ, et al. Carnosine, anserine, creatine, and inosine 5'-monophosphate contents in breast and thigh meats from 5 lines of Korean native chicken. Poult Sci 2013; 92:3275-82. https://doi.org/10.3382/ps.2013-03441   DOI
2 Sun YJ, Tian HS, Zhao GP, et al. Influence of different feeding methods on muscle flavor substances of Beijing You chicken. Chin Anim Husband Veteri Medic 2014;41:89-94.
3 Szklarczyk D, Gable AL, Lyon D, et al. STRING v11: proteinprotein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets. Nucleic Acids Res 2019;47:D607-13. https://doi. org/10.1093/nar/gky1131   DOI
4 Cox AG, Hwang KL, Brown KK, et al. Yap reprograms glutamine metabolism to increase nucleotide biosynthesis and enable liver growth. Nat Cell Biol 2016;18:886-96. https://doi.org/10.1038/ncb3389   DOI
5 Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001;25:402-8. https://doi.org/10. 1006/meth.2001.1262   DOI
6 Jassal B, Matthews L, Viteri G, et al. The reactome pathway knowledgebase. Nucleic Acids Res 2020;48:D498-503. https://doi.org/10.1093/nar/gkz1031   DOI
7 Dennison CS, King CM, Dicken MS, Hentges ST. Age-dependent changes in amino acid phenotype and the role of glutamate release from hypothalamic proopiomelanocortin neurons. J Comp Neurol 2016;524:1222-35. https://doi.org/10.1002/cne.23900   DOI
8 Keravis T, Lugnier C. Cyclic nucleotide phosphodiesterases (PDE) and peptide motifs. Curr Pharm Des 2010;16:111425. https://doi.org/10.2174/138161210790963760   DOI
9 Dalgaard LB, Rasmussen MK, Bertram HC, et al. Classification of wooden breast myopathy in chicken pectoralis major by a standardised method and association with conventional quality assessments. Int J Food Sci Technol 2018;53:174452. https://doi.org/10.1111/ijfs.13759   DOI
10 Chen L, Zhang YH, Wang S, Zhang Y, Huang T, Cai YD. Prediction and analysis of essential genes using the enrichments of gene ontology and KEGG pathways. Plos One 2017;12:e0184129. https://doi.org/10.1371/journal.pone.0184129   DOI
11 Yan JS, Liu PF, Xu LM, et al. Effects of exogenous inosine monophosphate on growth performance, flavor compounds, enzyme activity, and gene expression of muscle tissues in chicken. Poult Sci 2018;97:1229-37. https://doi.org/10.3382/ps/pex415   DOI
12 Kucukozet AO, Uslu MK. Cooking loss, tenderness, and sensory evaluation of chicken meat roasted after wrapping with edible films. Food Sci Technol Int 2018;24:576-84. https://doi.org/10.1177/1082013218776540   DOI
13 Li Q, Zhang L, Lu H, Song S, Luo Y. 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 2017;78: 317-24. https://doi.org/10.1016/j.lwt.2016.12.035   DOI
14 Kearney J. Food consumption trends and drivers. Philos Trans R Soc Lond B Biol Sci 2010;365:2793-807. https://doi.org/10.1098/rstb.2010.0149   DOI
15 Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA. Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene 1999;234:109-17. https://doi.org/10.1016/s0378-1119(99)00171-7   DOI
16 Beaumont V, Zhong S, Lin H, et al. Phosphodiesterase 10A inhibition improves cortico-basal ganglia function in Huntington's disease models. Neuron 2016;92:1220-37. https://doi.org/10.1016/j.neuron.2016.10.064   DOI
17 He YJ, Hakvoort TB, Vermeulen JL, Lamers WH, Van RMA. Glutamine synthetase is essential in early mouse embryogenesis. Dev Dyn 2007;236:1865-75. https://doi.org/10.1002/dvdy.21185   DOI
18 Spodenkiewicz M, Diez-Fernandez C, Rufenacht V, GemperleBritschgi C, Haberle J. Minireview on glutamine synthetase deficiency, an ultra-rare inborn error of amino acid biosynthesis. Biology 2016;5:40. https://doi.org/10.3390/biology5040040   DOI
19 Godfray HCJ, Beddington JR, Crute IR, et al. Food security: the challenge of feeding 9 billion people. Science 2010;327:812-8. https://doi.org/10.1126/science.1185383   DOI
20 Musundire MT, Halimani TE, Chimonyo M. Physical and chemical properties of meat from scavenging chickens and helmeted guinea fowls in response to age and sex. Br Poult Sci 2017;58:390-6. https://doi.org/10.1080/00071668.2017.1313961   DOI
21 Toomer OT, Livingston ML, Wall B, et al. Meat quality and sensory attributes of meat produced from broiler chickens fed a high oleic peanut diet. Poult Sci 2019;98:5188-97. https://doi.org/10.3382/ps/pez258   DOI
22 Kuttappan VA, Hargis BM, Owens CM. White striping and woody breast myopathies in the modern poultry industry: a review. Poult Sci 2016;95:2724-33. https://doi.org/10.3382/ps/pew216   DOI
23 Zhang J, Hu HH, Mu T, et al. Correlation analysis between AK1 mRNA expression and inosine monophosphate deposition in Jingyuan chickens. Animals 2020;10:439. https://doi.org/10.3390/ani10030439   DOI
24 Zhang T, Lu HZ, Wang L, Yin MC, Yang LK. Specific expression pattern of IMP metabolism related-genes in chicken muscle between cage and free range conditions. Plos One 2018;13:e0201736. https://doi.org/10.1371/journal.pone.0201736   DOI
25 Zhou XJ, Zhu NH, Zhang RJ. Effect of breed, age and feeding method on inosinic acid and intramuscular fat content of chicken meat. Chin J Anim Nutr 2010;22:1251-6.
26 Chen YB. Study on the relationship between the change rule of IMP content and correlation of related. Shaanxi, China: Shaanxi University of Technology; 2021. pp. 53-6.
27 Bonsdorff T, Gautier M, Farstad W, Ronningen K, Lingaas F, Olsaker I. Mapping of the bovine genes of the de novo AMP synthesis pathway. Anim Genet 2004;35:438-44. https://doi.org/10.1111/j.1365-2052.2004.01201.x   DOI
28 Liu Y, Tomg HQ, Liu LX, et al. Correlation between the content of inosine acid and meat quality of adult Daweishan mini chicken. Chin Poult 2017;39:11-6. https://doi.org/10.16372/j.issn.1004-6364.2017.19.003   DOI
29 Xiao J, Hua GH, Li H, et al. Study on slaughter performance and meat quality of Haikang chickens. Jiangsu Agric Sci 2019;47:196-200. https://doi.org/10.15889/j.issn.1002-1302.2019.17.049   DOI
30 Wang YW, Li YJ, Zhang XH, et al. Effects of gender and muscle location on meat components of Pingwu red chicken. Jiangsu Agric Sci 2018;46:179-82. https://doi.org/10.15889/j.issn.1002-1302.2018.22.042   DOI
31 Epstein PM, Andrenyak DM, Smith CJ, Pappano AJ. Ontogenetic changes in adenylate cyclase, cyclic AMP phosphodiesterase and calmodulin in chick ventricular myocardium. Biochem J 1987;243:525-31. https://doi.org/10.1042/bj2430525   DOI
32 Magdelaine P, Spiess MP, Valceschini E. Poultry meat consumption trends in europe. World Poult Sci J 2008;64:53-6. https://doi.org/10.1017/S0043933907001717   DOI
33 Fujishige K, Kotera J, Michibata H, et al. Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem 1999; 274:18438-45. https://doi.org/10.1074/jbc.274.26.18438   DOI
34 Kumada Y, Benson DR, Hillemann D, et al. Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes. Proc Natl Acad Sci USA 1993;90:300913. https://doi.org/10.1073/pnas.90.7.3009   DOI
35 Weber G, Prajda N, Lui MS, et al. Multi-enzyme-targeted chemotherapy by acivicin and actinomycin. Adv Enzyme Regul 1982;20:75-96. https://doi.org/10.1016/0065-2571(82)90009-7   DOI