Evidence map›Paper›PMID 27304846›Full record

ArticleInvestigative ophthalmology & visual science2016

The Phosphoinosotide 3-Kinase Catalytic Subunit p110α is Required for Normal Lens Growth.

Caterina Sellitto, Leping Li, Ehsan Vaghefi, Paul J Donaldson, Richard Z Lin, Thomas W White

Open access · goldAbstract read
In one paragraph

Article in Investigative ophthalmology & visual science, 2016. 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
0.9field-weighted citation impact, top 24% 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, 18 citations in OpenAlex.

  1. Review
  2. FoxO1 promotes high glucose-induced inflammation and cataract formation via JAK1/STAT1.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2025
    Article
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  16. Article
  17. The lens growth process.Progress in retinal and eye research · 2017
    Review
  18. A full lifespan model of vertebrate lens growth.Royal Society open science · 2017
    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

6 authors at 2 institutions in 2 countries.

Caterina SellittoDepartment of Physiology and Biophysics Stony Brook University, Stony Brook, New York, United States.
Leping LiDepartment of Physiology and Biophysics Stony Brook University, Stony Brook, New York, United States.
Ehsan VaghefiSchool of Optometry and Vision Science, School of Medical Sciences, University of Auckland, Auckland, New Zealand.
Paul J DonaldsonDepartment of Physiology, School of Medical Sciences, University of Auckland, Auckland, New Zealand.
Richard Z LinDepartment of Physiology and Biophysics Stony Brook University, Stony Brook, New York, United States 4Medical Service, Department of Veterans Affairs Medical Center, Northport, New York, United States.
Thomas W WhiteDepartment of Physiology and Biophysics Stony Brook University, Stony Brook, New York, United States.
Stony Brook University · USUniversity of Auckland · NZ

Funding

Lens Intercellular Communication Connexins and CataractsR01EY013163 · NEI · STATE UNIVERSITY NEW YORK STONY BROOK · PI WHITE, THOMAS W · 2000 to 2019
$6.2M
NEI NIH HHS R01 EY013163
6 · The paper itself

Abstract

purposeSignal transduction pathways influence lens growth, but little is known about the role(s) of the class 1A phosphoinositide 3-kinases (PI3Ks). To further investigate how signaling regulates lens growth, we generated and characterized mice in which the p110α and p110β catalytic subunits of PI3K were conditionally deleted in the mouse lens.

methodsFloxed alleles of the catalytic subunits of PI3K were conditionally deleted in the lens by using MLR10-cre transgenic mice. Lenses of age-matched animals were dissected and photographed. Postnatal lenses were fixed, paraffin embedded, sectioned, and stained with hematoxylin-eosin. Cell proliferation was quantified by labeling S-phase cells in intact lenses with 5-ethynyl-2'-deoxyuridine. Protein kinase B (AKT) activation was examined by Western blotting.

resultsLens-specific deletion of p110α resulted in a significant reduction of eye and lens size, without compromising lens clarity. Conditional knockout of p110β had no effect on lens size or clarity, and deletion of both the p110α and p110β subunits resulted in a phenotype that resembled the p110α single-knockout phenotype. Levels of activated AKT were decreased more in p110α- than in p110β-deficient lenses. A significant reduction in proliferating cells in the germinative zone was observed on postnatal day 0 in p110α knockout mice, which was temporally correlated with decreased lens volume.

conclusionsThese data suggest that the class 1A PI3K signaling pathway plays an important role in the regulation of lens size by influencing the extent and spatial location of cell proliferation in the perinatal period.

Indexed as

AnimalsBlotting, WesternCatalytic DomainCell ProliferationClass I Phosphatidylinositol 3-KinasesLens, CrystallineMiceMice, KnockoutModels, AnimalPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktSignal TransductionClass I Phosphatidylinositol 3-Kinasesp110delta protein, ratPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-akt

Identifiers

PMID27304846
PMCPMC4928694
OpenAlexW2430905729

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.