Evidence map›Paper›PMID 31771171›Full record

ArticleInternational journal of molecular sciences2019

Absolute Protein Amounts and Relative Abundance of Volume-regulated Anion Channel (VRAC) LRRC8 Subunits in Cells and Tissues Revealed by Quantitative Immunoblotting.

Sumaira Pervaiz, Anja Kopp, Lisa von Kleist, Tobias Stauber

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Structure of a volume-regulated heteromeric LRRC8A/C channel.Nature structural & molecular biology · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Ion Channels and Transporters in Muscle Cell Differentiation.International journal of molecular sciences · 2021
    Review
  15. Article
  16. 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 1 country.

Sumaira PervaizInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.ORCID 0000-0002-9631-6506
Anja KoppInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.ORCID 0000-0001-5484-7109
Lisa von KleistInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.ORCID 0000-0001-9938-6510
Tobias StauberInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.ORCID 0000-0003-0727-6109
Freie Universität Berlin · DEMSH Medical School Hamburg – University of Applied Sciences and Medical University · DE

Funding

Bundesministerium für Bildung und Forschung 031A314
6 · The paper itself

Abstract

The volume-regulated anion channel (VRAC) plays an important role in osmotic cell volume regulation. In addition, it is involved in various physiological processes such as insulin secretion, glia-neuron communication and purinergic signaling. VRAC is formed by hetero-hexamers of members of the LRRC8 protein family, which consists of five members, LRRC8A-E. LRRC8A is an essential subunit for physiological functionality of VRAC. Its obligate heteromerization with at least one of its paralogues, LRRC8B-E, determines the biophysical properties of VRAC. Moreover, the subunit composition is of physiological relevance as it largely influences the activation mechanism and especially the substrate selectivity. However, the endogenous tissue-specific subunit composition of VRAC is unknown. We have now developed and applied a quantitative immunoblot study of the five VRAC LRRC8 subunits in various mouse cell lines and tissues, using recombinant protein for signal calibration. We found tissue-specific expression patterns of the subunits, and generally relative low expression of the essential LRRC8A subunit. Immunoprecipitation of LRRC8A also co-precipitates an excess of the other subunits, suggesting that non-LRRC8A subunits present the majority in hetero-hexamers. With this, we can estimate that in the tested cell lines, the number of VRAC channels per cell is in the order of 10,000, which is in agreement with earlier calculations from the comparison of single-channel and whole-cell currents.

Indexed as

3T3 CellsAnimalsCell LineElectrophoresis, Polyacrylamide GelImmunoblottingImmunoprecipitationMaleMembrane ProteinsMiceVoltage-Dependent Anion ChannelsLRRC8A protein, mouseMembrane ProteinsVoltage-Dependent Anion Channelsanion channelheteromeric complexleucine-rich repeat-containingrecombinant proteinsubunit stoichiometrytissue-specific protein expressionvolume-regulated anion channel VRACvolume-sensitive organic outward rectifying channel VSOR

Identifiers

PMID31771171
PMCPMC6928916
OpenAlexW2989678979

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Registered trials

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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.