Evidence map›Paper›PMID 19705265›Full record

ArticleJournal of bioenergetics and biomembranes2009

Uncoupling protein-1 (UCP1) contributes to the basal proton conductance of brown adipose tissue mitochondria.

Nadeene Parker, Paul G Crichton, Antonio J Vidal-Puig, Martin D Brand

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Uncoupling Protein 1 Does Not Produce Heat without Activation.International journal of molecular sciences · 2022
    Review
  3. Mitochondrial HAnnual review of physiology · 2022
    Review
  4. Review
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  6. Review
  7. Article
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  12. Effects of caloric restriction on the expression of lipocalin-2 and its receptor in the brown adipose tissue of high-fat diet-fed mice.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2019
    Article
  13. Article
  14. Review
  15. UCP2- and non-UCP2-mediated electric current in eukaryotic cells exhibits different properties.Environmental science and pollution research international · 2015
    Article
  16. Review
  17. Article
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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 3 institutions in 2 countries.

Nadeene ParkerMRC Mitochondrial Biology Unit, Wellcome Trust / MRC Building, Hills Road, Cambridge, CB2 0XY, UK. n.parker@ucl.ac.uk
Paul G Crichton
Antonio J Vidal-Puig
Martin D Brand
MRC Mitochondrial Biology Unit · GBAddenbrooke's Hospital · GBUniversity College London · GB

Funding

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

Abstract

Proton leak pathways uncouple substrate oxidation from ATP synthesis in mitochondria. These pathways are classified as basal (not regulated) or inducible (activated and inhibited). Previously it was found that over half of the basal proton conductance of muscle mitochondria was catalyzed by the adenine nucleotide translocase (ANT), an abundant mitochondrial anion carrier protein. To determine whether ANT is the unique protein catalyst, or one of many proteins that catalyze basal proton conductance, we measured proton leak kinetics in mitochondria isolated from brown adipose tissue (BAT). BAT can express another mitochondrial anion carrier, UCP1, at concentrations similar to ANT. Basal proton conductance was measured under conditions where UCP1 and ANT were catalytically inactive and was found to be lower in mitochondria from UCP1 knockout mice compared to wild-type. Ablation of another abundant inner membrane protein, nicotinamide nucleotide transhydrogenase, had no effect on proton leak kinetics in mitochondria from liver, kidney or muscle, showing that basal proton conductance is not catalyzed by all membrane proteins. We identify UCP1 as a second protein propagating basal proton leak, lending support to the hypothesis that basal leak pathways are perpetrated by members of the mitochondrial anion carrier family but not by other mitochondrial inner membrane proteins.

Indexed as

Adipose Tissue, BrownAnimalsCells, CulturedElectric ConductivityFemaleIon Channel GatingIon ChannelsMaleMiceMice, KnockoutMitochondriaMitochondrial ProteinsProtonsUncoupling Protein 1Ion ChannelsMitochondrial ProteinsProtonsUcp1 protein, mouseUncoupling Protein 1

Identifiers

PMID19705265
OpenAlexW1988436663

What OpenQuestion holds

Textmetadata
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.