Animal Bioscience

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
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Association of single-nucleotide polymorphisms in dual specificity phosphatase 8 and insulin-like growth factor 2 genes with inosine-5'-monophosphate, inosine, and hypoxanthine contents in chickens

  • Jean Pierre Munyaneza (Division of Animal and Dairy Science, Chungnam National University) ;
  • Minjun Kim (Division of Animal and Dairy Science, Chungnam National University) ;
  • Eunjin Cho (Department of Bio-AI Convergence, Chungnam National University) ;
  • Aera Jang (Department of Applied Animal Science, College of Animal Life Science, Kangwon National University) ;
  • Hyo Jun Choo (Poultry Research Institute, National Institute of Animal Science) ;
  • Jun Heon Lee (Division of Animal and Dairy Science, Chungnam National University)
  • Received : 2023.03.08
  • Accepted : 2023.05.22
  • Published : 2023.09.01
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Abstract

Objective: This study aimed to identify the single-nucleotide polymorphisms (SNPs) in the dual-specificity phosphatase 8 (DUSP8) and insulin-like growth factor 2 (IGF2) genes and to explore their effects on inosine-5'-monophosphate (IMP), inosine, and hypoxanthine contents in Korean native chicken -red-brown line (KNC-R Line). Methods: A total sample of 284 (males, n = 127; females n = 157) and 230 (males, n = 106; females, n = 124) aged of 10 weeks old KNC-R line was used for genotyping of DUSP8 and IGF2 genes, respectively. One SNP (rs313443014 C>T) in DUSP8 gene and two SNPs (rs315806609A/G and rs313810945T/C) in IGF2 gene were used for genotyping by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) and KASP methods, respectively. The Two-way analysis of variance of the R program was used to associate DUSP8 and IGF2 genotypes with nucleotide contents in KNC-R chickens. Results: The DUSP8 (rs313443014 C>T) was polymorphic in KNC-R line and showed three genotypes: CC, CT, and TT. The IGF2 gene (rs315806609A/G and rs313810945T/C) was also polymorphic and had three genotypes per SNP, including GG, AG, and AA for the SNP rs315806609A/G and genotypes: CC, CT, and TT for the SNP rs313810945T/C. Association resulted into a strong significant association (p<0.01) with IMP, inosine, and hypoxanthine. Moreover, the significant effect of sex (p<0.05) on nucleotide content was also observed. Conclusion: The SNPs in the DUSP8 and IGF2 genes might be used as genetic markers in the selection and production of chickens with highly flavored meat.

Keywords

Acknowledgement

We acknowledge the financial support from the research encouragement scholarship for graduate students (2nd batch, the year 2021) of Chungnam National University, Daejeon 34134, South Korea.

References

  1. Kubberod E, Ueland O, Rodbotten M, Westad F, Risvik E. Gender specific preferences and attitudes towards meat. Food Qual Prefer 2002;13:285-94. https://doi.org/10.1016/S0950-3293(02)00041-1 
  2. Elzerman JE, Hoek AC, Van Boekel MAJS, Luning PA. Consumer acceptance and appropriateness of meat substitutes in a meal context. Food Qual Prefer 2011;22:233-40. https://doi.org/10.1016/j.foodqual.2010.10.006 
  3. Benningstad NCG, Kunst JR. Dissociating meat from its animal origins: A systematic literature review. Appetite 2020; 147:104554. https://doi.org/10.1016/j.appet.2019.104554 
  4. Chumngoen W, Tan FJ. Relationships between descriptive sensory attributes and physicochemical analysis of broiler and Taiwan native chicken breast meat. Asian-Australas J Anim Sci 2015;28:1028-37. https://doi.org/10.5713/ajas.14.0275 
  5. Marangoni F, Corsello G, Cricelli C, et al. Role of poultry meat in a balanced diet aimed at maintaining health and wellbeing: An Italian consensus document. Food Nutr Res 2015;59:27606. https://doi.org/10.3402/fnr.v59.27606 
  6. Munyaneza JP, Ediriweera TK, Kim M, et al. Genome-wide association studies of meat quality traits in chickens: a review. Korean J Agric Sci 2022;49:407-20. https://doi.org/10.7744/kjoas.20220029 
  7. Jin S, Park HB, Seo D, et al. Identification of quantitative trait loci for the fatty acid composition in Korean native chicken. Asian-Australas J Anim Sci 2018;31:1134-40. https://doi.org/10.5713/ajas.17.0781 
  8. Seo D, Park HB, Choi N, et al. Association of SNPs in AMY1A and AMY2A genes with chicken meat quality and clinical-chemical traits in chicken. J Fac Agric Kyushu Univ 2016;61:121-5. https://doi.org/10.5109/1564092 
  9. Choe JH, Nam K, Jung S, Kim B, Yun H, Jo C. Differences in the quality characteristics between commercial Korean native chickens and broilers. Korean J Food Sci Anim Resour 2010;30:13-9. https://doi.org/10.5851/kosfa.2010.30.1.13 
  10. Cahyadi M, Park HB, Seo DW, et al. Association of the thyroid hormone responsive spot 14 alpha gene with growth-related traits in Korean native chicken. Asian-Australas J Anim Sci 2020;33:1755-62. https://doi.org/10.5713/ajas.19.0541 
  11. 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 
  12. Seo DW, Park HB, Jung S, et al. QTL analyses of general compound, color, and pH traits in breast and thigh muscles in Korean native chicken. Livest Sci 2015;182:145-50. https://doi.org/10.1016/j.livsci.2015.09.020 
  13. Jin S, Lee JH, Seo DW, et al. A major locus for quantitatively measured shank skin color traits in Korean native chicken. Asian-Australas J Anim Sci 2016;29:1555-61. https://doi.org/10.5713/ajas.16.0183 
  14. Jin S, Jayasena DD, Jo C, Lee JH. The breeding history and commercial development of the Korean native chicken. Worlds Poult Sci J 2017;73:163-74. https://doi.org/10.1017/S004393391600088X 
  15. Cha J, Choo H, Srikanth K, et al. Genome-wide association study identifies 12 loci associated with body weight at age 8 weeks in Korean native chickens. Genes (Basel) 2021;12:1170. https://doi.org/10.3390/genes12081170 
  16. Jung YK, Jeon HJ, Jung S, et al. Comparison of quality traits of thigh meat from Korean native chickens and broilers. Korean J Food Sci Anim Resour 2011;31:684-92. https://doi.org/10.5851/kosfa.2011.31.5.684 
  17. Uemoto Y, Ohtake T, Sasago N, et al. Effect of two nonsynonymous ecto-5'-nucleotidase variants on the genetic architecture of inosine 5'-monophosphate (IMP) and its degradation products in Japanese Black beef. BMC Genomics 2017;18:874. https://doi.org/10.1186/s12864-017-4275-4 
  18. Jayasena DD, Ahn DU, Nam KC, Jo C. Factors affecting cooked chicken meat flavour: a review. World's Poult Sci J 2013;69:515-26. https://doi.org/10.1017/S0043933913000548 
  19. Garmyn A. Consumer preferences and acceptance of meat products. Foods 2020;9:708. https://doi.org/10.3390/foods9060708 
  20. Mir NA, Rafiq A, Kumar F, Singh V, Shukla V. Determinants of broiler chicken meat quality and factors affecting them: a review. J Food Sci Technol 2017;54:2997-3009. https://doi.org/10.1007/s13197-017-2789-z 
  21. Khan MI, Jo C, Tariq MR. Meat flavor precursors and factors influencing flavor precursors- A systematic review. Meat Sci 2015;110:278-84. https://doi.org/10.1016/j.meatsci.2015.08.002 
  22. Jayasena DD, Kim SH, Lee HJ, et al. Comparison of the amounts of taste-related compounds in raw and cooked meats from broilers and Korean native chickens. Poult Sci 2014;93:3163-70. https://doi.org/10.3382/ps.2014-04241 
  23. Ismail I, Joo ST. Poultry meat quality in relation to muscle growth and muscle fiber characteristics. Korean J Food Sci Anim Resour 2017;37:873-83. 
  24. Lengkidworraphiphat P, Wongpoomchai R, Bunmee T, Chariyakornkul A, Chaiwang N, Jaturasitha S. Taste-active and nutritional components of thai native chicken meat: a perspective of consumer satisfaction. Food Sci Anim Resour 2021;41:237-46. https://doi.org/10.5851/kosfa.2020.e94 
  25. Rikimaru K, Takahashi H. Evaluation of the meat from Hinai-jidori chickens and broilers: Analysis of general biochemical components, free amino acids, inosine 5'-monophosphate, and fatty acids. J Appl Poult Res 2010;19:327-33. https://doi.org/10.3382/japr.2010-00157 
  26. Chen GH, Li HF, Wu XS, et al. Factors affecting the inosine monophosphate content of muscles in Taihe silkies chickens. Asian-Australas J Anim Sci 2002;15:1359-63. https://doi.org/10.5713/ajas.2002.1358 
  27. Van der Steen, HAM, Prall GFW, Plastow GS. Application of genomics to the pork industry. J Anim Sci 2005;83:E1-E8. https://doi.org/10.2527/2005.8313_supplE1x 
  28. Anggraeni A, Gunawan A, Rukmiasih R, Suryati T, Sumantri C. Identification of poymorphism and association analyses of FMO3 gene related with carcass and meat quality in Cihateup duck. Anim Prod 2017;19:151-9.  https://doi.org/10.20884/1.jap.2017.19.3.623
  29. Geng X, Liu S, Yuan Z, Jiang Y, Zhi D, Liu Z. A genomewide association study reveals that genes with functions for bone development are associated with body conformation in catfish. Mar Biotechnol 2017;19:570-8. https://doi.org/10.1007/s10126-017-9775-3 
  30. Zhao L, Li Y, Li Y, et al. A genome-wide association study identifies the genomic region associated with shell color in Yesso scallop, Patinopecten yessoensis. Mar Biotechnol 2017;19:301-9. https://doi.org/10.1007/s10126-017-9751-y 
  31. Gunawan A, Anggraeni A, Listyarini K, Sumantri C. Potential functional variants for fatness, carcass and meat quality traits in exon 3 of fat mass and obesity-associated gene in Indonesian ducks. Int J Poult Sci 2018;17:443-51. https://doi.org/10.3923/ijps.2018.443.451 
  32. Chen HF, Chuang HC, Tan TH. Regulation of dual-specificity phosphatase (DUSP) ubiquitination and protein stability. Int J Mol Sci 2019;20:2668. https://doi.org/10.3390/ijms20112668 
  33. Ferguson BS, Nam H, Morrison RF. Dual-specificity phosphatases regulate mitogen-activated protein kinase signaling in adipocytes in response to inflammatory stress. Cell Signal 2019;53:234-45. https://doi.org/10.1016/j.cellsig.2018.10.011 
  34. Hink R, Hokanson J, Shah I, Long J, Goldman D, Sikela J. Investigation of DUSP8 and CALCA in alcohol dependence. Addict Biol 2003;8:305-12. https://doi.org/10.1080/13556210310001602211 
  35. Ding T, Zhou Y, Long R, et al. DUSP8 phosphatase: Structure, functions, expression regulation and the role in human diseases. Cell Biosci 2019;9:70. https://doi.org/10.1186/s13578-019-0329-4 
  36. Cargnello M, Roux PP. Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Microbiol Mol Biol Rev 2011;75:50-83. https://doi.org/10.1128/MMBR.00031-10 
  37. Jeong DG, Wei CH, Ku B, et al. The family wide structure and function of human dual-specificity protein phosphatases. Acta Cryst 2014;D70:421-35. https://doi.org/10.1107/S1399004713029866 
  38. Schriever SC, Kabra DG, Pfuhlmann K, et al. Type 2 diabetes risk gene Dusp8 regulates hypothalamic Jnk signaling and insulin sensitivity. J Clin Investig 2020;130:6093-108. https://doi.org/10.1172/JCI136363 
  39. Amills M, Jimenez N, Villalba D, et al. Identification of three single nucleotide polymorphisms in the chicken insulin-like growth factor 1 and 2 genes and their associations with growth and feeding traits. Poult Sci 2003;82:1485-93. https://doi.org/10.1093/ps/82.10.1485 
  40. Wang G, Bingxue Y, Xuemei D, Changlu L, Xiaoxiang H, Ning L. Insulin-like growth factor 2 as a candidate gene influencing growth and carcass traits and its bialleleic expression in chicken. Sci China Life Sci 2005;48:187-94. https://doi.org/10.1007/BF02879672 
  41. Yan L, Fang X, Liu Y, Elzo MA, Zhang C, Chen H. Exploring the genetic variants of insulin-like growth factor II gene and their associations with two production traits in Langshan chicken. J Appl Anim Res 2017;45:60-3. https://doi.org/10.1080/09712119.2015.1124328 
  42. Ye J. Mechanism of insulin resistance in obesity: a role of ATP. Front Med 2021;15:372-82. https://doi.org/10.1007/s11684-021-0862-5 
  43. Criado-Mesas L, Ballester M, Crespo-Piazuelo D, et al. Analysis of porcine IGF2 gene expression in adipose tissue and its effect on fatty acid composition. PLoS ONE 2019;14:e0220708. https://doi.org/10.1371/journal.pone.0220708 
  44. McTaggart JS, Clark R, Ashcroft FM. The role of the KATP channel in glucose homeostasis in health and disease: More than meets the islet. J Physiol 2010;588:3201-9. https://doi.org/10.1113/jphysiol.2010.191767 
  45. Bonora M, Patergnani S, Rimessi A, et al. ATP synthesis and storage. Purinergic Signal 2012;8:343-57. https://doi.org/10.1007/s11302-012-9305-8 
  46. Oprea E, Ruta LL, Farcasanu EC. Pharmacological aspects and health impact of sports and energy drinks. In sports and energy drinks. Cambridge, UK: Woodhead publishing; 2019. pp. 65-129. 
  47. Kim HC, Ko YJ, Jo C. Potential of 2D qNMR spectroscopy for distinguishing chicken breeds based on the metabolic differences. Food Chem 2021;342:128316. https://doi.org/10.1016/j.foodchem.2020.128316 
  48. Nei M, Kumar S. Molecular evolution and phylogenetics. New York, USA: Oxford University Press; 2000. p. 231-5. 
  49. Hartl DL, Clark AG. Principle of population genetics. Sunderland, MA, USA: Sinauer Associates; 1997. p. 81. 
  50. R Core Team. R: A language and environment for statistical computing. Vienna, Austria: R foundation for statistical computing; 2022. https://www.R-project.org/ 
  51. Hall TA. BioEdit: An important software for molecular biology. GERF Bull Biosci 2011;2:60-1. 
  52. Hu J, Yu P, Ding X, Xu M, Guo B, Xu Y. Genetic polymorphisms of the AMPD1 gene and their correlations with IMP contents in Fast Partridge and Lingshan chickens. Gene 2015;574:204-9. https://doi.org/10.1016/j.gene.2015.08.008 
  53. Manjula P, Choi N, Seo D, Lee JH. POU class 1 homeobox 1 gene polymorphisms associated with growth traits in Korean native chicken. Asian-Australas J Anim Sci 2018;31:643-9. https://doi.org/10.5713/ajas.17.0354 
  54. Allendorf FW, Luikart G, Aitken SN. Conservation and genetics of populations. Chichester, UK: John Wiley and Sons; 2013. pp. 118-32. 
  55. Munyaneza JP, Gunawan A, Noor RR. Exploring effects of betaine-homocysteine methyltransferase (BHMT) gene polymorphisms on fatty acid traits and cholesterol in sheep. J Indonesian Trop Anim Agric 2019;44:243-51. https://doi.org/10.14710/jitaa.44.3.243-251