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Depositordc.contributorKlaric, Lucija
Funderdc.contributor.otherMRC - Medical Research Councilen_UK
Data Creatordc.creatorHuffman, Jennifer
Data Creatordc.creatorHayward, Caroline
Date Accessioneddc.date.accessioned2017-07-03T14:53:55Z
Date Availabledc.date.available2017-07-03T14:53:55Z
Citationdc.identifier.citationHuffman, Jennifer; Hayward, Caroline. (2017). Dataset pertaining to the publication “Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults.”, [dataset]. Human Genetics Unit, Medical Research Council. Institute of Genetics and Molecular Medicine, University of Edinburgh. https://doi.org/10.7488/ds/2090.en
Persistent Identifierdc.identifier.urihttps://hdl.handle.net/10283/2759
Persistent Identifierdc.identifier.urihttps://doi.org/10.7488/ds/2090
Dataset Description (abstract)dc.description.abstractThe majority of human proteins are post-translationally modified by covalent addition of one or more complex oligosaccharides (glycans). Alterations in glycosylation processing are associated with numerous diseases and glycans are attracting increasing attention both as disease biomarkers and as targets for novel therapeutic approaches. Using a recently developed high-throughput high-performance liquid chromatography (HPLC) analysis method, we have reported, in a pilot genome-wide association study of 13 glycan features in 2705 individuals from three European populations, that polymorphisms at three loci (FUT8, FUT6/FUT3 and HNF1A) affect plasma levels of N-glycans. Here, we extended the analysis to 33 directly measured and 13 derived glycosylation traits in 3533 individuals and identified three novel gene association (MGAT5, B3GAT1 and SLC9A9) as well as replicated the previous findings using an additional European cohort. MGAT5 (meta-analysis association P-value = 1.80 × 10−10 for rs1257220) encodes a glycosyltransferase which is known to synthesize the associated glycans. In contrast, neither B3GAT1 (rs7928758, P = 1.66 × 10−08) nor SLC9A9 (rs4839604, P = 3.50 × 10−13) had previously been associated functionally with glycosylation of plasma proteins. Given the glucuronyl transferase activity of B3GAT1, we were able to show that glucuronic acid is present on antennae of plasma glycoproteins underlying the corresponding HPLC peak. SLC9A9 encodes a proton pump which affects pH in the endosomal compartment and it was recently reported that changes in Golgi pH can impair protein sialylation, giving a possible mechanism for the observed association.en_UK
Dataset Description (TOC)dc.description.tableofcontentsPlease see PlasmaGlycansGWAS_README_DATASHARE.pdfen_UK
Languagedc.language.isoengen_UK
Publisherdc.publisherHuman Genetics Unit, Medical Research Council. Institute of Genetics and Molecular Medicine, University of Edinburghen_UK
Relation (Is Referenced By)dc.relation.isreferencedbyhttp://hmg.oxfordjournals.org/content/20/24/5000.longen_UK
Rightsdc.rightsCreative Commons Attribution 4.0 International Public Licenseen
Subjectdc.subjectGWASen_UK
Subjectdc.subjectplasma glycansen_UK
Subjectdc.subjectpopulation geneticsen_UK
Subject Classificationdc.subject.classificationBiological Sciences::Molecular Geneticsen_UK
Titledc.titleDataset pertaining to the publication “Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults.”en_UK
Typedc.typedataseten_UK

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