Evidence map›Paper›PMID 21300843›Full record

ArticleDiabetes2011

Glycosylation failure extends to glycoproteins in gestational diabetes mellitus: evidence from reduced α2-6 sialylation and impaired immunomodulatory activities of pregnancy-related glycodelin-A.

Cheuk-Lun Lee, Philip C N Chiu, Poh-Choo Pang, Ivan K Chu, Kai-Fai Lee, Riitta Koistinen, Hannu Koistinen, Markku Seppälä, Howard R Morris, Bérangère Tissot and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Diabetes, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Observational
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. The story of the SdGlycoconjugate journal · 2023
    Review
  12. Review
  13. Article
  14. Review
  15. Identification of Sialyl-Lewis(x)-Interacting Protein on Human Spermatozoa.Frontiers in cell and developmental biology · 2021
    Article
  16. Review
  17. Protein Glycosylation in Diabetes.Advances in experimental medicine and biology · 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

13 authors at 3 institutions in 2 countries.

Cheuk-Lun LeeDepartment of Obstetrics and Gynecology, University of Hong Kong, Hong Kong, China.
Philip C N Chiu
Poh-Choo Pang
Ivan K Chu
Kai-Fai Lee
Riitta Koistinen
Hannu Koistinen
Markku Seppälä
Howard R Morris
Bérangère Tissot
Maria Panico
Anne Dell
William S B Yeung
University of Hong Kong · HKHelsinki University Hospital · FIUniversity of Helsinki · FI

Funding

Biotechnology and Biological Sciences Research Council BBF0083091
6 · The paper itself

Abstract

objectiveGestational diabetes mellitus (GDM) is a common metabolic disorder of pregnancy. Patients with GDM are at risk for high fetal mortality and gestational complications associated with reduced immune tolerance and abnormal carbohydrate metabolism. Glycodelin-A (GdA) is an abundant decidual glycoprotein with glycosylation-dependent immunomodulatory activities. We hypothesized that aberrant carbohydrate metabolism in GDM was associated with changes in glycosylation of GdA, leading to defective immunomodulatory activities. RESEARCH DESIGN AND

methodsGdA in the amniotic fluid from women with normal (NGdA) and GDM (DGdA) pregnancies was purified by affinity chromatography. Structural analysis of protein glycosylation was preformed by lectin-binding assay and mass spectrometry. Cytotoxicity, cell death, cytokine secretion, and GdA binding of the GdA-treated lymphocytes and natural killer (NK) cells were determined. The sialidase activity in the placental tissue from normal and GDM patients was measured.

resultsGDM affected the glycosylation but not the protein core of GdA. Specifically, DGdA had a lower abundance of α2-6-sialylated and high-mannose glycans and a higher abundance of glycans with Sda (NeuAcα2-3[GalNAcβ1-4]Gal) epitopes compared with NGdA. DGdA had reduced immuosuppressive activities in terms of cytotoxicity on lymphocytes, inhibitory activities on interleukin (IL)-2 secretion by lymphocytes, stimulatory activities on IL-6 secretion by NK cells, and binding to these cells. Desialylation abolished the immunomodulation and binding of NGdA. Placental sialidase activity was increased in GDM patients, which may account for the reduced sialic acid content of DGdA.

conclusionsTaken together, this study provides the first direct evidence for altered enzymatic glycosylation and impaired bioactivity of GdA in GDM patients.

Indexed as

AdultAmniotic FluidAnalysis of VarianceCell DeathDiabetes, GestationalFemaleFlow CytometryGas Chromatography-Mass SpectrometryGlycodelinGlycoproteinsGlycosylationHumansInterleukin-6LectinsN-Acetylneuraminic AcidPregnancyGlycodelinGlycoproteinsInterleukin-6LectinsN-Acetylneuraminic AcidPAEP protein, humanPregnancy Proteins

Identifiers

PMID21300843
PMCPMC3046852
OpenAlexW2158268603

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.