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Asian-Australas J Anim Sci > Volume 30(6); 2017 > Article
Asian-Australasian Journal of Animal Sciences 2017;30(6): 857-864. doi: https://doi.org/10.5713/ajas.16.0556
Histone acetyltransferase inhibitors antagonize AMP-activated protein kinase in postmortem glycolysis
Qiong Li1, Zhongwen Li2, Aihua Lou1, Zhenyu Wang2, Dequan Zhang2,*, Qingwu W. Shen1,*
1College of Food Science and Technology, Hunan Agricultural University, Changsha, Hunan 410128, China
2Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, China
* Corresponding Author: Dequan Zhang ,Tel: +86-10-62818740, Fax: +86-10-62818740, Email: dequan_zhang0118@126.com / Qingwu W. Shen ,Tel: +86-731-84617013, Fax: +86-731-84617093, Email: yaoyao3153@aliyun.com
Received: July 19, 2016;  Revised: September 12, 2016.  Accepted: October 24, 2016.  Published online October 28, 2016.

ABSTRACT
Objective:
The purpose of this study was to investigate the influence of AMP-activated protein kinase (AMPK) activation on protein acetylation and glycolysis in postmortem muscle to better understand the mechanism by which AMPK regulates postmortem glycolysis and meat quality.
Method:
A total of 32 mice were randomly assigned to four groups and intraperitoneally injected with 5-Aminoimidazole-4-carboxamide1-β-D-ribofuranoside (AICAR, a specific activator of AMPK), AICAR and histone acetyltransferase inhibitor II, or AICAR, Trichostatin A (TSA, an inhibitor of histone deacetylase I and II) and Nicotinamide (NAM, an inhibitor of the Sirt family deacetylases). After mice were euthanized, the Longissimus dorsi muscle was collected at 0 h, 45 min, and 24 h postmortem. AMPK activity, protein acetylation and glycolysis in postmortem muscle were measured.
Results:
Activation of AMPK by AICAR significantly increased glycolysis in postmortem muscle. At the same time, it increased the total acetylated proteins in muscle 45 min postmortem. Inhibition of protein acetylation by histone acetyltransferase inhibitors reduced AMPK activation induced increase in the total acetylated proteins and glycolytic rate in muscle early postmortem, while histone deacetylase inhibitors further promoted protein acetylation and glycolysis. Several bands of proteins were detected to be differentially acetylated in muscle with different glycolytic rates.
Conclusion:
Protein acetylation plays an important regulatory role in postmortem glycolysis. As AMPK mediates the effects of pre-slaughter stress on postmortem glycolysis, protein acetylation is likely a mechanism by which antemortem stress influenced postmortem metabolism and meat quality though the exact mechanism is to be elucidated.
Keywords: Postmortem Glycolysis; AMP-activated Protein Kinase (AMPK); Protein Acetylation; Pale, Soft, Exudative (PSE)
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