References
- 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
- Fischer K. Drip loss in pork: influencing factors and relation to further meat quality traits. J Anim Breed Genet 2007;124:12-8.
- Sreedhar AS, Csermely P. Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy. Pharmacol Ther 2004; 101:227-57. https://doi.org/10.1016/j.pharmthera.2003.11.004
- Pulford DJ, Dobbie P, Fraga Vazquez S, et al. Variation in bull beef quality due to ultimate muscle pH is correlated to endopeptidase and small heat shock protein levels. Meat Sci 2009;83:1-9. https://doi.org/10.1016/j.meatsci.2008.11.008
- Lomiwes D, Farouk MM, Frost DA, Dobbie PM, Young OA. Small heat shock proteins and toughness in intermediated pHu beef. Meat Sci 2013;95:472-9. https://doi.org/10.1016/j.meatsci.2013.05.022
- 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
- Wang DY, Zhang MH, Liu F, Zhu YZ, Xu WM. Purification and characterization of a phosphatidylcholine-binding protein from duck Biceps femoris muscle. Anim Prod Sci 2014;54:194-9. https://doi.org/10.1071/AN12321
- 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
- Laville E, Sayd T, Morzel M, et al. Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization. J Agric Food Chem 2009;57:10755-64. https://doi.org/10.1021/jf901949r
- Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5. https://doi.org/10.1038/227680a0
- Warriss PD. The relationship between pH45 and drip in pig muscle. Int. J Food Sci Technol 1982;17:573-8.
- Otto G, Roehe R, Looft H, Thoelking L, Kalm E. Comparison of different methods for determination of drip loss and their relationships to meat quality and carcass characteristics in pigs. Meat Sci 2004;68:401-9. https://doi.org/10.1016/j.meatsci.2004.04.007
- Hughes JM, Oiseth SK, Purslow PP, Warner RD. A structural approach to understanding the interactions between colour, water-holding capacity and tenderness. Meat Sci 2014;98:520-32. https://doi.org/10.1016/j.meatsci.2014.05.022
- Kristensen L, Purslow PP. The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins. Meat Sci 2001;58: 17-23. https://doi.org/10.1016/S0309-1740(00)00125-X
- Young JF, Bertram HC, Oksbjerg N. Rest before slaughter ameliorates pre-slaughter stress-induced increased drip loss but not stressinduced increase in the toughness of pork. Meat Sci 2009;83:634-41. https://doi.org/10.1016/j.meatsci.2009.07.019
- Van Laack RL, Faustman C, Sebranek JG. Pork quality and the expression of stress protein Hsp70 in swine. J Anim Sci 1993;71: 2958-64. https://doi.org/10.2527/1993.71112958x
- Warriss PD, Brown SN, Gade PB, et al. An analysis of data relating to pig carcass quality and indices of stress collected in the European Union. Meat Sci 1998;49:137-44. https://doi.org/10.1016/S0309-1740(97)00133-2
- Pérez MP, Palacio J, Santolaria MP, et al. Effect of transport time on welfare and meat quality in pigs. Meat Sci 2002;61:425-33. https://doi.org/10.1016/S0309-1740(01)00216-9
- Minois N. Longevity and aging: beneficial effects of exposure to mild stress. Biogerontology 2000;1:15-29. https://doi.org/10.1023/A:1010085823990
- Yu J, Bao E, Yan J, Lei L. Expression and localization of Hsps in the heart and blood vessel of heat-stressed broilers. Cell Stress Chaperon 2008;13:327-35. https://doi.org/10.1007/s12192-008-0031-7
- Xie J, Tang L, Lu L, et al. Differential expression of heat shock transcription factors and heat shock proteins after acute and chronic heat stress in laying chickens (Gallus gallus). PloS ONE 2014;9:e102204. https://doi.org/10.1371/journal.pone.0102204
- Horvath I, Multhoff G, Sonnleitner A, Vigh L. Membrane-associated stress proteins: More than simply chaperones. Biochim Biophys Acta 2008;1778:1653-64. https://doi.org/10.1016/j.bbamem.2008.02.012
- Pfister G, Stroh CM, Perschinka H, et al. Detection of HSP60 on the membrane surface of stressed human endothelial cells by atomic force and confocal microscopy. J Cell Sci 2005;118:1587-94. https://doi.org/10.1242/jcs.02292
- Harada Y, Sato C, Kitajima K. Complex formation of 70-kDa heat shock protein with acidic glycolipids and phospholipids. Biochem Biophys Res Commun 2007;353:655-60. https://doi.org/10.1016/j.bbrc.2006.12.068
- Lambert IH, Nielsen JH, Andersen HJ, Ortenblad N. Cellular model for induction of drip loss in meat. J Agric Food Chem 2001;49:4876-83. https://doi.org/10.1021/jf010121y
- Ouali A, Herrera-Mendez CH, Coulis G, et al. Meat tenderisation and muscle cell death, two highly related events. Tehnoligija Mesa 2007;48:1-15.
- Rowe LJ, Huff-Lonergan E, Lonergan SM. Desmin degradation influences water-holding capacity and tenderness of fresh pork. J Anim Sci 2001;79:443.
-
Zhang WG, Lonergan SM, Gardner MA, Huff-Lonergan E. Contribution of postmortem changes of integrin, desmin and
$\mu$ -calpain to variation in water holding capacity of pork. Meat Sci 2006;74:578-85. https://doi.org/10.1016/j.meatsci.2006.05.008 - Averna M, Tullio RD, Pedrazzi M, et al. Interaction between calpain-1 and HSP90: New insights into the regulation of localization and activity of the protease. PloS ONE 2015;10:e0116738. https://doi.org/10.1371/journal.pone.0116738
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