Mitochondria-associated lactate dehydrogenase is not a biologically significant contributor to bioenergetic function in murine striated muscle.

08:00 EDT 22nd March 2019 | BioPortfolio

Summary of "Mitochondria-associated lactate dehydrogenase is not a biologically significant contributor to bioenergetic function in murine striated muscle."

Previous studies indicate that mitochondria-localized lactate dehydrogenase (mLDH) might be a significant contributor to metabolism. In the heart, the presence of mLDH could provide cardiac mitochondria with a higher capacity to generate reducing equivalents directly available for respiration, especially during exercise when circulating lactate levels are high. The purpose of this study was to test the hypothesis that mLDH contributes to striated muscle bioenergetic function. Mitochondria isolated from murine cardiac and skeletal muscle lacked an appreciable ability to respire on lactate in the absence or presence of exogenous NAD. Although three weeks of treadmill running promoted physiologic cardiac growth, mitochondria isolated from the hearts of acutely exercised or exercise-adapted mice showed no further increase in lactate oxidation capacity. In all conditions tested, cardiac mitochondria respired at >20-fold higher levels with provision of pyruvate compared with lactate. Similarly, skeletal muscle mitochondria showed little capacity to respire on lactate. Protease protection assays of isolated cardiac mitochondria confirmed that LDH is not localized within the mitochondrion. We conclude that mLDH does not contribute to cardiac bioenergetics in mice.


Journal Details

This article was published in the following journal.

Name: Redox biology
ISSN: 2213-2317
Pages: 101177


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Medical and Biotech [MESH] Definitions

A cytochrome form of lactate dehydrogenase found in the MITOCHONDRIA. It catalyzes the oxidation of L-lactate to PYRUVATE with transfer of electrons to CYTOCHROME C. The enzyme utilizes FMN and PROTOHEME IX as cofactors.

A species ARTERIVIRUS, occurring in a number of transplantable mouse tumors. Infected mice have permanently elevated serum levels of lactate dehydrogenase.

A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

An acetic acid derivative that is a metabolite of TRICHLOROETHYLENE and is formed during chlorine disinfection of drinking water. It has effects on GLUCOSE metabolism, lowers LACTATE, and activates the PYRUVATE DEHYDROGENASE COMPLEX.

Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.

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