Evidence map›Paper›PMID 25825024›Full record

ArticleNature communications2015

Glycosylation of immunoglobulin G determines osteoclast differentiation and bone loss.

Ulrike Harre, Stefanie C Lang, René Pfeifle, Yoann Rombouts, Sabine Frühbeißer, Khaled Amara, Holger Bang, Anja Lux, Carolien A Koeleman, Wolfgang Baum and 11 more

Registry-linked trialAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03394092 (Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis), which is not on this map. Cited by 148 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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.

NCT03394092 completednot on this mapstarted 2018, after this paper: background citation

Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis

TypeobservationalSponsorThe First Affiliated Hospital of Dalian Medical UniversityRan2018 to 2019Enrolled100ConditionsAcute Coronary SyndromeArmsQuantitative measurements the changes of IgG glycosylation
3 · Its place in the literature

Who cites it

148 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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88 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors.

Ulrike HarreDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Stefanie C LangDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
René Pfeifle1] Department of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany [2] Nikolaus Fiebiger Center of Molecular Medicine, University of Erlangen- Nuremberg, Erlangen 91054, Germany.
Yoann Rombouts1] Department of Rheumatology, Leiden University Medical Center, Leiden 2300 RC, The Netherlands [2] Center of Proteomics and Metabolomics, Leiden University Medical Center, Leiden 2300 RC, The Netherlands.
Sabine FrühbeißerDepartment of Chemistry and Pharmacy, Interdisciplinary Center for Molecular Materials (ICMM), University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Khaled AmaraRheumatology Unit, Department of Medicine, Karolinska Institute and Karolinska University Hospital, Solna 17177, Sweden.
Holger BangOrgentec Diagnostika, Mainz 55129, Germany.
Anja LuxDepartment of Genetics, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Carolien A Koeleman1] Department of Rheumatology, Leiden University Medical Center, Leiden 2300 RC, The Netherlands [2] Center of Proteomics and Metabolomics, Leiden University Medical Center, Leiden 2300 RC, The Netherlands.
Wolfgang BaumDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Katharina DietelDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Franziska GröhnDepartment of Chemistry and Pharmacy, Interdisciplinary Center for Molecular Materials (ICMM), University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Vivianne MalmströmRheumatology Unit, Department of Medicine, Karolinska Institute and Karolinska University Hospital, Solna 17177, Sweden.
Lars KlareskogRheumatology Unit, Department of Medicine, Karolinska Institute and Karolinska University Hospital, Solna 17177, Sweden.
Gerhard Krönke1] Department of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany [2] Nikolaus Fiebiger Center of Molecular Medicine, University of Erlangen- Nuremberg, Erlangen 91054, Germany.
Roland KocijanDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Falk NimmerjahnDepartment of Genetics, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
René E M ToesDepartment of Rheumatology, Leiden University Medical Center, Leiden 2300 RC, The Netherlands.
Martin HerrmannDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.
Hans Ulrich SchererDepartment of Rheumatology, Leiden University Medical Center, Leiden 2300 RC, The Netherlands.
Georg SchettDepartment of Internal Medicine 3, University of Erlangen-Nuremberg, Erlangen 91054, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunglobulin G (IgG) sialylation represents a key checkpoint that determines the engagement of pro- or anti-inflammatory Fcγ receptors (FcγR) and the direction of the immune response. Whether IgG sialylation influences osteoclast differentiation and subsequently bone architecture has not been determined yet, but may represent an important link between immune activation and bone loss. Here we demonstrate that desialylated, but not sialylated, immune complexes enhance osteoclastogenesis in vitro and in vivo. Furthermore, we find that the Fc sialylation state of random IgG and specific IgG autoantibodies determines bone architecture in patients with rheumatoid arthritis. In accordance with these findings, mice treated with the sialic acid precursor N-acetylmannosamine (ManNAc), which results in increased IgG sialylation, are less susceptible to inflammatory bone loss. Taken together, our findings provide a novel mechanism by which immune responses influence the human skeleton and an innovative treatment approach to inhibit immune-mediated bone loss.

Indexed as

AnimalsArthritis, ExperimentalArthritis, RheumatoidBone and BonesBone ResorptionCell DifferentiationDynamic Light ScatteringFemaleGalactoseGlycosylationHexosaminesHumansImmunoglobulin Fc FragmentsImmunoglobulin GMaleMiceGalactoseHexosaminesImmunoglobulin Fc FragmentsImmunoglobulin GN-acetylmannosamineN-Acetylneuraminic AcidReceptors, FcRNA, Messenger

Identifiers

PMID25825024
PMCPMC4389255

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Registered trials

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.