Inhibition of pyruvate dehydrogenase accelerates anaerobic glycolysis under postmortem simulating conditions.

Autor: Taylor MJ; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Stafford CD; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Buhler JF; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Dang DS; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Alruzzi MA; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Najm TA; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., Gerrard SD; School of Animal Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States., Thornton KJ; Department of Animal, Dairy and Veterinary Sciences, Utah State University, Logan, UT 84322, United States., van Vliet S; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States., El-Kadi SW; School of Animal Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States., Gerrard DE; School of Animal Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, United States., Matarneh SK; Department of Nutrition, Dietetics and Food Sciences, Utah State University, Logan, UT 84322, United States. Electronic address: sulaiman.matarneh@usu.edu.
Jazyk: angličtina
Zdroj: Meat science [Meat Sci] 2024 Jul; Vol. 213, pp. 109510. Date of Electronic Publication: 2024 Apr 07.
DOI: 10.1016/j.meatsci.2024.109510
Abstrakt: This research aimed to explore the potential influence of mitochondria on the rate of anaerobic glycolysis. We hypothesized that mitochondria could reduce the rate of anaerobic glycolysis and pH decline by metabolizing a portion of glycolytic pyruvate. We utilized an in vitro model and incorporated CPI-613 and Avidin to inhibit pyruvate dehydrogenase (PDH) and pyruvate carboxylase (PC), respectively. Four treatments were tested: 400 μM CPI-613, 1.5 U/ml Avidin, 400 μM CPI-613 + 1.5 U/ml Avidin, or control. Glycolytic metabolites and pH of the in vitro model were evaluated throughout a 1440-min incubation period. CPI-613-containing treatments, with or without Avidin, decreased pH levels and increased glycogen degradation and lactate accumulation compared to the control and Avidin treatments (P < 0.05), indicating increased glycolytic flux. In a different experiment, two treatments, 400 μM CPI-613 or control, were employed to track the fates of pyruvate using [ 13 C 6 ]glucose. CPI-613 reduced the contribution of glucose carbon to tricarboxylic acid cycle intermediates compared to control (P < 0.05). To test whether the acceleration of acidification in reactions containing CPI-613 was due to an increase in the activity of key enzymes of glycogenolysis and glycolysis, we evaluated the activities of glycogen phosphorylase, phosphofructokinase, and pyruvate kinase in the presence or absence of 400 μM CPI-613. The CPI-613 treatment did not elicit an alteration in the activity of these three enzymes. These findings indicate that inhibiting PDH increases the rate of anaerobic glycolysis and pH decline, suggesting that mitochondria are potential regulators of postmortem metabolism.
Competing Interests: Declaration of competing interest The authors declare no conflicts of interest.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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