Evidence map›Paper›PMID 21792912›Full record

ArticleJournal of cellular physiology2011

The effect of endothelin-1 on Src-family tyrosine kinases and Na,K-ATPase activity in porcine lens epithelium.

A Mandal, M Shahidullah, C Beimgraben, N A Delamere

Abstract readComparative Study
In one paragraph

Article in Journal of cellular physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
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  4. Regulation of Neuronal NaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
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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 1 institution in 1 country.

A MandalDepartment of Physiology, University of Arizona, Tucson, Arizona 85724, USA.
M Shahidullah
C Beimgraben
N A Delamere
University of Arizona · US

Funding

TRPV4 as a remote controller of lens functionR01EY009532 · NEI · UNIVERSITY OF LOUISVILLE · PI DELAMERE, NICHOLAS A · 1993 to 2024
$8.0M
NEI NIH HHS EY009532NEI NIH HHS R01 EY009532
6 · The paper itself

Abstract

Previous studies show Src family kinase (SFK) activation is involved in a response that stimulates Na,K-ATPase. Here, we tested whether SFK activation is involved in the Na,K-ATPase response to endothelin-1 (ET-1). Intact porcine lenses were exposed to 100 nM ET-1 for 5-30 min. Then, the epithelium was removed and used for Na,K-ATPase activity measurement and Western blot analysis of SFK activation. Na,K-ATPase activity was reduced by ∼30% in lenses exposed to ET-1 for 15 min. The response was abolished by the SFK inhibitor PP2 or the ET receptor antagonist, PD145065. Activation of a ∼61 kDa SFK was evident from an increase in Y416 phosphorylation, which reached a maximum at 15 min ET-1 treatment, and a decrease in Y527 phosphorylation. PP2 prevented SFK activation. Since Fyn, Src, Hck, and Yes may contribute to the observed 61 kDa band, these SFKs were isolated by immunoprecipitation and analyzed. Based on Y416 phosphorylation, ET-1 appeared to activate Fyn, while Src and Hck were inhibited and Yes was unaltered. ET-1 requires SFK activation to cause Na,K-ATPase inhibition. ET-1 elicits a different pattern of SFK activation from that reported earlier for purinergic agonists that stimulate Na,K-ATPase activity and activate Src. In the ET-1 response Src is inhibited and Fyn is activated. The findings suggest SFK phosphorylation is involved in a regulatory mechanism for Na,K-ATPase. Knowing this may help us understand drug actions on Na,K-ATPase. Faulty regulation of Na,K-ATPase in the lens could contribute to cataract formation since an abnormal sodium content is associated with lens opacification.

Indexed as

Adenosine TriphosphateAnimalsEndothelin-1Endothelin Receptor AntagonistsEnzyme ActivationEpitheliumLens, CrystallineOligopeptidesOrgan Culture TechniquesProto-Oncogene Proteins c-fynSignal TransductionSodium-Potassium-Exchanging ATPasesrc-Family KinasesSus scrofaUridine TriphosphateAdenosine TriphosphateEndothelin-1Endothelin Receptor AntagonistsOligopeptidesPD 145065Proto-Oncogene Proteins c-fynSodium-Potassium-Exchanging ATPasesrc-Family KinasesUridine Triphosphate

Identifiers

PMID21792912
PMCPMC5985970
OpenAlexW2092633731

What OpenQuestion holds

Textmetadata
LicenceTDM
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.