학술논문
Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers.
Document Type
article
Author
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; Igor Rudan
Source
PLoS Genetics, Vol 9, Iss 1, p e1003225 (2013)
Subject
Language
English
ISSN
1553-7390
1553-7404
1553-7404
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