Evidence map›Paper›PMID 21873671›Full record

ArticleInvestigative ophthalmology & visual science2011

Molecular chaperone function for myocilin.

Ann Marie Anderssohn, Kalani Cox, Kevin O'Malley, Scott Dees, Mojgan Hosseini, Lacey Boren, Anthony Wagner, John M Bradley, Mary J Kelley, Ted S Acott

Open access · bronzeAbstract read
In one paragraph

Article in Investigative ophthalmology & visual science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Clusterin, other extracellular chaperones, and eye disease.Progress in retinal and eye research · 2022
    Review
  5. Review
  6. Article
  7. Article
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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

10 authors at 2 institutions in 1 country.

Ann Marie AnderssohnCasey Eye Institute, Oregon Health & Science University, Portland, Oregon 97239, USA.
Kalani Cox
Kevin O'Malley
Scott Dees
Mojgan Hosseini
Lacey Boren
Anthony Wagner
John M Bradley
Mary J Kelley
Ted S Acott
University of Portland · USOregon Health & Science University · US

Funding

Proteomics CoreP30EY010572 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI TED S ACOTT · 1995 to 2026
$19.4M
BIOLOGY OF TRABECULAR RESPONSE TO LASER TRABECULOPLASTYR01EY008247 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI ACOTT, TED S · 1989 to 2017
$7.7M
VERTEBRATE EYE: STUDIES OF AQUEOUS OUTFLOWR01EY003279 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI ACOTT, TED S · 1985 to 2012
$5.5M
NEI NIH HHS EY003279NEI NIH HHS EY008247NEI NIH HHS EY010572NEI NIH HHS P30 EY010572NEI NIH HHS R01 EY003279NEI NIH HHS R01 EY008247
6 · The paper itself

Abstract

purposeMyocilin is thought to be a stress response protein, but its exact molecular functions have not been established. Studies were conducted to see whether myocilin can act as a general molecular chaperone.

methodsMyocilin was isolated and purified from porcine trabecular meshwork (TM) cell culture media. Its ability to protect citrate synthase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and the restriction endonuclease DrdI from thermal inactivation was evaluated. Light scattering was used to evaluate thermally induced aggregation of citrate synthase. Myocilin induction was assessed after exposure of TM cells to several types of stress treatments.

resultsLevels of extracellular myocilin expressed by TM cells were increased in response to mechanical stretch, heat shock, TNFα, or IL-1α. Myocilin protected citrate synthase activity against thermal inactivation for 5 minutes at 55°C in a concentration-dependent manner, with nearly full protection of 1.5 μM citrate synthase in the presence of 650 nM myocilin. Myocilin significantly reduced thermal aggregation of citrate synthase to levels 36% to 44% of control levels. Myocilin also protected GAPDH from thermal inactivation for 10 minutes at 45°C. Myocilin at 18 nM was more effective than 1 μM bovine serum albumin at protecting DrdI from thermal inactivation.

conclusionsMyocilin is induced in response to several cellular stresses and displays general molecular chaperone activity by protecting DrdI, citrate synthase, and GAPDH from thermal inactivation. Myocilin also suppresses the thermal aggregation of citrate synthase. One function of myocilin may be to serve as a molecular chaperone.

Indexed as

AnimalsBlotting, WesternCells, CulturedCitrate (si)-SynthaseCytoskeletal ProteinsDeoxyribonucleases, Type II Site-SpecificElectrophoresis, Polyacrylamide GelEnzyme InhibitorsEye ProteinsGlyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)GlycoproteinsHot TemperatureMolecular ChaperonesMyocilinStress, MechanicalStress, PhysiologicalCitrate (si)-SynthaseCytoskeletal ProteinsDeoxyribonucleases, Type II Site-Specificendodeoxyribonuclease DrdIEnzyme InhibitorsEye ProteinsGlyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)GlycoproteinsMolecular ChaperonesMyocilin

Identifiers

PMID21873671
PMCPMC3183979
OpenAlexW2017471761

What OpenQuestion holds

Textmetadata
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.