Evidence map›Paper›PMID 19490625›Full record

ArticleBMC cell biology2009

The N-glycome of human embryonic stem cells.

Tero Satomaa, Annamari Heiskanen, Milla Mikkola, Cia Olsson, Maria Blomqvist, Minna Tiittanen, Taina Jaatinen, Olli Aitio, Anne Olonen, Jari Helin and 6 more

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 108 citations in OpenAlex.

  1. The restricted N-glycome of neurons is programmed during differentiation.bioRxiv : the preprint server for biology · 2024
    Article
  2. Conformational Properties of ArylThe Journal of organic chemistry · 2023
    Article
  3. Article
  4. ReliableMolecules (Basel, Switzerland) · 2023
    Article
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  8. Establishing Rules for Self-Adhesion and Aggregation ofLangmuir : the ACS journal of surfaces and colloids · 2020
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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

16 authors at 4 institutions in 1 country.

Tero SatomaaGlykos Finland Ltd, Helsinki, Finland. tero.satomaa@glykos.fi
Annamari Heiskanen
Milla Mikkola
Cia Olsson
Maria Blomqvist
Minna Tiittanen
Taina Jaatinen
Olli Aitio
Anne Olonen
Jari Helin
Jukka Hiltunen
Jari Natunen
Timo Tuuri
Timo Otonkoski
Juhani Saarinen
Jarmo Laine
Glykos (Finland) · FIFinnish Red Cross · FIUniversity of Helsinki · FIVäestöliitto · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundComplex carbohydrate structures, glycans, are essential components of glycoproteins, glycolipids, and proteoglycans. While individual glycan structures including the SSEA and Tra antigens are already used to define undifferentiated human embryonic stem cells (hESC), the whole spectrum of stem cell glycans has remained unknown. We undertook a global study of the asparagine-linked glycoprotein glycans (N-glycans) of hESC and their differentiated progeny using MALDI-TOF mass spectrometric and NMR spectroscopic profiling. Structural analyses were performed by specific glycosidase enzymes and mass spectrometric fragmentation analyses.

resultsThe data demonstrated that hESC have a characteristic N-glycome which consists of both a constant part and a variable part that changes during hESC differentiation. hESC-associated N-glycans were downregulated and new structures emerged in the differentiated cells. Previously mouse embryonic stem cells have been associated with complex fucosylation by use of SSEA-1 antibody. In the present study we found that complex fucosylation was the most characteristic glycosylation feature also in undifferentiated hESC. The most abundant complex fucosylated structures were Lex and H type 2 antennae in sialylated complex-type N-glycans.

conclusionThe N-glycan phenotype of hESC was shown to reflect their differentiation stage. During differentiation, hESC-associated N-glycan features were replaced by differentiated cell-associated structures. The results indicated that hESC differentiation stage can be determined by direct analysis of the N-glycan profile. These results provide the first overview of the N-glycan profile of hESC and form the basis for future strategies to target stem cell glycans.

Indexed as

GlycomicsCarbohydrate ConformationCarbohydrate SequenceCell DifferentiationDown-RegulationEmbryonic Stem CellsFucoseHumansMolecular Sequence DataPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationFucosePolysaccharides

Identifiers

PMID19490625
PMCPMC2696424
OpenAlexW2031598261

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.