Evidence map›Paper›PMID 9417140›Full record

ArticleThe Journal of general physiology1998

Protease modulation of the activity of the epithelial sodium channel expressed in Xenopus oocytes.

A Chraïbi, V Vallet, D Firsov, S K Hess, J D Horisberger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

72 citing papers in PubMed, 183 citations in OpenAlex.

  1. Article
  2. Review
  3. Elevated intracellular NaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Epithelial NaAnnual review of physiology · 2018
    Review
  8. Protease-activated receptors in kidney disease progression.American journal of physiology. Renal physiology · 2016
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. ENaC regulation by proteases and shear stress.Current molecular pharmacology · 2013
    Review
  19. Acid-sensing ion channels in pathological conditions.Advances in experimental medicine and biology · 2013
    Review
  20. Article

12 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

5 authors at 1 institution in 1 country.

A ChraïbiInstitute of Pharmacology and Toxicology, University of Lausanne, CH-1005 Lausanne, Switzerland.
V Vallet
D Firsov
S K Hess
J D Horisberger
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated the effect of extracellular proteases on the amiloride-sensitive Na+ current (INa) in Xenopus oocytes expressing the three subunits alpha, beta, and gamma of the rat or Xenopus epithelial Na+ channel (ENaC). Low concentrations of trypsin (2 microg/ml) induced a large increase of INa within a few minutes, an effect that was fully prevented by soybean trypsin inhibitor, but not by amiloride. A similar effect was observed with chymotrypsin, but not with kallikrein. The trypsin-induced increase of INa was observed with Xenopus and rat ENaC, and was very large (approximately 20-fold) with the channel obtained by coexpression of the alpha subunit of Xenopus ENaC with the beta and gamma subunits of rat ENaC. The effect of trypsin was selective for ENaC, as shown by the absence of effect on the current due to expression of the K+ channel ROMK2. The effect of trypsin was not prevented by intracellular injection of EGTA nor by pretreatment with GTP-gammaS, suggesting that this effect was not mediated by G proteins. Measurement of the channel protein expression at the oocyte surface by antibody binding to a FLAG epitope showed that the effect of trypsin was not accompanied by an increase in the channel protein density, indicating that proteolysis modified the activity of the channel present at the oocyte surface rather than the cell surface expression. At the single channel level, in the cell-attached mode, more active channels were observed in the patch when trypsin was present in the pipette, while no change in channel activity could be detected when trypsin was added to the bath solution around the patch pipette. We conclude that extracellular proteases are able to increase the open probability of the epithelial sodium channel by an effect that does not occur through activation of a G protein-coupled receptor, but rather through proteolysis of a protein that is either a constitutive part of the channel itself or closely associated with it.

Indexed as

AmilorideAnimalsCalciumChymotrypsinDiureticsEpinephrineEpithelial CellsGene ExpressionGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)OocytesPatch-Clamp TechniquesRatsSecond Messenger SystemsSodium ChannelsSympathomimeticsAmilorideCalciumChymotrypsinDiureticsEpinephrineGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Sodium ChannelsSympathomimeticsTrypsin

Identifiers

PMID9417140
PMCPMC1887769
OpenAlexW2062889240

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.