Evidence map›Paper›PMID 27705766›Full record

ArticleBiophysical journal2016

Investigation of LRRC8-Mediated Volume-Regulated Anion Currents in Xenopus Oocytes.

Héctor Gaitán-Peñas, Antonella Gradogna, Lara Laparra-Cuervo, Carles Solsona, Victor Fernández-Dueñas, Alejandro Barrallo-Gimeno, Francisco Ciruela, Melike Lakadamyali, Michael Pusch, Raúl Estévez

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 119 citations in OpenAlex.

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17 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 1 country.

Héctor Gaitán-PeñasUnitat de Fisiología, Departament de Ciències Fisiològiques II, IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat, Spain; U-750, CIBERER, ISCIII, Spain.
Antonella GradognaIstituto di Biofisica, CNR, Genoa, Italy.
Lara Laparra-CuervoICFO-Institut de Ciències Fotòniques, The Barcelona Institute of Science and Technology, Castelldefels, Spain.
Carles SolsonaUnitat de Neurobiologia, Departament Patologia i Terapèutica Experimental IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat.
Victor Fernández-DueñasUnitat de Farmacologia, Departament Patologia i Terapèutica Experimental IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat.
Alejandro Barrallo-GimenoUnitat de Fisiología, Departament de Ciències Fisiològiques II, IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat, Spain; U-750, CIBERER, ISCIII, Spain.
Francisco CiruelaUnitat de Farmacologia, Departament Patologia i Terapèutica Experimental IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat.
Melike LakadamyaliICFO-Institut de Ciències Fotòniques, The Barcelona Institute of Science and Technology, Castelldefels, Spain.
Michael PuschIstituto di Biofisica, CNR, Genoa, Italy. Electronic address: pusch@ge.ibf.cnr.it.
Raúl EstévezUnitat de Fisiología, Departament de Ciències Fisiològiques II, IDIBELL-Universitat de Barcelona, L'Hospitalet de Llobregat, Spain; U-750, CIBERER, ISCIII, Spain. Electronic address: restevez@ub.edu.
Universitat de Barcelona · ESCentre for Biomedical Network Research on Rare Diseases · ESInstitute of Photonic Sciences · ESInstituto Biofisika · ESInstitut d'Investigació Biomédica de Bellvitge · ES

Funding

Telethon GGP12008
6 · The paper itself

Abstract

Volume-regulated anion channels (VRACs) play an important role in controlling cell volume by opening upon cell swelling. Recent work has shown that heteromers of LRRC8A with other LRRC8 members (B, C, D, and E) form the VRAC. Here, we used Xenopus oocytes as a simple system to study LRRC8 proteins. We discovered that adding fluorescent proteins to the C-terminus resulted in constitutive anion channel activity. Using these constructs, we reproduced previous findings indicating that LRRC8 heteromers mediate anion and osmolyte flux with subunit-dependent kinetics and selectivity. Additionally, we found that LRRC8 heteromers mediate glutamate and ATP flux and that the inhibitor carbenoxolone acts from the extracellular side, binding to probably more than one site. Our results also suggest that the stoichiometry of LRRC8 heteromers is variable, with a number of subunits ≥6, and that the heteromer composition depends on the relative expression of different subunits. The system described here enables easy structure-function analysis of LRRC8 proteins.

Indexed as

Adenosine TriphosphateAnimalsAnionsCarbenoxoloneExtracellular SpaceGlutamic AcidHumansIn Vitro TechniquesKineticsLuminescent ProteinsMembrane PotentialsMembrane ProteinsNeurotransmitter AgentsOocytesOsmolar ConcentrationPermeabilityAdenosine TriphosphateAnionsCarbenoxoloneGlutamic AcidLRRC8A protein, humanLuminescent ProteinsMembrane ProteinsNeurotransmitter AgentsTaurineWater

Identifiers

PMID27705766
PMCPMC5052465
OpenAlexW2528465111

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.