Evidence map›Paper›PMID 26314228›Full record

ArticleArthritis & rheumatology (Hoboken, N.J.)2016

Cysteine-Mediated Redox Regulation of Cell Signaling in Chondrocytes Stimulated With Fibronectin Fragments.

Scott T Wood, David L Long, Julie A Reisz, Raghunatha R Yammani, Elizabeth A Burke, Chananat Klomsiri, Leslie B Poole, Cristina M Furdui, Richard F Loeser

Open access · greenAbstract readHistorical Article
In one paragraph

Article in Arthritis & rheumatology (Hoboken, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  3. Role and mechanism of Integrin α5β1 in bone formation and disease.Frontiers in cell and developmental biology · 2025
    Review
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  7. Article
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  13. Antioxidants (Basel, Switzerland) · 2021
    Article
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  15. Article
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  20. Review
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

9 authors at 2 institutions in 1 country.

Scott T WoodUniversity of North Carolina School of Medicine, Chapel Hill.
David L LongWake Forest University School of Medicine, Winston-Salem, North Carolina.
Julie A ReiszWake Forest University School of Medicine, Winston-Salem, North Carolina.
Raghunatha R YammaniWake Forest University School of Medicine, Winston-Salem, North Carolina.
Elizabeth A BurkeWake Forest University School of Medicine, Winston-Salem, North Carolina.
Chananat KlomsiriWake Forest University School of Medicine, Winston-Salem, North Carolina.
Leslie B PooleWake Forest University School of Medicine, Winston-Salem, North Carolina.
Cristina M FurduiWake Forest University School of Medicine, Winston-Salem, North Carolina.
Richard F LoeserUniversity of North Carolina School of Medicine, Chapel Hill.
Wake Forest University · USUniversity of North Carolina at Chapel Hill · US

Funding

Oxidative Stress and the Development of OsteoarthritisR01AG044034 · NIA · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI RICHARD F LOESER · 2012 to 2026
$5.7M
Integrin Function in CartilageR37AR049003 · NIAMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI LOESER, RICHARD F · 2012 to 2021
$4.1M
Integrin Function in CartilageR01AR049003 · NIAMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI LOESER, RICHARD F · 2002 to 2011
$2.8M
New Reagents for Tracking Protein Oxidation in Cells by MS and Imaging MethodsR33CA177461 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI FURDUI, CRISTINA MARIA, POOLE, LESLIE B · 2013 to 2015
$1.0M
NCI NIH HHS CA-177461NCI NIH HHS R33 CA177461NIAMS NIH HHS AR-049003NIAMS NIH HHS R01 AR049003NIAMS NIH HHS R37 AR049003NIA NIH HHS AG-044034NIA NIH HHS R01 AG044034
6 · The paper itself

Abstract

objectiveOxidative posttranslational modifications of intracellular proteins can potentially regulate signaling pathways relevant to cartilage destruction in arthritis. In this study, oxidation of cysteine residues to form sulfenic acid (S-sulfenylation) was examined in osteoarthritic (OA) chondrocytes and investigated in normal chondrocytes as a mechanism by which fragments of fibronectin (FN-f) stimulate chondrocyte catabolic signaling.

methodsChondrocytes isolated from OA and normal human articular cartilage were analyzed using analogs of dimedone that specifically and irreversibly react with protein S-sulfenylated cysteines. Global S-sulfenylation was measured in cell lysates with and without FN-f stimulation by immunoblotting and in fixed cells by confocal microscopy. S-sulfenylation in specific proteins was identified by mass spectroscopy and confirmed by immunoblotting. Src activity was measured in live cells using a fluorescence resonance energy transfer biosensor.

resultsProteins in chondrocytes isolated from OA cartilage were found to have elevated basal levels of S-sulfenylation relative to those of chondrocytes from normal cartilage. Treatment of normal chondrocytes with FN-f induced increased levels of S-sulfenylation in multiple proteins, including the tyrosine kinase Src. FN-f treatment also increased the levels of Src activity. Pretreatment with dimedone to alter S-sulfenylation function or with Src kinase inhibitors inhibited FN-f-induced production of matrix metalloproteinase 13.

conclusionThese results demonstrate for the first time the presence of oxidative posttranslational modification of proteins in human articular chondrocytes by S-sulfenylation. Due to the ability to regulate the activity of a number of cell signaling pathways, including catabolic mediators induced by fibronectin fragments, S-sulfenylation may contribute to cartilage destruction in OA and warrants further investigation.

Indexed as

Oxidation-ReductionAdultAgedAged, 80 and overCartilage, ArticularCase-Control StudiesChondrocytesCyclohexanonesCysteineFemaleFibronectinsHistory, AncientHumansImmunoblottingMass SpectrometryMatrix Metalloproteinase 13CyclohexanonesCysteinedimedoneFibronectinsMatrix Metalloproteinase 13MMP13 protein, humanPeptide Fragmentssrc-Family KinasesSulfenic Acids

Identifiers

PMID26314228
PMCPMC4849859
OpenAlexW1843436898

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.