Evidence map›Paper›PMID 23532520›Full record

ArticleInvestigative ophthalmology & visual science2013

Antiapoptotic properties of α-crystallin-derived peptide chaperones and characterization of their uptake transporters in human RPE cells.

Parameswaran G Sreekumar, Paresh Chothe, Krishna K Sharma, Rinku Baid, Uday Kompella, Christine Spee, Nandini Kannan, Christina Manh, Stephen J Ryan, Vadivel Ganapathy and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Investigative ophthalmology & visual science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

47 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  8. αB-crystallin mini-peptides support corneal healingInternational journal of ophthalmology · 2024
    Article
  9. Article
  10. Article
  11. Mini-Journal of ophthalmology · 2023
    Article
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  18. Involvement of a NaPharmaceutical research · 2020
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 1 country.

Parameswaran G SreekumarArnold and Mabel Beckman Macular Research Center, Doheny Eye Institute, Los Angeles, California, USA.
Paresh Chothe
Krishna K Sharma
Rinku Baid
Uday Kompella
Christine Spee
Nandini Kannan
Christina Manh
Stephen J Ryan
Vadivel Ganapathy
Ram Kannan
David R Hinton
University of Southern California · USAugusta University · USDoheny Eye Institute · USUniversity of Colorado Anschutz Medical Campus · USUniversity of Missouri · US

Funding

Southern California Clinical and Translational Science InstituteUL1TR000130 · NCATS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI BUCHANAN, THOMAS A · 2012 to 2015
$36.0M
VISION RESEARCHP30EY003040 · NEI · DOHENY EYE INSTITUTE · PI SUN, DEMING · 1985 to 2013
$7.0M
EXPERIMENTAL APPROACH TO MACULOPATHYR01EY001545 · NEI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HINTON, DAVID R. · 1985 to 2016
$6.0M
Retinal Iron Homeostasis in Health and DiseaseR01EY019672 · NEI · AUGUSTA UNIVERSITY · PI GANAPATHY, VADIVEL · 2010 to 2013
$1.4M
Development of Small Heat Shock Proteins as Therapeutic Agents in the EyeRC1EY020361 · NEI · UNIVERSITY OF COLORADO DENVER · PI PETRASH, JONATHAN MARK · 2009 to 2010
$992k
Crystallin-Derived Mini-Chaperones as Protein Aggregation InhibitorsR21EY021011 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 2010 to 2011
$409k
NCATS NIH HHS UL1 TR000130NCATS NIH HHS UL1TR000130NEI NIH HHS EY01545NEI NIH HHS EY019672NEI NIH HHS EY021011NEI NIH HHS EY03040NEI NIH HHS P30 EY003040NEI NIH HHS R01 EY001545NEI NIH HHS R01 EY019672NEI NIH HHS R21 EY021011NEI NIH HHS RC1 EY020361
6 · The paper itself

Abstract

purposeThe chaperone proteins, α-crystallins, also possess antiapoptotic properties. The purpose of the present study was to investigate whether 19 to 20-mer α-crystallin-derived mini-chaperone peptides (α-crystallin mini-chaperone) are antiapoptotic, and to identify their putative transporters in human fetal RPE (hfRPE) cells.

methodsCell death and caspase-3 activation induced by oxidative stress were quantified in early passage hfRPE cells in the presence of 19 to 20-mer αA- or αB-crystallin-derived or scrambled peptides. Cellular uptake of fluorescein-labeled, α-crystallin-derived mini-peptides and recombinant full-length αB-crystallin was determined in confluent hfRPE. The entry mechanism in hfRPE cells for α-crystallin mini-peptides was investigated. The protective role of polycaprolactone (PCL) nanoparticle encapsulated αB-crystallin mini-chaperone peptides from H2O2-induced cell death was studied.

resultsPrimary hfRPE cells exposed to oxidative stress and either αA- or αB-crystallin mini-chaperones remained viable and showed marked inhibition of both cell death and activation of caspase-3. Uptake of full-length αB-crystallin was minimal while a time-dependent uptake of αB-crystallin-derived peptide was observed. The mini-peptides entered the hfRPE cells via the sodium-coupled oligopeptide transporters 1 and 2 (SOPT1, SOPT2). PCL nanoparticles containing αB-crystallin mini-chaperone were also taken up and protected hfRPE from H2O2-induced cell death at significantly lower concentrations than free αB-crystallin mini-chaperone peptide.

conclusionsαA- and αB-crystallin mini-chaperones offer protection to hfRPE cells and inhibit caspase-3 activation. The oligopeptide transporters SOPT1 and SOPT2 mediate the uptake of these peptides in RPE cells. Nanodelivery of αB-crystallin-derived mini-chaperone peptide offers an alternative approach for protection of hfRPE cells from oxidant injury.

Indexed as

alpha-Crystallin A Chainalpha-Crystallin B ChainApoptosisApoptosis Regulatory ProteinsCaspase 3Cell LineDose-Response Relationship, DrugFluorescent Antibody Technique, IndirectHumansHydrogen PeroxideMembrane Transport ProteinsMolecular ChaperonesOxidantsOxidative StressPeptidesRecombinant Proteinsalpha-Crystallin A Chainalpha-Crystallin B ChainApoptosis Regulatory ProteinsCaspase 3Hydrogen PeroxideMembrane Transport ProteinsMolecular ChaperonesOxidantsPeptidesRecombinant Proteins

Identifiers

PMID23532520
PMCPMC3632268
OpenAlexW1967412587

What OpenQuestion holds

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Registered trials

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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.