Evidence map›Paper›PMID 18251717›Full record

ArticleThe Biochemical journal2008

Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria.

Nadeene Parker, Charles Affourtit, Antonio Vidal-Puig, Martin D Brand

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 73 citations in OpenAlex.

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  8. Uncoupling protein 1 controls reactive oxygen species in brown adipose tissue.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  20. Endurance exercise training blunts the deleterious effect of high-fat feeding on whole body efficiency.American journal of physiology. Regulatory, integrative and comparative physiology · 2011
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Nadeene ParkerMRC Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 0XY, UK. np@mrc-dunn.cam.ac.uk
Charles Affourtit
Antonio Vidal-Puig
Martin D Brand
Unité de Nutrition Humaine · FRAddenbrooke's Hospital · GB

Funding

Medical Research Council G0400192Medical Research Council G0600717Medical Research Council MC_U105663137Wellcome Trust 065326/Z/01/ZWellcome Trust 066750/B/01/Z
6 · The paper itself

Abstract

Leak of protons into the mitochondrial matrix during substrate oxidation partially uncouples electron transport from phosphorylation of ADP, but the functions and source of basal and inducible proton leak in vivo remain controversial. In the present study we describe an endogenous activation of proton conductance in mitochondria isolated from rat and mouse skeletal muscle following addition of respiratory substrate. This endogenous activation increased with time, required a high membrane potential and was diminished by high concentrations of serum albumin. Inhibition of this endogenous activation by GDP [classically considered specific for UCPs (uncoupling proteins)], carboxyatractylate and bongkrekate (considered specific for the adenine nucleotide translocase) was examined in skeletal muscle mitochondria from wild-type and Ucp3-knockout mice. Proton conductance through endogenously activated UCP3 was calculated as the difference in leak between mitochondria from wild-type and Ucp3-knockout mice, and was found to be inhibited by carboxyatractylate and bongkrekate, but not GDP. Proton conductance in mitochondria from Ucp3-knockout mice was strongly inhibited by carboxyatractylate, bongkrekate and partially by GDP. We conclude the following: (i) at high protonmotive force, an endogenously generated activator stimulates proton conductance catalysed partly by UCP3 and partly by the adenine nucleotide translocase; (ii) GDP is not a specific inhibitor of UCP3, but also inhibits proton translocation by the adenine nucleotide translocase; and (iii) the inhibition of UCP3 by carboxyatractylate and bongkrekate is likely to be indirect, acting through the adenine nucleotide translocase.

Indexed as

AnimalsAtractylosideBongkrekic AcidEnergy MetabolismFemaleIon ChannelsMaleMalonatesMembrane Potential, MitochondrialMiceMice, KnockoutMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsMitochondria, MuscleMuscle, SkeletalNitrogen OxidesAtractylosideBongkrekic AcidcarboxyatractylosideIon ChannelsMalonatesmalonic acidMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsNitrogen OxidesnitronesPalmitatesProton PumpsSerum Albumin, BovineUCP3 protein, humanUcp3 protein, mouseUcp3 protein, ratUncoupling AgentsUncoupling Protein 3

Identifiers

PMID18251717
PMCPMC2474556
OpenAlexW1986176631

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.