Evidence map›Paper›PMID 24458570›Full record

ArticleProteomics. Clinical applications2014

Aberrant glycosylation in the human trabecular meshwork.

Adam E Sienkiewicz, Brandon N Rosenberg, Genea Edwards, Teresia A Carreon, Sanjoy K Bhattacharya

Abstract read
In one paragraph

Article in Proteomics. Clinical applications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  9. Review
  10. Review
  11. Proteomics and the eye.Proteomics. Clinical applications · 2014
    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

5 authors at 2 institutions in 1 country.

Adam E SienkiewiczBascom Palmer Eye Institute, University of Miami, Miami, FL, USA.
Brandon N Rosenberg
Genea Edwards
Teresia A Carreon
Sanjoy K Bhattacharya
Miami Transplant Institute · USUniversity of Miami · US

Funding

Shared Equipment ModuleP30EY014801 · NEI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI Victor L Perez · 2004 to 2026
$12.2M
TRABECULAR MESHWORK PROTEINS IN GLAUCOMAR01EY016112 · NEI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BHATTACHARYA, SANJOY K · 2006 to 2016
$3.7M
University of Miami Computational Ocular Genomics Training ProgramT32EY023194 · NEI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SCOTT, WILLIAM K · 2013 to 2017
$661k
Proteomic Analyses of Human Trabecular MeshworkR03EY015266 · NEI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BHATTACHARYA, SANJOY K · 2005 to 2007
$451k
NEI NIH HHS EY016112NEI NIH HHS EY016112S1NEI NIH HHS P30 EY014801NEI NIH HHS P30-EY14801NEI NIH HHS R01 EY016112NEI NIH HHS R03 EY015266NEI NIH HHS T32 EY023194NEI NIH HHS T32EY023194-01
6 · The paper itself

Abstract

purposeTo determine the difference in protein glycosylation and glycosylation enzyme levels between glaucomatous and control trabecular meshwork (TM). EXPERIMENTAL

designGlaucomatous and normal donor (n = 12 each) TM tissues, lectin fluorescence, fluorophore-assisted carbohydrate analyses, and quantitative MS were used to determine the glycosylation levels. Primary TM cells and glycosylation inhibitors were used to determine their effect on cell shape and motility.

resultsIn contrast to elevated levels of glycoproteins determined by lectin fluorescence, simultaneous hyper- and hypo-glycosylation in glaucomatous TM was revealed by fluorophore-assisted carbohydrate analyses. Analyses of enzymes showed elevation of beta-glycosidase 1 and decrease in galactosyltransferase family 6 domain containing protein 1 in the glaucomatous TM. Quantitative MS identified select protein level changes between glaucomatous and normal TM. Primary TM cells were treated with inhibitors to elicit hypo-glycosylation, which affected cell shape, motility, and fluorescent tracer transport across a layer of TM cells. CONCLUSIONS AND CLINICAL RELEVANCE: Global protein glycosylation is aberrant in glaucomatous TM compared to controls. The results presented here suggest that the alteration in global TM protein glycosylation encompassing cellular and extracellular matrix proteins contributes to glaucoma pathology likely mediated through changes in properties of TM cells.

Indexed as

EnzymesExtracellular Matrix ProteinsGene Expression Regulation, EnzymologicGlaucomaGlycosylationHumansTrabecular MeshworkEnzymesExtracellular Matrix ProteinsCarbohydrate electrophoresisGlaucomaGlycosylationTrabecular meshwork

Identifiers

PMID24458570
PMCPMC4015974
OpenAlexW2161524746

What OpenQuestion holds

Textmetadata
LicenceTDM
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.