Evidence map›Paper›PMID 24039863›Full record

ArticlePloS one2013

Targeted biomarker discovery by high throughput glycosylation profiling of human plasma alpha1-antitrypsin and immunoglobulin A.

L Renee Ruhaak, Carolien A M Koeleman, Hae-Won Uh, Jord C Stam, Diana van Heemst, Andrea B Maier, Jeanine J Houwing-Duistermaat, Paul J Hensbergen, P Eline Slagboom, André M Deelder and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
2.4field-weighted citation impact, top 11% 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, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Glycosylation and Aging.Advances in experimental medicine and biology · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. High-throughput SerumMolecular & cellular proteomics : MCP · 2019
    Article
  14. Article
  15. Review
  16. Review
  17. Glycomic and glycoproteomic analysis of glycoproteins-a tutorial.Analytical and bioanalytical chemistry · 2017
    Article
  18. Article
  19. Review
  20. Article
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 2 institutions in 1 country.

L Renee RuhaakCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Carolien A M Koeleman
Hae-Won Uh
Jord C Stam
Diana van Heemst
Andrea B Maier
Jeanine J Houwing-Duistermaat
Paul J Hensbergen
P Eline Slagboom
André M Deelder
Manfred Wuhrer
Leiden University Medical Center · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N-glycosylation patterns are known to show vast genetic as well as physiological and pathological variation and represent a large pool of potential biomarkers. Large-scale studies are needed for the identification and validation of biomarkers, and the analytical techniques required have recently been developed. Such methods have up to now mainly been applied to complex mixtures of glycoproteins in biofluids (e.g. plasma). Here, we analyzed N-glycosylation profiles of alpha1-antitrypsin (AAT) and immunoglobulin A (IgA) enriched fractions by 96-well microtitration plate based high-throughput immuno-affinity capturing and N-glycan analysis using multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (CGE-LIF). Human plasma samples were from the Leiden Longevity Study comprising 2415 participants of different chronological and biological ages. Glycosylation patterns of AAT enriched fractions were found to be associated with chronological (calendar) age and they differed between females and males. Moreover, several glycans in the AAT enriched fraction were associated with physiological parameters marking cardiovascular and metabolic diseases. Pronounced differences were found between males and females in the glycosylation profiles of IgA enriched fractions. Our results demonstrate that large-scale immuno-affinity capturing of proteins from human plasma using a bead-based method combined with high-throughput N-glycan analysis is a powerful tool for the discovery of glycosylation-based biomarker candidates.

Indexed as

ProteomicsAge Factorsalpha 1-AntitrypsinBiomarkersFemaleGlycoproteinsGlycosylationHigh-Throughput Screening AssaysHumansImmunoglobulin AInflammationLongevityMalePolysaccharidesReproducibility of ResultsSex Factorsalpha 1-AntitrypsinBiomarkersGlycoproteinsImmunoglobulin APolysaccharides

Identifiers

PMID24039863
PMCPMC3767703
OpenAlexW2086381568

What OpenQuestion holds

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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.