- Volume 30 Issue 2
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Changes in expression of monocarboxylate transporters, heat shock proteins and meat quality of Large White Yorkshire and Ghungroo pigs during hot summer period
- Parkunan, Thulasiraman ;
- Das, Arun K. ;
- Banerjee, Dipak ;
- Mohanty, Niharika ;
- Paul, Avishek ;
- Nanda, P.K. ;
- Biswas, TK ;
- Naskar, Syamal ;
- Bag, Sadhan ;
- Sarkar, Mihir ;
- Mohan, Narayana H. ;
- Das, Bikash Chandra
- Received : 2016.01.07
- Accepted : 2016.05.12
- Published : 2017.02.01
Objective: Present study explores the effect of hot summer period on the glycolytic rate of early post-mortem meat quality of Ghungroo and Large White Yorkshire (LWY) pig and comparative adaptability to high temperature between above breeds by shifting the expression of stress related genes like mono-carboxylate transporters (MCTs) and heat shock proteins (HSPs). Methods: Healthy pigs of two different breeds, viz., LYW and Ghungroo (20 from each) were maintained during hot summer period (May to June) with a mean temperature of about
Ghungroo Pig;Glycolytic Rate;Heat Shock Proteins (HSPs);Meat Quality;Mono-carboxylate Transporters (MCTs);Large White Yorkshire;Summer Stress
- Baumgard LH, Rhoads RP, Rhoads ML, et al. Impact of climate change on livestock production. In: Sejian V, Naqvi SMK, Ezeji T, Lakritz J, Lal R, editors. Environmental stress and amelioration in livestock production. 1st ed: Springer; 2012. p. 413-68.
- Berton MP, de Cassia Dourado R, de Lima FBF, et al. Growingfinishing performance and carcass yield of pigs reared in a climate-controlled and uncontrolled environment. Int J Biometeorol 2015; 59:955-60. https://doi.org/10.1007/s00484-014-0908-3
- 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
- Luca AD, Mullen AM, Elia G, Davey G, Hamill RM. Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity. Meat Sci 2011;88:261-70. https://doi.org/10.1016/j.meatsci.2010.12.033
- Yu J, Tang S, Bao E, et al. The effect of transportation on the expression of heat shock proteins and meat quality of M. longissimus dorsi in pigs. Meat Sci 2009;83:474-8. https://doi.org/10.1016/j.meatsci.2009.06.028
- Ruusunen M, Puolanne E. Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties. Meat Sci 2004;67:533-9. https://doi.org/10.1016/j.meatsci.2003.12.008
- Essen-Gustavsson B. Activity-and inactivity-related muscle adaptation in the animal kingdom. 2nd ed. Champaigne, IL: Human Kinetic Publishers; 1986.
- Poole RC, Halestrap AP. Transport of lactate and other monocarboxylates across mammalian plasma membranes. Am J Physiol Cell Physiol 1993;264:C761-C82. https://doi.org/10.1152/ajpcell.1993.264.4.C761
- Halestrap A, Price N. The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Biochem J 1999;343:281-99. https://doi.org/10.1042/bj3430281
- Ryu Y, Choi Y, Kim B. Variations in metabolite contents and protein denaturation of the Longissimus dorsi muscle in various porcine quality classifications and metabolic rates. Meat Sci 2005;71:522-9. https://doi.org/10.1016/j.meatsci.2005.04.034
- Scheffler T, Gerrard D. 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
- Choe J, Choi Y, Lee S, et al. The relation between glycogen, lactate content and muscle fiber type composition, and their influence on postmortem glycolytic rate and pork quality. Meat Sci 2008; 80:355-62. https://doi.org/10.1016/j.meatsci.2007.12.019
- Dreiling C, Brown D, Casale L, Kelly L. Muscle glycogen: comparison of iodine binding and enzyme digestion assays and application to meat samples. Meat Sci 1987;20:167-77. https://doi.org/10.1016/0309-1740(87)90009-X
- Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001;29:e45. https://doi.org/10.1093/nar/29.9.e45
- Honikel K. How to measure the water-holding capacity of meat? Recommendation of standardized methods. Evaluation and control of meat quality in pigs. Dublin, Ireland: Springer; 1987. p. 129-42.
- Sierra I. Production of young and heavy lamb in the Aragonese rasa breed. Zaragoza, Spain: Institute of Economy and Productions Livestock of the Ebro 1973;18 1973;18.
- Maria G, Villarroel M, Chacon G, Gebresenbet G. Scoring system for evaluating the stress to cattle of commercial loading and unloading. Vet Record 2004;154:818-21. https://doi.org/10.1136/vr.154.26.818
- Shaw F, Tume R. The assessment of pre-slaughter and slaughter treatments of livestock by measurement of plasma constituents-a review of recent work. Meat Sci 1992;32:311-29. https://doi.org/10.1016/0309-1740(92)90095-L
- Dzugaj A. Localization and regulation of muscle fructose-1, 6-bisphosphatase, the key enzyme of glyconeogenesis. Adv Enzyme Regul 2006;46:51-71. https://doi.org/10.1016/j.advenzreg.2006.01.021
- Hambrecht E, Eissen J, Newman D, et al. Preslaughter handling effects on pork quality and glycolytic potential in two muscles differing in fiber type composition. J Anim Sci 2005;83:900-7. https://doi.org/10.2527/2005.834900x
- Yla-Ajos MS, Lindahl G, Young JF, et al. Post-mortem activity of the glycogen debranching enzyme and change in the glycogen pools in porcine M. longissimus dorsi from carriers and noncarriers of the RN-gene. Meat Sci 2007;75:112-9. https://doi.org/10.1016/j.meatsci.2006.06.018
- Aalhus J, Best D, Murray A, Jones S. A comparison of the quality characteristics of pale, soft and exudative beef and pork. J Muscle Foods 1998;9:267-80. https://doi.org/10.1111/j.1745-4573.1998.tb00660.x
- Henckel P, Karlsson A, Oksbjerg N, Petersen JS. Control of post mortem pH decrease in pig muscles: experimental design and testing of animal models. Meat Sci 2000;55:131-8. https://doi.org/10.1016/S0309-1740(99)00135-7
- Sellier P, Monin G. Genetics of pig meat quality: a review. J Muscle Foods 1994;5:187-219. https://doi.org/10.1111/j.1745-4573.1994.tb00530.x
- Ryu Y, Kim B. Comparison of histochemical characteristics in various pork groups categorized by postmortem metabolic rate and pork quality. J Anim Sci 2006;84:894-901. https://doi.org/10.2527/2006.844894x
- Bendall JR. Postmortem changes in muscle. In: Bourne GH, editor. The structure and function of muscle. New York: Academic Press; 1973. p. 244-309.
- Przybylski W, Vernin P, Monin G. Relationship between glycolytic potential and ultimate pH in bovine, porcine and ovine muscles. J Muscle Foods 1994;5:245-55. https://doi.org/10.1111/j.1745-4573.1994.tb00534.x
- Sahlin K. Intracellular pH and energy metabolism in skeletal muscle of man with special reference to exercise. Acta physiol Scand Suppl 1978;455:1-56.
- van de Wiel DF, Zhang WL. Identification of pork quality parameters by proteomics. Meat Sci 2007;77:46-54. https://doi.org/10.1016/j.meatsci.2007.04.017
- Fischer K. Drip loss in pork: influencing factors and relation to further meat quality traits. J Anim Breed Genet 2007;124:12-18.
- Immonen K, Ruusunen M, Puolanne E. Some effects of residual glycogen concentration on the physical and sensory quality of normal pH beef. Meat Sci 2000;55:33-8. https://doi.org/10.1016/S0309-1740(99)00122-9
- Nollet LM, Toldra F. Handbook of muscle foods analysis. 1st ed: Boka Raton, FL: CRC Press; 2008.
- Bernard C, Cassar-Malek I, Le Cunff M, et al. New indicators of beef sensory quality revealed by expression of specific genes. J Agric Food Chem 2007;55:5229-37. https://doi.org/10.1021/jf063372l
- Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J Leukocyte Biol 2007;81:15-27. https://doi.org/10.1189/jlb.0306167
- Kiang JG, Tsokos GC. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 1998;80: 183-201. https://doi.org/10.1016/S0163-7258(98)00028-X
- Parkunan T, Banerjee D, Mohanty N, et al. A comparative study on the expression profile of MCTs and HSPs in Ghungroo and Large White Yorkshire breeds of pigs during different seasons. Cell Stress Chaperones 2015;20:441-9. https://doi.org/10.1007/s12192-014-0569-5
- Rylander MN, Feng Y, Bass J, Diller KR. Thermally induced injury and heat‐shock protein expression in cells and tissues. Ann NY Acad Sci 2006;1066:222-42.
- Dangi SS, Gupta M, Maurya D, et al. Expression profile of HSP genes during different seasons in goats (Capra hircus). Trop Anim Health Prod 2012;44:1905-12. https://doi.org/10.1007/s11250-012-0155-8
- Sepponen K. Monocarboxylate transporters and heat shock proteins in domestic pigs in relation to stress and meat quality [dissertation]. Helsinki: University of Helsinki; 2008.
- Dimmer K, Friedrich B, Lang F, Deitmer J, Broer S. The low-affinity monocarboxylate transporter MCT4 is adapted to the export of lactate in highly glycolytic cells. Biochem J 2000;350:219-27. https://doi.org/10.1042/bj3500219
- Lin R-Y, Vera JC, Chaganti RS, Golde DW. Human monocarboxylate transporter 2 (MCT2) is a high affinity pyruvate transporter. J Biol Chem 1998;273:28959-65. https://doi.org/10.1074/jbc.273.44.28959
- Wilson MC, Jackson VN, Heddle C, et al. Lactic acid efflux from white skeletal muscle is catalyzed by the monocarboxylate transporter isoform MCT3. J Biol Chem 1998;273:15920-6. https://doi.org/10.1074/jbc.273.26.15920
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Supported by : Department of Biotechnology