Loci Associated with N-Glycosylation of Human Immunoglobulin G Show Pleiotropy with Autoimmune Diseases and Haematological Cancers
Gordan Lauc,
Jennifer E Huffman,
Maja Pučić,
Lina Zgaga,
Barbara Adamczyk,
Ana Mužinić,
Mislav Novokmet,
Ozren Polašek,
Olga Gornik,
Jasminka Krištić,
Toma Keser,
Veronique Vitart,
Blanca Scheijen,
Hae-Won Uh,
Mariam Molokhia,
Alan Leslie Patrick,
Paul McKeigue,
Ivana Kolčić,
Ivan Krešimir Lukić,
Olivia Swann,
Frank N van Leeuwen,
L Renee Ruhaak,
Jeanine J Houwing-Duistermaat,
P Eline Slagboom,
Marian Beekman,
Anton J M de Craen,
André M Deelder,
Qiang Zeng,
Wei Wang,
Nicholas D Hastie,
Ulf Gyllensten,
James F Wilson,
Manfred Wuhrer,
Alan F Wright,
Pauline M Rudd,
Caroline Hayward,
Yurii Aulchenko,
Harry Campbell and
Igor Rudan
PLOS Genetics, 2013, vol. 9, issue 1, 1-17
Abstract:
Glycosylation of immunoglobulin G (IgG) influences IgG effector function by modulating binding to Fc receptors. To identify genetic loci associated with IgG glycosylation, we quantitated N-linked IgG glycans using two approaches. After isolating IgG from human plasma, we performed 77 quantitative measurements of N-glycosylation using ultra-performance liquid chromatography (UPLC) in 2,247 individuals from four European discovery populations. In parallel, we measured IgG N-glycans using MALDI-TOF mass spectrometry (MS) in a replication cohort of 1,848 Europeans. Meta-analysis of genome-wide association study (GWAS) results identified 9 genome-wide significant loci (P
Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:plo:pgen00:1003225
DOI: 10.1371/journal.pgen.1003225
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