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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, Nanjing 210095, China
M. F. Wang
Affiliation:
Institute for Animal Husbandry and Veterinary Research, Henan Academy of Agricultural Sciences, Huayuan Road No.116 Road, Zhengzhou 450002, 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, Nanjing 210095, China
X. S. Zhu
Affiliation:
College of Life Science and Chemistry, Jiangsu Second Normal University, West Beijing Road No.77 Road, Nanjing 210013, 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, Nanjing 210095, 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, Nanjing 210095, China
Corresponding
E-mail address:

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
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Copyright
© The Animal Consortium 2017 

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