Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/80300
Type: Artigo de periódico
Title: Redox state of endogenous coenzyme Q modulates the inhibition of linoleic acid-induced uncoupling by guanosine triphosphate in isolated skeletal muscle mitochondria
Author: Jarmuszkiewicz, W
Navet, R
Alberici, LC
Douette, P
Sluse-Goffart, CM
Sluse, FE
Vercesi, AE
Abstract: The skeletal muscle mitochondria contain two isoforms of uncoupling protein, UCP2 and mainly UCP3, which had been shown to be activated by free fatty acids and inhibited by purine nucleotides in reconstituted systems. On the contrary in isolated mitochondria, the protonophoretic action of muscle UCPs had failed to be demonstrated in the absence of superoxide production. We showed here for the first time that muscle UCPs were activated in state 3 respiration by linoleic acid and dissipated energy from oxidative phosphorylation by decreasing the ADP/O ratio. The efficiency of UCPs in mitochondrial uncoupling increased when the state 3 respiratory rate decreased. The inhibition of the linoleic acid-induced uncoupling by a purine nucleotide (GTP), was not observed in state 4 respiration, in uninhibited state 3 respiration, as well as in state 3 respiration inhibited by complex III inhibitors. On the contrary, the progressive inhibition of state 3 respiration by n-butyl malonate, which inhibits the uptake of succinate, led to a full inhibitory effect of GTP. Therefore, as the inhibitory effect of GTP was observed only when the reduced state of coenzyme Q was decreased, we propose that the coenzyme Q redox state could be a metabolic sensor that modulates the purine nucleotide inhibition of FFA-activated UCPs in muscle mitochondria.
Subject: muscle
mitochondria
uncoupling proteins
coenzyme Q
purine nucleotide inhibition
Country: EUA
Editor: Kluwer Academic/plenum Publ
Rights: fechado
Identifier DOI: 10.1023/B:JOBB.0000047331.25248.7a
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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