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Open AccessArticle

Fine-Mapping of the Human Blood Plasma N-Glycome onto Its Proteome

1
Department of Physiology and Biophysics, Weill Cornell Medicine-Qatar, Education City, PO 24144, Doha, Qatar
2
BICRO BIOCentar, Glycoscience Research Laboratory, Genos Ltd., Borongajska cesta 83H, 10000 Zagreb, Croatia
3
Department of Clinical Epidemiology, Leiden University Medical Centre, P.O. Box 9600, 2300 RC Leiden, The Netherlands
4
Department of Twin Research and Genetic Epidemiology, King’s College London, London SE1 7EH, UK
5
Scientific Service Group Biomolecular Mass Spectrometry, Max Planck Institute for Heart and Lung Research, W.G. Kerckhoff Institute, Ludwigstr. 43, D-61231 Bad Nauheim, Germany
*
Author to whom correspondence should be addressed.
Metabolites 2019, 9(7), 122; https://doi.org/10.3390/metabo9070122
Received: 29 April 2019 / Revised: 21 June 2019 / Accepted: 24 June 2019 / Published: 26 June 2019
(This article belongs to the Special Issue Metabolomics in Epidemiological Studies)
Most human proteins are glycosylated. Attachment of complex oligosaccharides to the polypeptide part of these proteins is an integral part of their structure and function and plays a central role in many complex disorders. One approach towards deciphering this human glycan code is to study natural variation in experimentally well characterized samples and cohorts. High-throughput capable large-scale methods that allow for the comprehensive determination of blood circulating proteins and their glycans have been recently developed, but so far, no study has investigated the link between both traits. Here we map for the first time the blood plasma proteome to its matching N-glycome by correlating the levels of 1116 blood circulating proteins with 113 N-glycan traits, determined in 344 samples from individuals of Arab, South-Asian, and Filipino descent, and then replicate our findings in 46 subjects of European ancestry. We report protein-specific N-glycosylation patterns, including a correlation of core fucosylated structures with immunoglobulin G (IgG) levels, and of trisialylated, trigalactosylated, and triantennary structures with heparin cofactor 2 (SERPIND2). Our study reveals a detailed picture of protein N-glycosylation and suggests new avenues for the investigation of its role and function in the associated complex disorders. View Full-Text
Keywords: glycomics; proteomics; N-glycosylation; population study; aptamers; HILIC-UPLC; SOMAscan glycomics; proteomics; N-glycosylation; population study; aptamers; HILIC-UPLC; SOMAscan
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Suhre, K.; Trbojević-Akmačić, I.; Ugrina, I.; Mook-Kanamori, D.O.; Spector, T.; Graumann, J.; Lauc, G.; Falchi, M. Fine-Mapping of the Human Blood Plasma N-Glycome onto Its Proteome. Metabolites 2019, 9, 122.

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