Evidence map›Paper›PMID 29800803›Full record

ArticleDifferentiation; research in biological diversity

Epha2 and Efna5 participate in lens cell pattern-formation.

Yuefang Zhou, Alan Shiels

Open access · hybridAbstract read
In one paragraph

Article in Differentiation; research in biological diversity. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

28 citing papers in PubMed, 32 citations in OpenAlex.

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  13. Charged multivesicular body protein 4b forms complexes with gap junction proteins during lens fiber cell differentiation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
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  20. An Atlas of Heparan Sulfate Proteoglycans in the Postnatal Rat Lens.Investigative ophthalmology & visual science · 2021
    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

2 authors at 1 institution in 1 country.

Yuefang ZhouDepartment of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, MO, USA.
Alan ShielsDepartment of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, MO, USA. Electronic address: shiels@vision.wustl.edu.
Washington University in St. Louis · US

Funding

WASHINGTON UNIVERSITY CENTER VISION RESEARCHP30EY002687 · NEI · WASHINGTON UNIVERSITY · PI Steven Bassnett · 1985 to 2026
$18.4M
EPH-RECEPTOR SIGNALING IN LENS DEVELOPMENT AND AGINGR01EY023549 · NEI · WASHINGTON UNIVERSITY · PI SHIELS, ALAN · 2013 to 2017
$1.7M
NEI NIH HHS P30 EY002687NEI NIH HHS R01 EY023549
6 · The paper itself

Abstract

Ephrin type-A receptor 2 (EPHA2) and one of its ligands, ephrin-A5 (EFNA5), have been associated with loss of eye lens transparency, or cataract, - an important cause of visual impairment. Here we show that mice functionally lacking EPHA2 (Epha2-null), EFNA5 (Efna5-null), or both receptor and ligand (Epha2/Efna5-null) consistently develop mostly transparent lenses with an internal refractive disturbance and a grossly disturbed cellular architecture. In situ hybridization localized Epha2 and Efna5 transcripts to lens epithelial cells and nascent fiber cells at the lens equator. In vivo labeling of Epha2-null lenses with a thymidine analog detected a significant decrease in lens epithelial cell proliferation within the germinative zone resulting in impaired early lens growth. Ex vivo imaging of Epha2-null, Efna5-null, and Epha2/Efna5-null lenses labelled in vivo with a membrane-targeted red fluorescent protein revealed misalignment of elongating fiber cells at the lens equator and loss of Y-suture pattern formation near the anterior and posterior poles of the lens. Immuno-fluorescent labeling of lens major intrinsic protein or aquaporin-0 (MIP/AQP0) showed that the precise, radial column patterning of hexagonal fiber cells throughout the cortex region was disrupted in Epha2-null, Efna5-null and Epha2/Efna5-null lenses. Collectively, these data suggest that Epha2 and Efna5 participate in the complex, global patterning of lens fiber cells that is necessary for maximal optical quality.

Indexed as

AnimalsCataractEphrin-A5Epithelial CellsLens, CrystallineMice, KnockoutMorphogenesisReceptor, EphA2Ephrin-A5Receptor, EphA2CataractEphrin ligandEphrin receptorLensY-suture formation

Identifiers

PMID29800803
PMCPMC6287607
OpenAlexW2803786595

What Socratic 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 Socratic graph.