Evidence map›Paper›PMID 26990173›Full record

ArticleRedox biology2016

PARP-1 inhibition influences the oxidative stress response of the human lens.

Andrew J O Smith, Simon S R Ball, Richard P Bowater, I Michael Wormstone

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Global challenges for lens and cataract research.Frontiers in ophthalmology · 2026
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  11. Oral Administration of Gintonin Protects the Brains of Mice against AOxidative medicine and cellular longevity · 2021
    Article
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  15. The role of poly(ADP-ribose) polymerases in manganese exposed Caenorhabditis elegans.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2020
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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 2 institutions in 1 country.

Andrew J O SmithSchool of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
Simon S R BallSchool of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
Richard P BowaterSchool of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. Electronic address: r.bowater@uea.ac.uk.
I Michael WormstoneSchool of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. Electronic address: i.m.wormstone@uea.ac.uk.
Norwich Research Park · GBUniversity of East Anglia · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase-1 (PARP-1) is best characterised for its involvement in DNA repair. PARP-1 activity is also linked to cell fate, confounding its roles in maintaining genome integrity. The current study assessed the functional roles of PARP-1 within human lens cells in response to oxidative stress. The human lens epithelial cell line FHL124 and whole human lens cultures were used as experimental systems. Hydrogen peroxide (H2O2) was employed to induce oxidative stress and cell death was assessed by LDH release. The functional influence of PARP-1 was assessed using targeted siRNA and chemical inhibition (by AG14361). Immunocytochemistry and western blotting were used to assess PARP-1 expression and the alkaline comet assay determined the levels of DNA strand breaks. PARP-1 was generally observed in the cell nucleus in both the FHL124 cell line and whole human lenses. PARP-1 inhibition rendered FHL124 cells more susceptible to H2O2-induced DNA strand breaks. Interestingly, reduction of PARP-1 activity significantly inhibited H2O2-induced cell death relative to control cells. Inhibition of PARP-1 in whole human lenses resulted in a reduced level of lens opacity and cell death following exposure to H2O2 relative to matched pair controls. Thus, we show that PARP-1 could play a role in the fate of human lens cells, and these first observations in human lenses suggest that it could impact on lens opacity. Further studies are required to elucidate the regulatory processes that give rise to these effects.

Indexed as

AzulenesBenzodiazepinesCataractCell LineCell NucleusDNA DamageDNA RepairEpithelial CellsHumansHydrogen PeroxideLens, CrystallineOxidation-ReductionOxidative StressPoly (ADP-Ribose) Polymerase-1RNA, Small Interfering1-(4-dimethylaminomethylphenyl)-8,9-dihydro-7H-2,7,9a-benzo(cd)azulen-6-oneAzulenesBenzodiazepinesHydrogen PeroxidePARP1 protein, humanPoly (ADP-Ribose) Polymerase-1RNA, Small InterferingCataractCell survivalDNA damageHumanLensPoly (ADP-ribose) polymerase-1

Identifiers

PMID26990173
PMCPMC4799059
OpenAlexW2295817239

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.