ArticleJournal of bioenergetics and biomembranes2005
In phosphorylating Acanthamoeba castellanii mitochondria the sensitivity of uncoupling protein activity to GTP depends on the redox state of quinone.
Article in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 28 citations in OpenAlex.
- Understanding coenzyme Q.Physiological reviews · 2024Review
- Article
- Loss of Myostatin Alters Mitochondrial Oxidative Phosphorylation, TCA Cycle Activity, and ATP Production in Skeletal Muscle.International journal of molecular sciences · 2022Article
- The interplay between mitochondrial reactive oxygen species formation and the coenzyme Q reduction level.Redox biology · 2018Article
- Being right on Q: shaping eukaryotic evolution.The Biochemical journal · 2016Review
- Hydroxynonenal, a lipid peroxidation end product, stimulates uncoupling protein activity in Acanthamoeba castellanii mitochondria; the sensitivity of the inducible activity to purine nucleotides depends on the membranous ubiquinone redox state.Journal of bioenergetics and biomembranes · 2012Article
- Impact of oxidative stress on Acanthamoeba castellanii mitochondrial bioenergetics depends on cell growth stage.Journal of bioenergetics and biomembranes · 2011Article
- Mitochondrial function plasticity in Acanthamoeba castellanii during growth in batch culture.Journal of bioenergetics and biomembranes · 2007Article
- Fatty acid efficiency profile in uncoupling of Acanthamoeba castellanii mitochondria.Journal of bioenergetics and biomembranes · 2007Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In isolated Acanthamoeba castellanii mitochondria respiring in state 3 with external NADH or succinate, the linoleic acid-induced purine nucleotide-sensitive uncoupling protein activity is able to uncouple oxidative phosphorylation. The linoleic acid-induced uncoupling can be inhibited by a purine nucleotide (GTP) when quinone (Q) is sufficiently oxidized, indicating that in A. castellanii mitochondria respiring in state 3, the sensitivity of uncoupling protein activity to GTP depends on the redox state of the membranous Q. Namely, the inhibition of the linoleic acid-induced uncoupling by GTP is not observed in uninhibited state 3 respiration as well as in state 3 respiration progressively inhibited by complex III inhibitors, i.e., when the rate of quinol (QH(2))-oxidizing pathway is decreased. On the contrary, the progressive decrease of state 3 respiration by declining respiratory substrate availability (by succinate uptake limitation or by decreasing external NADH concentration), i.e., when the rate of Q-reducing pathways is decreased, progressively leads to a full inhibitory effect of GTP. Moreover, in A. castellanii mitochondria isolated from cold-treated cells, where a higher uncoupling protein activity is observed, the inhibition of the linoleic acid-induced proton leak by GTP is revealed for the same low values of the Q reduction level.
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