Evidence map›Paper›PMID 30345709›Full record

ArticleJournal of gastroenterology and hepatology2019

Unique patterns of glycosylation in immunoglobulin subclass G4-related disease and primary sclerosing cholangitis.

Emma L Culver, Fleur S van de Bovenkamp, Ninotska I L Derksen, Jana Koers, Tamsin Cargill, Eleanor Barnes, Louise A de Neef, Carolien A M Koeleman, Rob C Aalberse, Manfred Wuhrer and 1 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Journal of gastroenterology and hepatology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Omics in IgG4-related disease.Chinese medical journal · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Immunoglobulin G Glycosylation in Diseases.Experientia supplementum (2012) · 2021
    Article
  18. Article
  19. Article
  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

11 authors at 3 institutions in 2 countries.

Emma L CulverTranslational Gastroenterology Unit and Oxford NIHR Biomedical Research Centre, John Radcliffe Hospital, Oxford, UK.ORCID http://orcid.org/0000-0001-9644-8392
Fleur S van de BovenkampSanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
Ninotska I L DerksenSanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
Jana KoersSanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
Tamsin CargillTranslational Gastroenterology Unit and Oxford NIHR Biomedical Research Centre, John Radcliffe Hospital, Oxford, UK.
Eleanor BarnesTranslational Gastroenterology Unit and Oxford NIHR Biomedical Research Centre, John Radcliffe Hospital, Oxford, UK.
Louise A de NeefCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Carolien A M KoelemanCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Rob C AalberseSanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Theo RispensSanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
Sanquin · NLJohn Radcliffe Hospital · GBLeiden University Medical Center · NL

Funding

European Association for the Study of the Liver (EASL)Landsteiner Foundation for Blood Transfusion 1626Medical Research Council MR/K010239/1Medical Research Council UKNational Institute of Health Research (NIHR) Biomedical Research CentreNIHR Senior InvestigatorOxford NIHR Biomedical Research CentreOxfordshire Health Service Research Committee (OHSRC) 1253Wellcome TrustWellcome Trust 211042/Z/18/Z
6 · The paper itself

Abstract

BACKGROUND AND

aimImmunoglobulin subclass G4-related disease (IgG4-RD) is characterized by an abundance of IgG4 antibodies in the serum and tissue. Glycosylation status of antibodies can impact on immune effector functions and disease pathophysiology. We sought to establish glycosylation patterns in a prospective cohort of patients with IgG4-RD and the relationship with disease activity and response to treatment.

methodsWe assessed IgG Fc-tail and Fab-arm glycosylation status in patients with IgG4-RD (n = 22), disease controls with primary sclerosing cholangitis (PSC) (n = 22), and healthy controls (n = 22). Serum IgG and subclasses were quantified using ELISA. Fc and Fab glycosylation were analyzed by mass spectrometry and lectin affinity chromatography, respectively. Disease activity, organ damage, and response to treatment were assessed using the IgG4 Responder Index.

resultsImmunoglobulin G Fab sialylation was increased in IgG4-RD compared with PSC and healthy control (P = 0.01), with a preferential increase in IgG4-specific Fab sialylation, which was independent of IgG4 Fab-arm exchange. There was a reduction in IgG1-specific Fc bisection and hybrid structures in IgG4-RD (P < 0.01), which recovered upon steroid treatment and correlated with disease activity. Overall, IgG Fc galactosylation was reduced in both IgG4-RD and PSC (P < 0.01), with a preferential reduction in IgG1-specific sialylation and enhancement of IgG4-specific bisection in PSC. IgG4 fucosylation and IgG1/2/3 hybrid structures negatively correlated with complement C3 and C4 levels in IgG4-RD (P < 0.01), but not PSC.

conclusionWe report the first study showing unique antibody glycosylation status in a prospective cohort of IgG4-RD and PSC patients, which may determine modulation of the immune system and contribute to disease pathophysiology.

Indexed as

Protein Processing, Post-TranslationalAdrenal Cortex HormonesAdultAgedAged, 80 and overCase-Control StudiesCholangitis, SclerosingFemaleGlycosylationHumansImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulin G4-Related DiseaseMaleMiddle AgedAdrenal Cortex HormonesImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GcomplementglycosylationIgG4 antibodyIgG4-related diseaseprimary sclerosing cholangitis

Identifiers

PMID30345709
PMCPMC6899843
OpenAlexW2896688625

What OpenQuestion holds

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LicenceCC BY
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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.