Evidence map›Paper›PMID 18504317›Full record

ArticleThe Journal of general physiology2008

Surface expression of epithelial Na channel protein in rat kidney.

Gustavo Frindt, Zuhal Ergonul, Lawrence G Palmer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

68 citing papers in PubMed, 104 citations in OpenAlex.

  1. Trial
  2. ENaC processing in rat kidney: effects of salt loading and ADH.American journal of physiology. Renal physiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Control of ENaC ubiquitination.American journal of physiology. Renal physiology · 2024
    Article
  9. Article
  10. Article
  11. High dietary KAmerican journal of physiology. Renal physiology · 2023
    Article
  12. Article
  13. Article
  14. Expression of ENaC subunits in epithelia.The Journal of general physiology · 2022
    Article
  15. Article
  16. Cleavage state of γENaC in mouse and rat kidneys.American journal of physiology. Renal physiology · 2021
    Article
  17. Article
  18. Aldosterone-dependent and -independent regulation of NaAmerican journal of physiology. Renal physiology · 2020
    Article
  19. Ubiquitination of renal ENaC subunits in vivo.American journal of physiology. Renal physiology · 2020
    Article
  20. Article

8 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

3 authors at 1 institution in 1 country.

Gustavo FrindtDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY 10065, USA.
Zuhal Ergonul
Lawrence G Palmer
Cornell University · US

Funding

Epithelial Na Channels and Regulation of Na ExcretionR01DK059659 · NIDDK · WEILL MEDICAL COLL OF CORNELL UNIV · PI PALMER, LAWRENCE G · 2002 to 2012
$3.7M
NIDDK NIH HHS DK59659NIDDK NIH HHS R01 DK059659
6 · The paper itself

Abstract

Expression of epithelial Na channel (ENaC) protein in the apical membrane of rat kidney tubules was assessed by biotinylation of the extracellular surfaces of renal cells and by membrane fractionation. Rat kidneys were perfused in situ with solutions containing NHS-biotin, a cell-impermeant biotin derivative that attaches covalently to free amino groups on lysines. Membranes were solubilized and labeled proteins were isolated using neutravidin beads, and surface beta and gammaENaC subunits were assayed by immunoblot. Surface alphaENaC was assessed by membrane fractionation. Most of the gammaENaC at the surface was smaller in molecular mass than the full-length subunit, consistent with cleavage of this subunit in the extracellular moiety close to the first transmembrane domains. Insensitivity of the channels to trypsin, measured in principal cells of the cortical collecting duct by whole-cell patch-clamp recording, corroborated this finding. ENaC subunits could be detected at the surface under all physiological conditions. However increasing the levels of aldosterone in the animals by feeding a low-Na diet or infusing them directly with hormone via osmotic minipumps for 1 wk before surface labeling increased the expression of the subunits at the surface by two- to fivefold. Salt repletion of Na-deprived animals for 5 h decreased surface expression. Changes in the surface density of ENaC subunits contribute significantly to the regulation of Na transport in renal cells by mineralocorticoid hormone, but do not fully account for increased channel activity.

Indexed as

AldosteroneAnimalsBiotinCell FractionationCell MembraneCell PolarityChromatography, AffinityEpithelial CellsEpithelial Sodium ChannelsFemaleGene ExpressionIon Channel GatingKidney Tubules, CollectingLysineMaleOocytesAldosteroneBiotinbiotinyl N-hydroxysuccinimide esterEpithelial Sodium ChannelsLysineProtein SubunitsSodiumSuccinimidesTrypsin

Identifiers

PMID18504317
PMCPMC2391254
OpenAlexW2138550890

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.