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Metabolic clearance of oxaloacetate and mitochondrial complex II respiration: Divergent control in skeletal muscle and brown adipose tissue
Journal article   Open access   Peer reviewed

Metabolic clearance of oxaloacetate and mitochondrial complex II respiration: Divergent control in skeletal muscle and brown adipose tissue

Adam J. Rauckhorst, Liping Yu, Brian D. Fink, Ritu Som, Eric B. Taylor and William I. Sivitz
Biochimica et biophysica acta. Bioenergetics, Vol.1864(1), pp.148930-148930
01/01/2023
DOI: 10.1016/j.bbabio.2022.148930
PMCID: PMC10225247
PMID: 36272463
url
https://doi.org/10.1016/j.bbabio.2022.148930View
Published (Version of record) Open Access

Abstract

At low inner mitochondrial membrane potential (AT) oxaloacetate (OAA) accumulates in the organelles concurrently with decreased complex II-energized respiration. This is consistent with AT -dependent OAA in-hibition of succinate dehydrogenase. To assess the metabolic importance of this process, we tested the hypothesis that perturbing metabolic clearance of OAA in complex II-energized mitochondria would alter O2 flux and, further, that this would occur in both AT and tissue-dependent fashion. We carried out respiratory and metabolite studies in skeletal muscle and interscapular brown adipose tissue (IBAT) directed at the effect of OAA transamination to aspartate (catalyzed by the mitochondrial form of glutamic-oxaloacetic transaminase, Got2) on complex II-energized respiration. Addition of low amounts of glutamate to succinate-energized mitochondria at low AT increased complex II (succinate)-energized respiration in muscle but had little effect in IBAT mito-chondria. The transaminase inhibitor, aminooxyacetic acid, increased OAA concentrations and impaired succinate-energized respiration in muscle but not IBAT mitochondria at low but not high AT. Immunoblotting revealed that Got2 expression was far greater in muscle than IBAT mitochondria. Because we incidentally observed metabolism of OAA to pyruvate in IBAT mitochondria, more so than in muscle mitochondria, we also examined the expression of mitochondrial oxaloacetate decarboxylase (ODX). ODX was detected only in IBAT mitochondria. In summary, at low but not high AT, mitochondrial transamination clears OAA preventing loss of complex II respiration: a process far more active in muscle than IBAT mitochondria. We also provide evidence that OAA decarboxylation clears OAA to pyruvate in IBAT mitochondria.
Biophysics Biochemistry & Molecular Biology Life Sciences & Biomedicine Science & Technology

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