Evidence map›Paper›PMID 31616032›Full record

ArticleScientific reports2019

Site-specific N-glycosylation of HeLa cell glycoproteins.

Lilla Turiák, Simon Sugár, András Ács, Gábor Tóth, Ágnes Gömöry, András Telekes, Károly Vékey, László Drahos

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  10. Comprehensive MembraneMass spectrometry (Tokyo, Japan) · 2023
    Article
  11. International journal of molecular sciences · 2022
    Article
  12. Article
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  14. Article
  15. Review
  16. 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

8 authors at 3 institutions in 1 country.

Lilla TuriákMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary. turiak.lilla@ttk.mta.hu.
Simon SugárMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.
András ÁcsMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.
Gábor TóthMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.
Ágnes GömöryMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.
András TelekesDepartment of Oncology, St Lazarus County Hospital, Füleki út 54-56, H-3100, Salgótarján, Hungary.
Károly VékeyMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.
László DrahosMS Proteomics Research Group, Research Centre for Natural Sciences, Magyar tudósok körútja 2, H-1117, Budapest, Hungary.ORCID http://orcid.org/0000-0001-9589-6652
HUN-REN Research Centre for Natural Sciences · HUBudapest University of Technology and Economics · HUSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have characterized site-specific N-glycosylation of the HeLa cell line glycoproteins, using a complex workflow based on high and low energy tandem mass spectrometry of glycopeptides. The objective was to obtain highly reliable data on common glycoforms, so rigorous data evaluation was performed. The analysis revealed the presence of a high amount of bovine serum contaminants originating from the cell culture media - nearly 50% of all glycans were of bovine origin. Unaccounted, the presence of bovine serum components causes major bias in the human cellular glycosylation pattern; as is shown when literature results using released glycan analysis are compared. We have reliably identified 43 (human) glycoproteins, 69 N-glycosylation sites, and 178 glycoforms. HeLa glycoproteins were found to be highly (68.7%) fucosylated. A medium degree of sialylation was observed, on average 46.8% of possible sialylation sites were occupied. High-mannose sugars were expressed in large amounts, as expected in the case of a cancer cell line. Glycosylation in HeLa cells is highly variable. It is markedly different not only on various proteins but also at the different glycosylation sites of the same protein. Our method enabled the detailed characterization of site-specific N-glycosylation of several glycoproteins expressed in HeLa cell line.

Indexed as

Culture MediaGlycoproteinsGlycosylationHeLa CellsHumansMetabolomicsPolysaccharidesTandem Mass SpectrometryCulture MediaGlycoproteinsPolysaccharides

Identifiers

PMID31616032
PMCPMC6794373
OpenAlexW2981099567

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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.