Evidence map›Paper›PMID 26987815›Full record

ArticleThe Biochemical journal2016

αB-crystallin is essential for the TGF-β2-mediated epithelial to mesenchymal transition of lens epithelial cells.

Rooban B Nahomi, Mina B Pantcheva, Ram H Nagaraj

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 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
3.0field-weighted citation impact, top 10% 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, 26 citations in OpenAlex.

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  8. EMT signaling: potential contribution of CRISPR/Cas gene editing.Cellular and molecular life sciences : CMLS · 2020
    Review
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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

3 authors at 2 institutions in 1 country.

Rooban B NahomiDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, School of Medicine, Cleveland, OH 44106, U.S.A. Department of Ophthalmology, University of Colorado, School of Medicine, Aurora, CO 80045, U.S.A.
Mina B PantchevaDepartment of Ophthalmology, University of Colorado, School of Medicine, Aurora, CO 80045, U.S.A.
Ram H NagarajDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, School of Medicine, Cleveland, OH 44106, U.S.A. Department of Ophthalmology, University of Colorado, School of Medicine, Aurora, CO 80045, U.S.A. ram.nagaraj@ucdenver.edu.
Case Western Reserve University · USUniversity of Colorado Denver · US

Funding

TISSUE CULTURE AND HYBRIDOMA MODULEP30EY011373 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Irina A Pikuleva · 1997 to 2026
$17.7M
Molecular Mechanisms of Protein Crosslinking in the LensR01EY023286 · NEI · UNIVERSITY OF COLORADO DENVER · PI NAGARAJ, RAM H · 2013 to 2022
$2.9M
LENS CAPSULE AND SECONDARY CATARACTR01EY022061 · NEI · UNIVERSITY OF COLORADO DENVER · PI NAGARAJ, RAM H · 2013 to 2017
$1.9M
NEI NIH HHS P30 EY011373NEI NIH HHS R01 EY022061NEI NIH HHS R01 EY023286
6 · The paper itself

Abstract

Transforming growth factor (TGF)-β2-mediated pathways play a major role in the epithelial to mesenchymal transition (EMT) of lens epithelial cells (LECs) during secondary cataract formation, which is also known as posterior capsule opacification (PCO). Although αB-crystallin is a major protein in LEC, its role in the EMT remains unknown. In a human LEC line (FHL124), TGF-β2 treatment resulted in changes in the EMT-associated proteins at the mRNA and protein levels. This was associated with nuclear localization of αB-crystallin, phosphorylated Smad2 (pSmad2) (S245/250/255), pSmad3 (S423/425), Smad4 and Snail and the binding of αB-crystallin to these transcription factors, all of which were reduced by the down-regulation of αB-crystallin. Expression of the functionally defective R120G mutant of αB-crystallin reduced TGF-β2-induced EMT in LECs of αB-crystallin knockout (KO) mice. Treatment of bovine lens epithelial explants and mouse LEC with TGF-β2 resulted in changes in the EMT-associated proteins at the mRNA and protein levels. This was accompanied by increase in phosphorylation of p44/42 mitogen-activated protein kinases (MAPK) (T202/Y204), p38 MAPK (T180/Y182), protein kinase B (Akt) (S473) and Smad2 when compared with untreated cells. These changes were significantly reduced in αB-crystallin depleted or knocked out LEC. The removal of the fibre cell mass from the lens of wild-type (WT) mice resulted in the up-regulation of EMT-associated genes in the capsule-adherent epithelial cells, which was reduced in the αB-crystallin KO mice. Together, our data show that αB-crystallin plays a central role in the TGF-β2-induced EMT of LEC. αB-Crystallin could be targeted to prevent PCO and pathological fibrosis in other tissues.

Indexed as

AnimalsCattleCell LineCrystallinsEpithelial CellsEpithelial-Mesenchymal TransitionHeLa CellsHumansLens, CrystallineMiceMice, KnockoutSignal TransductionSmad2 ProteinSmad3 ProteinSmad4 ProteinSnail Family Transcription FactorsCrystallinsSmad2 ProteinSmad3 ProteinSmad4 ProteinSnail Family Transcription FactorsTransforming Growth Factor beta2epithelial to mesenchymal transitionlens epithelial cellsTGF-β2αB-crystallin

Identifiers

PMID26987815
PMCPMC4928857
OpenAlexW2302190017

What OpenQuestion holds

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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.