Antemortem stress regulates protein acetylation and glycolysis in postmortem muscle. (1st July 2016)

• Record Type: Journal Article
• Authors: Li, Zhongwen; Li, Xin; Wang, Zhenyu; Shen, Qingwu W.; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 202(2016)
• Page Start: 94
• Page End: 98
• Publication Date: 2016-07-01
• Subjects: HAT -- HDAC -- Protein acetylation -- Postmortem glycolysis -- PSE; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2016.01.085
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Protein acetylation regulates glycolysis in postmortem muscle. Pre-slaughter stress increases total acetylated proteins in muscle early postmortem. Pre-slaughter stress increases postmortem glycolysis by protein acetylation. Pyruvate kinase activity is activated by acetylation. Abstract: Although exhaustive research has established that preslaughter stress is a major factor contributing to pale, soft, exudative (PSE) meat, questions remain regarding the biochemistry of postmortem glycolysis. In this study, the influence of preslaughter stress on protein acetylation in relationship to glycolysis was studied. The data show that antemortem swimming significantly enhanced glycolysis and the total acetylated proteins in postmortem longissimus dorsi (LD) muscle of mice. Inhibition of protein acetylation by histone acetyltransferase (HAT) inhibitors eliminated stress induced increase in glycolysis. Inversely, antemortem injection of histone deacetylase (HDAC) inhibitors, trichostatin A (TSA) and nicotinamide (NAM), further increased protein acetylation early postmortem and the glycolysis. These data provide new insight into the biochemistry of postmortem glycolysis by showing that protein acetylation regulates glycolysis, which may participate in the regulation of preslaughter stress on glycolysis in postmortem muscle.