Hostname: page-component-8448b6f56d-c4f8m Total loading time: 0 Render date: 2024-04-17T05:06:26.378Z Has data issue: false hasContentIssue false

Expression of heat shock protein 70 in transport-stressed broiler pectoralis major muscle and its relationship with meat quality

Published online by Cambridge University Press:  12 January 2017

T. Xing
Affiliation:
National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, Nanjing Agricultural University, Weigang No.1, Nanjing210095, China
M. F. Wang
Affiliation:
Institute for Animal Husbandry and Veterinary Research, Henan Academy of Agricultural Sciences, Huayuan Road No.116 Road, Zhengzhou450002, China
M. Y. Han
Affiliation:
National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, Nanjing Agricultural University, Weigang No.1, Nanjing210095, China
X. S. Zhu
Affiliation:
College of Life Science and Chemistry, Jiangsu Second Normal University, West Beijing Road No.77 Road, Nanjing210013, China
X. L. Xu*
Affiliation:
National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, Nanjing Agricultural University, Weigang No.1, Nanjing210095, China
G. H. Zhou
Affiliation:
National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, Nanjing Agricultural University, Weigang No.1, Nanjing210095, China
*
Get access

Abstract

Omics research has indicated that heat shock protein 70 (HSP70) is a potential biomarker of meat quality. However, the specific changes and the potential role of HSP70 in postmortem meat quality development need to be further defined. In this study, Arbor Acres broiler chickens (n=126) were randomly categorized into three treatment groups of unstressed control (C), 0.5-h transport (T) and subsequent water shower spray following transport (T/W). Each treatment consisted of six replicates with seven birds each. The birds were transported according to a designed protocol. The pectoralis major (PM) muscles of the transport-stressed broilers were categorized as normal and pale, soft and exudative (PSE)-like muscle samples according to L* and pH24 h values to test the expression and location of HSP70. Results revealed that the activities of plasma creatine kinase and lactate dehydrogenase increased significantly (P<0.05) in normal and PSE-like muscle samples after transportation. The mRNA expression of HSP70 in normal muscle samples increased significantly (P<0.05) compared with that in the controls after stress. The protein expression of HSP70 increased significantly in normal muscle samples and decreased significantly (P<0.05) in PSE-like muscles. Immuno-fluorescence showed that HSP70 was present in the cytoplasm and on surface membranes of PM muscle cells in the normal samples following stress. Meanwhile, HSP70 was present on the surface membranes and extracellular matrix but was barely visible in the cytoplasm of the PSE-like samples. Principal component analysis showed high correlations between HSP70 and meat quality and stress indicators. In conclusion, this research suggests that the variation in HSP70 expression may provide a novel insight into the pathways underlying meat quality development.

Type
Research Article
Copyright
© The Animal Consortium 2017 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Adzitey, F and Nurul, H 2011. Pale soft exudative (PSE) and dark firm dry (DFD) meats: causes and measures to reduce these incidences – a mini review. International Food Research Journal 18, 1120.Google Scholar
Åkerfelt, M, Morimoto, RI and Sistonen, L 2010. Heat shock factors: integrators of cell stress, development and lifespan. Nature Reviews Molecular Cell Biology 11, 545555.CrossRefGoogle ScholarPubMed
Al-Aqil, A and Zulkifli, I 2009. Changes in heat shock protein 70 expression and blood characteristics in transported broiler chickens as affected by housing and early age feed restriction. Poultry Science 88, 13581364.Google Scholar
Barbut, S 2012. Convenience breaded poultry meat products – new developments. Trends in Food Science & Technology 26, 1420.Google Scholar
Bjarnadóttir, SaGn, Hollung, K, Færgestad, EM and Veiseth-Kent, E 2010. Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: shifts in energy status and myofibrillar stability. Journal of Agricultural and Food Chemistry 58, 74087414.Google Scholar
Delezie, E, Swennen, Q, Buyse, J and Decuypere, E 2007. The effect of feed withdrawal and crating density in transit on metabolism and meat quality of broilers at slaughter weight. Poultry Science 86, 14141423.Google Scholar
De Maio, A 2011. Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. Cell Stress and Chaperones 16, 235249.Google Scholar
Di Luca, A, Mullen, AM, Elia, G, Davey, G and Hamill, RM 2011. Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity. Meat Science 88, 261270.Google Scholar
Gabriel, JE, Ferro, JA, Stefani, RMP, Ferro, MIT, Gomes, SL and Macari, M 1996. Effect of acute heat stress on heat shock protein 70 messenger RNA and on heat shock protein expression in the liver of broilers. British Poultry Science 37, 443449.Google Scholar
Guarnieri, PD, Soares, AL, Olivo, R, Schneider, JP and Macedo, RM 2004. Preslaughter handling with water shower spray inhibits PSE (Pale, Soft, Exudative) broiler breast meat in a commercial plant. Biochemical and ultrastructural observations. Journal of Food Biochemistry 28, 269277.Google Scholar
Hao, Y and Gu, X 2014. Effects of heat shock protein 90 expression on pectoralis major oxidation in broilers exposed to acute heat stress. Poultry Science 1, 27092717.Google Scholar
Huff-Lonergan, E and Lonergan, SM 2005. Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Science 71, 194204.Google Scholar
Jiang, N, Wang, P, Xing, T, Han, M and Xu, X 2016. An evaluation of the effect of water-misting sprays with forced ventilation on the occurrence of pale, soft, and exudative meat in transported broilers during summer: impact of the thermal microclimate. Journal of Animal Science 94, 22182227.Google Scholar
Khazzaka, A, Figwer, P, Poirel, M, Serrar, M and Franck, M 2006. Hsp70 response in pigs is affected by their Halothane genotypes after heat stress. Journal of Thermal Biology 31, 605610.CrossRefGoogle Scholar
Kim, YHB, Warner, RD and Rosenvold, K 2014. Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review. Animal Production Science 54, 375395.Google Scholar
Larkins, NT, Murphy, RM and Lamb, GD 2012. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. American Journal of Physiology – Cell Physiology 303, 654665.CrossRefGoogle ScholarPubMed
Mathur, S, Walley, KR, Wang, Y, Indrambarya, T and Boyd, JH 2011. Extracellular heat shock protein 70 induces cardiomyocyte inflammation and contractile dysfunction via TLR2. Circulation Journal 75, 24452452.CrossRefGoogle ScholarPubMed
Mayer, M and Bukau, B 2005. Hsp70 chaperones: cellular functions and molecular mechanism. Cellular and Molecular Life Sciences 62, 670684.Google Scholar
Milne, KJ and Noble, EG 2002. Exercise-induced elevation of HSP70 is intensity dependent. Journal of Applied Physiology 93, 561568.CrossRefGoogle ScholarPubMed
Neufer, P, Ordway, G, Hand, GA, Shelton, JM, Richardson, JA, Benjamin, IJ and Williams, RS 1996. Continuous contractile activity induces fiber type specific expression of HSP70 in skeletal muscle. American Journal of Physiology – Cell Physiology 271, 18281837.Google Scholar
Periale, L, Peskov, V, Iacobaeus, C, Francke, T and Pavlopoulos, N 2015. The effect of different degrees of feed restriction on heat shock protein 70, acute phase proteins, and other blood parameters in female broiler breeders. Poultry Science 94, 23222329.Google Scholar
Sandercock, D, Hunter, R, Nute, G, Mitchell, M and Hocking, P 2001. Acute heat stress-induced alterations in blood acid-base status and skeletal muscle membrane integrity in broiler chickens at two ages: implications for meat quality. Poultry Science 80, 418425.Google Scholar
Scheffler, T and Gerrard, D 2007. Mechanisms controlling pork quality development: the biochemistry controlling postmortem energy metabolism. Meat Science 77, 716.Google Scholar
Soleimani, AF, Zulkifli, I, Omar, AR and Raha, AR 2011. Physiological responses of 3 chicken breeds to acute heat stress. Poultry Science 90, 14351440.CrossRefGoogle ScholarPubMed
Song, D-J and King, AJ 2015. Effects of heat stress on broiler meat quality. World’s Poultry Science Journal 71, 701709.CrossRefGoogle Scholar
Sugimoto, M, Furuoka, H and Sugimoto, Y 2003. Deletion of one of the duplicated Hsp70 genes causes hereditary myopathy of diaphragmatic muscles in Holstein‐Friesian cattle. Animal Genetics 34, 191197.Google Scholar
Vega, VL, Rodríguez-Silva, M, Frey, T, Gehrmann, M, Diaz, JC, Steinem, C, Multhoff, G, Arispe, N and De Maio, A 2008. Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. The Journal of Immunology 180, 42994307.Google Scholar
Warriss, PD and Brown, SN 1987. The relationships between initial pH, reflectance and exudation in pig muscle. Meat Science 20, 6574.Google Scholar
Xie, J, Tang, L, Lu, L, Zhang, L, Xi, L, Liu, H-C, Odle, J and Luo, X 2014. Differential expression of heat shock transcription factors and heat shock proteins after acute and chronic heat stress in laying chickens (Gallus gallus). Plos One 9, e102204.Google Scholar
Xing, T, Xu, X, Zhou, G, Wang, P and Jiang, N 2015. The effect of transportation of broilers during summer on the expression of heat shock protein 70, postmortem metabolism and meat quality. Journal of Animal Science 93, 6270.Google Scholar
Yu, J, Tang, S, Bao, E, Zhang, M, Hao, Q and Yue, Z 2009. The effect of transportation on the expression of heat shock proteins and meat quality of M. longissimus dorsi in pigs. Meat Science 83, 474478.Google Scholar
Zhang, L and Barbut, S 2005. Rheological characteristics of fresh and frozen PSE, normal and DFD chicken breast meat. British Poultry Science 46, 687693.Google Scholar