Evidence map›Paper›PMID 21372248›Full record

ArticleMolecular & cellular proteomics : MCP2011

Fc-glycosylation of IgG1 is modulated by B-cell stimuli.

Jun Wang, Crina I A Balog, Kathrin Stavenhagen, Carolien A M Koeleman, Hans Ulrich Scherer, Maurice H J Selman, André M Deelder, Tom W J Huizinga, René E M Toes, Manfred Wuhrer

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed, 1 pooled it
16.2field-weighted citation impact, top 1% 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

82 citing papers in PubMed, 1 synthesis or guideline pooled it, 161 citations in OpenAlex.

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  13. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
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22 more citing papers are in PubMed but not listed here.

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 2 countries.

Jun WangDepartment of Rheumatology, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, The Netherlands.
Crina I A Balog
Kathrin Stavenhagen
Carolien A M Koeleman
Hans Ulrich Scherer
Maurice H J Selman
André M Deelder
Tom W J Huizinga
René E M Toes
Manfred Wuhrer
Leiden University Medical Center · NLCenter for Rheumatology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have recently shown that IgG1 directed against antigens thought to be involved in the pathogenesis of rheumatoid arthritis harbor different glycan moieties on their Fc-tail, as compared with total sera IgG1. Given the crucial roles of Fc-linked N-glycans for the structure and biological activity of IgG, Fc-glycosylation of antibodies is receiving considerable interest. However, so far little is known about the signals and factors that could influence the composition of these carbohydrate structures on secreted IgG produced by B lymphocytes. Here we show that both "environmental" factors, such as all-trans retinoic acid (a natural metabolite of vitamin A), as well as factors stimulating the innate immune system (i.e. CpG oligodeoxynucleotide, a ligand for toll-like receptor 9) or coming from the adaptive immune system (i.e. interleukin-21, a T-cell derived cytokine) can modulate IgG1 Fc-glycosylation. These factors affect Fc-glycan profiles in different ways. CpG oligodeoxynucleotide and interleukin-21 increase Fc-linked galactosylation and reduce bisecting N-acetylglucosamine levels, whereas all-trans retinoic acid significantly decreases galactosylation and sialylation levels. Moreover, these effects appeared to be stable and specific for secreted IgG1 as no parallel changes of the corresponding glycans in the cellular glycan pool were observed. Interestingly, several other cytokines and molecules known to affect B-cell biology and antibody production did not have an impact on IgG1 Fc-coupled glycan profiles. Together, these data indicate that different stimuli received by B cells during their activation and differentiation can modulate the Fc-linked glycosylation of secreted IgG1 without affecting the general cellular glycosylation machinery. Our study, therefore, furthers our understanding of the regulation of IgG1 glycosylation at the cellular level.

Indexed as

AcetylglucosamineAnimalsB-LymphocytesCarrier ProteinsCell DifferentiationCells, CulturedGalactoseGlycosylationHumansImmunoglobulin Fc FragmentsInterleukin-21InterleukinsMiceOligodeoxyribonucleotidesSialic AcidsSteroidsAcetylglucosamineCarrier ProteinsCPG-oligonucleotideEA-4 (ATRA steroidal analog)GalactoseImmunoglobulin Fc FragmentsInterleukin-21InterleukinsOligodeoxyribonucleotidesprolactin-binding proteinSialic AcidsSteroidsTretinoin

Identifiers

PMID21372248
PMCPMC3098587
OpenAlexW2055973314

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.