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*

*Corresponding author for this work

    Research output: Contribution to JournalArticleAcademicpeer-review

    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.

    Original languageEnglish
    Article number979
    Pages (from-to)1-11
    Number of pages11
    JournalScientific Reports
    Volume8
    Issue number1
    DOIs
    Publication statusPublished - 17 Jan 2018

    Funding

    This work was supported by the European Union, Seventh Framework Programme via the projects EuTRiPD under grant agreement Marie Curie ITN-GA-2011-287813 (E.F.) as well as HighGlycan under grant agreement HEALTH-F5-2011-278535 (K.R.R., A.L.H.E. and M.W.) This work was supported by the European Union, Seventh Framework Programme via the projects “EuTRiPD” under grant agreement Marie Curie ITN-GA-2011-287813 (E.F.) as well as “HighGlycan” under grant agreement HEALTH-F5-2011-278535 (K.R.R., A.L.H.E. and M.W.).

    FundersFunder number
    Seventh Framework Programme278535, 287813
    Marie CurieITN-GA-2011-287813, HEALTH-F5-2011-278535
    European Commission
    Seventh Framework Programme

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