Evidence map›Paper›PMID 17522142›Full record

ArticleAmerican journal of physiology. Cell physiology2007

Purinergic agonists stimulate lens Na-K-ATPase-mediated transport via a Src tyrosine kinase-dependent pathway.

Shigeo Tamiya, Mansim C Okafor, Nicholas A Delamere

Abstract read
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In one paragraph

Article in American journal of physiology. Cell physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. GNature communications · 2022
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  8. The Significance of TRPV4 Channels and Hemichannels in the Lens and Ciliary Epithelium.Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics · 2016
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Shigeo TamiyaDept of Physiology, University of Arizona Health Sciences Center, Tucson, AZ 85724-5051, USA.
Mansim C Okafor
Nicholas A Delamere
University of Louisville Hospital · 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 EY09532
6 · The paper itself

Abstract

The Na-K-ATPase is vital for maintenance of lens transparency. Past studies using intact lens suggested the involvement of tyrosine kinases in short-term regulation of Na-K-ATPase. Furthermore, in vitro phosphorylation of a lens epithelial membrane preparation by Src family kinases (SFKs), a family of nonreceptor tyrosine kinases, resulted in modification of Na-K-ATPase activity. Here, the effect of purinergic agonists, ATP and UTP, on Na-K-ATPase function and SFK activation was examined in the rabbit lens. Na-K-ATPase function was examined using two different approaches, measurement of ouabain-sensitive potassium ((86)Rb) uptake by the intact lens, and Na-K-ATPase activity in lens epithelial homogenates. ATP and UTP caused a significant increase in ouabain-sensitive potassium ((86)Rb) uptake. Na-K-ATPase activity was increased in the epithelium of lenses pretreated with ATP. Lenses treated with ATP or UTP displayed activation of SFKs as evidenced by increased Western blot band density of active SFK (phosphorylated at the active loop Y416) and decreased band density of inactive SFKs (phosphorylated at the COOH terminal). A single PY416-Src immunoreactive band at approximately 60 kDa was observed, suggesting not all Src family members are activated. Immunoprecipitation studies showed that band density of active Src, and to a lesser extent active Fyn, was significantly increased, while active Yes did not change. Preincubation of the lenses with SFK inhibitor PP2 abolished the ATP-induced increase in ouabain-sensitive potassium ((86)Rb) uptake. The results suggest selective activation of Src and/or Fyn is part of a signaling mechanism initiated by purinergic agonists that increases Na-K-ATPase-mediated transport in the organ-cultured lens.

Indexed as

Signal TransductionAdenosine TriphosphateAnimalsEnzyme ActivationEnzyme InhibitorsLens, CrystallineOrgan Culture TechniquesOuabainPhosphorylationPotassiumProto-Oncogene Proteins c-fynProto-Oncogene Proteins c-yesPurinergic P2 Receptor AgonistsPyrimidinesRabbitsReceptors, Purinergic P2Adenosine TriphosphateAG 1879Enzyme InhibitorsOuabainPotassiumProto-Oncogene Proteins c-fynProto-Oncogene Proteins c-yesPurinergic P2 Receptor AgonistsPyrimidinesReceptors, Purinergic P2Rubidium RadioisotopesSodium-Potassium-Exchanging ATPasesrc-Family KinasesUridine Triphosphate

Identifiers

PMID17522142
OpenAlexW2127706439

What OpenQuestion holds

Textmetadata
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.