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Guanidinoacetic acid regulated postmortem muscle glycolysis associated with AMPK signaling and protein acetylation |
Ning Liu1 
, Bolin Zhang2,3,*
, Shubai Wang2
, Qingzhen Zhong1
, Zewei Sun1,*
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1College of Animal Science and Technology, Jilin Agricultural University, No. 2888, Xincheng Road, Jingyue District, Changchun 130118, China
2College of Animal Science and Technology, Qingdao Agricultural University, Chang Cheng Road, Cheng Yang District, Qingdao 266109, China
3Department of Biology and Agriculture, Zunyi Normal College, Ping’an Avenue, Hong Huagang District, Zunyi 563006, China |
Correspondence:
Bolin Zhang, Tel: +86-532-58957780, Fax: +86-532-58957780, Email: bolin-zhang@163.com
Zewei Sun,Email: sunzeweicaj@163.com
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Received: 20 June 2024 • Revised: 3 September 2024 • Accepted: 14 October 2024 |
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| Abstract |
Objective
Antemortem stress accelerated muscle energy consumption in postmortem muscle. The objective of our study was to investigate the regulation of guanidinoacetic acid (GAA) administration on the postmortem glycolysis and protein acetylation in postmortem muscle of antemortem stress.
Methods
Forty C57BL/6 male mice were chosen and randomly assigned to four treatment groups (A, B, C and D), each treatment consisted of 10 replicates. Mice in group B, C and D were treated with 0.05% GAA oral administration for 6 days. On the 7th day of the experiment, the mice in group A and B were injected with saline, and mice in group C and D were injected with 5-aminoimidazole-4-carboxamide1-β-D-ribofuranoside (AICAR,50 μg/g body weight) and a combined injection with AICAR (50 μg/g body weight) and histone acetylase inhibitor Ⅱ (HAT Ⅱ,185 μg/g body weight), respectively.
Results
The results showed that the values of pH45min and pH24h of postmortem muscle in GAA administration were higher than those in the control group. However, the opposite result was observed in AICAR group. Moreover, the activities of acetone kinase, hexokinase and fruc-tose-2,6-diphosphatase, combined with the protein abundance of phosphorylated liver kinase, phosphorylated AMPKα2 and total acetylated protein were all decreased by GAA administration and HAT Ⅱ treatment.
Conclusion
Taken together, AMPK signaling and protein acetylation could mediate the regulation of GAA administration on postmortem glycolysis of antemortem stress-muscle.
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| Keywords:
AMPK Signaling; Antemortem Stress; Glycolysis; Guanidinoacetic Acid; Protein Acetylation |
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