Evidence map›Paper›PMID 31907043›Full record

ArticleJournal of translational medicine2020

Glycosylation deficiency of lipopolysaccharide-binding protein and corticosteroid-binding globulin associated with activity and response to treatment for rheumatoid arthritis.

Federica Ciregia, Dominique Baiwir, Gaël Cobraiville, Thibaut Dewael, Gabriel Mazzucchelli, Valérie Badot, Silvana Di Romana, Paschalis Sidiras, Tatiana Sokolova, Patrick Durez and 2 more

Open access · goldAbstract read
In one paragraph

Article in Journal of translational medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
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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

12 authors at 5 institutions in 1 country.

Federica CiregiaLaboratory of Rheumatology, GIGA-I3, University of Liège, CHU de Liège, 4000, Liège, Belgium. federica.ciregia@uliege.be.ORCID 0000-0002-5851-9249
Dominique BaiwirGIGA Proteomic Facility, University of Liège, 4000, Liège, Belgium.
Gaël CobraivilleLaboratory of Rheumatology, GIGA-I3, University of Liège, CHU de Liège, 4000, Liège, Belgium.
Thibaut DewaelLaboratory of Rheumatology, GIGA-I3, University of Liège, CHU de Liège, 4000, Liège, Belgium.
Gabriel MazzucchelliMass Spectrometry Laboratory, System Biology and Chemical Biology, GIGA-Research, University of Liège, 4000, Liège, Belgium.
Valérie BadotDepartment of Rheumatology, CHU Brugmann, 1200, Brussels, Belgium.
Silvana Di RomanaDepartment of Rheumatology, CHU Saint-Pierre, 1200, Brussels, Belgium.
Paschalis SidirasDepartment of Rheumatology, Hôpital Erasme, Université Libre de Bruxelles, 1200, Brussels, Belgium.
Tatiana SokolovaDepartment of Rheumatology, Cliniques Universitaires Saint-Luc, Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain, 1200, Brussels, Belgium.
Patrick DurezDepartment of Rheumatology, Cliniques Universitaires Saint-Luc, Institut de Recherche Expérimentale et Clinique (IREC), Université Catholique de Louvain, 1200, Brussels, Belgium.
Michel G MalaiseLaboratory of Rheumatology, GIGA-I3, University of Liège, CHU de Liège, 4000, Liège, Belgium.
Dominique de SenyLaboratory of Rheumatology, GIGA-I3, University of Liège, CHU de Liège, 4000, Liège, Belgium.
University of Liège · BECliniques Universitaires Saint-Luc · BECentre Hospitalier Universitaire Brugmann · BECentre Hospitalier Universitaire de Saint-Pierre · BEUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSerum protein glycosylation is an area of investigation in inflammatory arthritic disorders such as rheumatoid arthritis (RA). Indeed, some studies highlighted abnormalities of protein glycosylation in RA. Considering the numerous types of enzymes, monosaccharides and glycosidic linkages, glycosylation is one of the most complex post translational modifications. By this work, we started with a preliminary screening of glycoproteins in serum from RA patients and controls.

methodsIn order to isolate glycoproteins from serum, lectin wheat germ agglutinin was used and quantitative differences between patients and controls were investigated by LC-MS/MS. Consequently, we focused our attention on two glycoproteins found in this explorative phase: corticosteroid-binding globulin (CBG) and lipopolysaccharide-binding protein (LBP). The subsequent validation with immunoassays was widened to a larger number of early RA (ERA) patients (n = 90) and well-matched healthy controls (n = 90).

resultsWe observed a significant reduction of CBG and LBP glycosylation in ERA patients compared with healthy controls. Further, after 12 months of treatment, glycosylated CBG and LBP levels increased both to values comparable to those of controls. In addition, these changes were correlated with clinical parameters.

conclusionsThis study enables to observe that glycosylation changes of CBG and LBP are related to RA disease activity and its response to treatment.

Indexed as

Arthritis, RheumatoidTranscortinAcute-Phase ProteinsCarrier ProteinsChromatography, LiquidGlycosylationHumansLipopolysaccharide-Binding ProteinMembrane GlycoproteinsTandem Mass SpectrometryAcute-Phase ProteinsCarrier ProteinsLipopolysaccharide-Binding ProteinMembrane GlycoproteinsTranscortinBiomarkersCBGGlycosylationLBPPost translational modificationsRheumatoid arthritis

Identifiers

PMID31907043
PMCPMC6945416
OpenAlexW3007236383

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.