Evidence map›Paper›PMID 23049853›Full record

ArticlePloS one2012

Cytoplasmic and nuclear anti-apoptotic roles of αB-crystallin in retinal pigment epithelial cells.

Woo Jin Jeong, Jee Hyun Rho, Young Geol Yoon, Seung Hee Yoo, Na Young Jeong, Won Yeol Ryu, Hee Bae Ahn, Woo Chan Park, Sae Heun Rho, Hee Seong Yoon and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
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  5. Review
  6. Review
  7. Review
  8. Article
  9. Protein polymer nanoparticles engineered as chaperones protect against apoptosis in human retinal pigment epithelial cells.Journal of controlled release : official journal of the Controlled Release Society · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Alpha B-crystallin is a new prognostic marker for laryngeal squamous cell carcinoma.Journal of experimental & clinical cancer research : CR · 2012
    Article
  15. 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

12 authors at 3 institutions in 1 country.

Woo Jin JeongDepartment of Ophthalmology, Dong-A University College of Medicine, Seo-gu, Busan, Republic of Korea.
Jee Hyun Rho
Young Geol Yoon
Seung Hee Yoo
Na Young Jeong
Won Yeol Ryu
Hee Bae Ahn
Woo Chan Park
Sae Heun Rho
Hee Seong Yoon
Yung Hyun Choi
Young Hyun Yoo
Dong-A University · KRDong-Eui University · KRSungmo Eye Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to its well-characterized role in the lens, αB-crystallin performs other functions. Methylglyoxal (MGO) can alter the function of the basement membrane of retinal pigment epithelial (RPE) cells. Thus, if MGO is not efficiently detoxified, it can induce adverse reactions in RPE cells. In this study, we examined the mechanisms underlying the anti-apoptotic activity of αB-crystallin in the human retinal pigment epithelial cell line ARPE-19 following MGO treatment using various assays, including nuclear staining, flow cytometry, DNA electrophoresis, pulse field gel electrophoresis, western blot analysis, confocal microscopy and co-immunoprecipitation assays. To directly assess the role of phosphorylation of αB-crystallin, we used site-directed mutagenesis to convert relevant serine residues to alanine residues. Using these techniques, we demonstrated that MGO induces apoptosis in ARPE-19 cells. Silencing αB-crystallin sensitized ARPE-19 cells to MGO-induced apoptosis, indicating that αB-crystallin protects ARPE-19 cells from MGO-induced apoptosis. Furthermore, we found that αB-crystallin interacts with the caspase subtypes, caspase-2L, -2S, -3, -4, -7, -8, -9 and -12 in untreated control ARPE-19 cells and that MGO treatment caused the dissociation of these caspase subtypes from αB-crystallin; transfection of S19A, S45A or S59A mutants caused the depletion of αB-crystallin from the nuclei of untreated control RPE cells leading to the release of caspase subtypes. Additionally, transfection of these mutants enhanced MGO-induced apoptosis in ARPE-19 cells, indicating that phosphorylation of nuclear αB-crystallin on serine residues 19, 45 and 59 plays a pivotal role in preventing apoptosis in ARPE-19 cells. Taken together, these results suggest that αB-crystallin prevents caspase activation by physically interacting with caspase subtypes in the cytoplasm and nucleus, thereby protecting RPE cells from MGO-induced apoptosis.

Indexed as

Apoptosisalpha-Crystallin B ChainCaspasesCell LineCell NucleusCells, CulturedCell SurvivalCytoplasmDNAFlow CytometryHumansMicroscopy, ConfocalMicroscopy, FluorescenceMutagenesis, Site-DirectedPloidiesPyruvaldehydealpha-Crystallin B ChainCaspasesDNAPyruvaldehydeRNA, Small InterferingSerine

Identifiers

PMID23049853
PMCPMC3458930
OpenAlexW2062014153

What OpenQuestion holds

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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.