Evidence map›Paper›PMID 29343697›Full record

ArticleScientific reports2018

Effluent and serum protein N-glycosylation is associated with inflammation and peritoneal membrane transport characteristics in peritoneal dialysis patients.

Evelina Ferrantelli, Karima Farhat, Agnes L Hipgrave Ederveen, Karli R Reiding, Robert H J Beelen, Frans J van Ittersum, Manfred Wuhrer, Viktoria Dotz

Open access · goldAbstract readMulticenter Study
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Proteomic Research in Peritoneal Dialysis.International journal of molecular sciences · 2020
    Review
  11. Sialic acid derivatization for glycan analysis by mass spectrometry.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  12. 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.

Evelina FerrantelliVU University Medical Center, Department of Molecular Cell Biology and Immunology, Amsterdam, The Netherlands.
Karima FarhatVU University Medical Center, Department of Nephrology, Amsterdam, The Netherlands.
Agnes L Hipgrave EderveenCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Karli R ReidingCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Robert H J BeelenVU University Medical Center, Department of Molecular Cell Biology and Immunology, Amsterdam, The Netherlands.
Frans J van IttersumVU University Medical Center, Department of Nephrology, Amsterdam, The Netherlands.
Manfred WuhrerVU University Medical Center, Department of Molecular Cell Biology and Immunology, Amsterdam, The Netherlands.ORCID http://orcid.org/0000-0002-0814-4995
Viktoria DotzCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands. v-dotz@t-online.de.ORCID http://orcid.org/0000-0002-9888-7409
Leiden University Medical Center · NLAmsterdam UMC Location Vrije Universiteit Amsterdam · NLAmsterdam UMC Location University of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mass spectrometric glycomics was used as an innovative approach to identify biomarkers in serum and dialysate samples from peritoneal dialysis (PD) patients. PD is a life-saving treatment worldwide applied in more than 100,000 patients suffering from chronic kidney disease. PD treatment uses the peritoneum as a natural membrane to exchange waste products from blood to a glucose-based solution. Daily exposure of the peritoneal membrane to these solutions may cause complications such as peritonitis, fibrosis and inflammation which, in the long term, lead to the failure of the treatment. It has been shown in the last years that protein N-glycosylation is related to inflammatory and fibrotic processes. Here, by using a recently developed MALDI-TOF-MS method with linkage-specific sialic acid derivatisation, we showed that alpha2,6-sialylation, especially in triantennary N-glycans from peritoneal effluents, is associated with critical clinical outcomes in a prospective cohort of 94 PD patients. Moreover, we found an association between the levels of presumably immunoglobulin-G-related glycans as well as galactosylation of diantennary glycans with PD-related complications such as peritonitis and loss of peritoneal mesothelial cell mass. The observed glycomic changes point to changes in protein abundance and protein-specific glycosylation, representing candidate functional biomarkers of PD and associated complications.

Indexed as

Biological TransportBiomarkersBlood ProteinsDialysis SolutionsFemaleFibrosisGlucoseGlycosylationHumansInflammationMaleMembrane Transport ProteinsMiddle AgedPeritoneal DialysisPeritoneumPeritonitisBiomarkersBlood ProteinsDialysis SolutionsGlucoseMembrane Transport Proteins

Identifiers

PMID29343697
PMCPMC5772620
OpenAlexW2783591628

What OpenQuestion holds

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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.