Animal Bioscience

  • 제35권4호
  • /
  • Pages.624-630
  • /
  • 2022
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  • 2765-0189(pISSN)
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  • 2765-0235(eISSN)
아세아태평양축산학회 (Asian Australasian Association of Animal Production Societies)
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Expression levels of filaggrin-2 in relation to drip loss in pigs

  • Kayan, Autchara (Department of Animal Science, Faculty of Agriculture, Kasetsart University) ;
  • Koomkrong, Nunyarat (Department of Animal Science, Faculty of Science and Technology, Suratthani Rajabhat University)
  • 투고 : 2021.05.10
  • 심사 : 2021.09.11
  • 발행 : 2022.04.01
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초록

Objective: The aim of this study was to investigate the expression level of filaggrin-2 (FLG2) in correlation with drip loss. Methods: The muscle samples were randomly taken from a local meat supplier. Samples were taken from Longissimus lumborum muscles to evaluate the drip loss (n = 100). Five muscles per group (low and high drip loss) were selected to evaluate FLG2 mRNA and protein expression levels. Results: mRNA of FLG2 gene was not significantly different in pigs with different levels of drip loss (p>0.05). Statistical analysis revealed that FLG2 protein expression levels were significantly different between the drip loss groups. Western blot revealed that the high drip loss group had higher FLG2 protein expression level than the low drip loss group (p<0.001). Moreover, immunohistochemistry revealed the high signal intensity was on the muscle cell membrane and cytoplasm. Conclusion: FLG2 protein might play roles in drip loss of pork and will provide the basis for information to improving meat quality traits in pigs.

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과제정보

Authors are grateful to Department of Animal Science, Faculty of Agriculture and Histological Preparation LAB, Faculty of Veterinary Medicine, Kasetsart University for the utilization of laboratory facilities.

참고문헌

  1. Ocampo Ibanez ID, Bermudez F, Diaz, H. Effect of storage time, muscle type, and animal genotype on drip loss in raw pork. Acta Agron 2009;58:180-8.
  2. Schafer A, Rosenvold K, Purslow PP, Andersen HJ, Henckel P. Physiological and structural events post mortem of importance for drip loss in pork. Meat Sci 2002;61:355-66. https://doi.org/10.1016/S0309-1740(01)00205-4
  3. Pas MFt, Kruijt L, Pierzchala M, et al. Identification of proteomic biomarkers in M. Longissimus dorsi as potential predictors of pork quality. Meat Sci 2013;95:679-87. https://doi.org/10.1016/j.meatsci.2012.12.015
  4. Zhang M, Wang D, Geng Z, et al. The level of heat shock protein 90 in pig Longissimus dorsi muscle and its relationship with meat pH and quality. Food Chem 2014;165:337-41. https://doi.org/10.1016/j.foodchem.2014.05.111
  5. Luca AD, Elia G, Hamill R, Mullen AM. 2D DIGE proteomic analysis of early post mortem muscle exudate highlights the importance of the stress response for improved water-holding capacity of fresh pork meat. Proteomics 2013;13:1528-44. https://doi.org/10.1002/pmic.201200145
  6. Luca AD, Elia G, Mullen AM, Hamill RM. Monitoring post mortem changes in porcine muscle through 2-D DIGE proteome analysis of Longissimus muscle exudate. Proteome Sci 2013;11:9. https://doi.org/10.1186/1477-5956-11-9
  7. Hsu C-Y, Henry J, Raymond A-A, et al. Deimination of human filaggrin-2 promotes its proteolysis by calpain 1. J Biol Chem 2011;286:23222-33. https://doi.org/10.1074/jbc.M110.197400
  8. Warriss PD. Meat science: an introductory text. 2nd ed. Wallingford, UK: CABI Publishers; 2010.
  9. Hertog-Meischke MJAd, Laack RJLMv, Smulders FJM. The water-holding capacity of fresh meat. Vet Q 1997;19:175-81. https://doi.org/10.1080/01652176.1997.9694767
  10. Huff-Lonergan E, Lonergan SM. Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci 2005;71:194-204. https://doi.org/10.1016/j.meatsci.2005.04.022
  11. Offer G, Knight P, Jeacocke R, et al. The structural basis of the water-holding, appearance and toughness of meat and meat products. Food Microstruct 1989;8:151-70.
  12. Pendaries V, Lamer ML, Cau L, et al. In a three-dimensional reconstructed human epidermis filaggrin-2 is essential for proper cornification. Cell Death Dis 2015;6:e1656. https://doi.org/10.1038/cddis.2015.29
  13. Melody JL, Lonergan SM, Rowe LJ, Huiatt TW, Mayes MS, Huff-Lonergan E. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J Anim Sci 2004;82:1195-205. https://doi.org/10.2527/2004.8241195x
  14. Luca AD, Hamill RM, Mullen AM, Slavov N, Elia G. Comparative proteomic profiling of divergent phenotypes for water holding capacity across the post mortem ageing period in porcine muscle exudate. PLoS ONE 2016;11:e0150605. https://doi.org/10.1371/journal.pone.0150605
  15. Seykora J, Dentchev T, Margolis DJ. Filaggrin-2 barrier protein inversely varies with skin inflammation. Exp Dermatol 2015;24:720-2. https://doi.org/10.1111/exd.12749
  16. Mohamad J, Sarig O, Godsel LM, et al. Filaggrin 2 deficiency results in abnormal cell-cell adhesion in the cornified cell layers and causes peeling skin syndrome type A. J Invest Dermatol 2018;138:1736-43. https://doi.org/10.1016/j.jid.2018.04.032
  17. Honikel KO, Kim CJ, Hamm R, Roncales P. Sarcomere shortening of prerigor muscles and its influence on drip loss. Meat Sci 1986;16:267-82. https://doi.org/10.1016/0309-1740(86)90038-0
  18. Bee G, Anderson AL, Lonergan SM, Huff-Lonergan E. Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork. Meat Sci 2007;76:359-65. https://doi.org/10.1016/j.meatsci.2006.12.004
  19. Kayan A, Uddin MJ, Cinar MU, et al. Investigation on interferon alpha-inducible protein 6 (IFI6) gene as a candidate for meat and carcass quality in pig. Meat Sci 2011;88:755-60. https://doi.org/10.1016/j.meatsci.2011.03.009
  20. Traore S, Aubry L, Gatellier P, et al. Higher drip loss is associated with protein oxidation. Meat Sci 2012;90:917-24. https://doi.org/10.1016/j.meatsci.2011.11.033
  21. Rozen S, Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. In: Misener S, Krawetz SA, editors. Bioinformatics methods and protocols. Methods in Molecular Biology, vol 132. Totowa, NJ. USA: Humana Press; 2000. vol 12. pp. 365-386. https://doi.org/10.1385/1-59259-192-2:365
  22. Khoshoii AA, Mobini B, Rahimi E. Comparison of chicken strains: Muscle fibre diameter and numbers in Pectoralis superficialis muscle. Glob Vet 2013;11:55-8.
  23. Koomkrong N, Gongruttananun N, Boonkaewwan C, Noosud J, Theerawatanasirikul S, Kayan A. Fiber characteristics of pork muscle exhibiting different levels of drip loss. Anim Sci J 2017;88:2044-9. https://doi.org/10.1111/asj.12859
  24. Adzitey F, Nurul H. Pale soft exudative (PSE) and dark firm dry (DFD) meats: causes and measures to reduce these incidences - a mini review. Int Food Res J 2011;18:11-20.
  25. Borchers N, Otto G, Kalm E. Genetic relationship of drip loss to further meat quality traits in purebred Pietrains. Arch Tierz 2007;50:84-91. https://doi.org/10.5194/aab-50-84-2007
  26. Morlein D, Link G, Werner C, Wicke M. Suitability of three commercially produced pig breeds in Germany for a meat quality program with emphasis on drip loss and eating quality. Meat Sci 2007;77:504-11. https://doi.org/10.1016/j.meatsci.2007.04.030
  27. Warriss PD, Brown SN. The relationships between initial pH, reflectance and exudation in pig muscle. Meat Sci 1987;20:65-74. https://doi.org/10.1016/0309-1740(87)90051-9
  28. Ryu YC, Kim BC. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Sci 2005;71:351-7. https://doi.org/10.1016/j.meatsci.2005.04.015
  29. Sieczkowska H, Andrzejczuk A, Zybert A, et al. Usefulness of pork meat quality classes criteria in assessing of its culinary value. Sci Ann Polish Soc Anim Prod 2017;13:53-62. https://doi.org/10.5604/01.3001.0013.5218
  30. Zelechowska E, Przybylski W, Jaworska D, Sante-Lhoutellier V. Technological and sensory pork quality in relation to muscle and drip loss protein profiles. Eur Food Res Technol 2012;234:883-94. https://doi.org/10.1007/s00217-012-1705-z
  31. Scheffler TL, Gerrard DE. Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Sci 2007;77:7-16. https://doi.org/10.1016/j.meatsci.2007.04.024
  32. Juzl M, Sulcerova H, Gregor T, et al. The relationship between colour and other meat quality traits in Czech Large White pigs. Maso Int - J Food Sci Technol 2012;2:131-6.
  33. Jennen D, Brings A, Liu G, et al. Genetic aspects concerning drip loss and water-holding capacity of porcine meat. J Anim Breed Genet 2007;124:2-11. https://doi.org/10.1111/j.1439-0388.2007.00681.x
  34. Willson HE, Rojas de Oliveira H, Schinckel AP, Grossi D, Brito LF. Estimation of genetic parameters for pork quality, novel carcass, primal-cut and growth traits in Duroc pigs. Animals 2020;10:779. https://doi.org/10.3390/ani10050779
  35. Warner R, Greenwood P, Pethick D, Ferguson DM. Genetic and environmental effects on meat quality. Meat Sci 2010; 86:171-83. https://doi.org/10.1016/j.meatsci.2010.04.042
  36. Zaman R, Nassir HM, Abdurrazq NB, Salleh HM, Rahman MT. Effects of different methods of slaughtering on protein expression in chicken meat. IIUM Eng J 2012;13:27-33. https://doi.org/10.31436/iiumej.v13i1.227
  37. Guo Y, Xiao P, Lei S, et al. How is mRNA expression predictive for protein expression? A correlation study on human circulating monocytes. Acta Biochim Biophys Sin 2008;40:426-36. https://doi.org/10.1111/j.1745-7270.2008.00418.x
  38. Bernevic B, Petrea BA, Galetskiya D, et al. Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis. Int J Mass Spectrom 2011;305:217-27. https://doi.org/10.1016/j.ijms.2010.11.010
  39. Henderson CA, Gomez CG, Novak SM, Mi-Mi L, Gregorio CC. Overview of the muscle cytoskeleton. Compr Physiol 2017;7:891-944. https://doi.org/10.1002/cphy.c160033
  40. Wang J, Yan X-L, Liu R, Fu Q, Zhou G, Zhang W. Differences in calpain system, desmin degradation and water holding capacity between commercial Meishan and Duroc × Landrace × Yorkshire crossbred pork. Anim Sci J 2016;87:109-16. https://doi.org/10.1111/asj.12394
  41. Kristensen L, Purslow PP. The effect of ageing on the waterholding capacity of pork: role of cytoskeletal proteins. Meat Sci 2001;58:17-23. https://doi.org/10.1016/S0309-1740(00)00125-X
  42. Zhang M, Wang D, Geng Z, et al. Differential expression of heat shock protein 90, 70, 60 in chicken muscles postmortem and its relationship with meat quality. Asian-Australas J Anim Sci 2017;30:94-9. https://doi.org/10.5713/ajas.16.0132