High Throughput Isolation and Glycosylation Analysis of IgG–Variability and Heritability of the IgG Glycome in Three Isolated Human Populations
Maja Pučić,Ana Knezevic,Jana Vidič,Barbara Adamczyk,Mislav Novokmet,Ozren Polasek,Olga Gornik,Sandra Supraha-Goreta,Mark R. Wormald,Irma Redzic,Harry Campbell,Alan F. Wright,Nicholas D. Hastie,James F. Wilson,Igor Rudan,Manfred Wuhrer,Pauline M. Rudd,Djuro Josic,Djuro Josic,Gordan Lauc +19 more
TLDR
The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs.About:
This article is published in Molecular & Cellular Proteomics.The article was published on 2011-10-01 and is currently open access. It has received 422 citations till now. The article focuses on the topics: Glycome & Glycosylation.read more
Citations
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Biological Age Predictors
TL;DR: Current state-of-the-art findings considering six potential types of biological age predictors are summarized, including epigenetic clocks, telomere length, transcriptomic predictors, proteomic Predictors, metabolomics-based predictor, and composite biomarker predictors.
Journal ArticleDOI
Glycans as cancer biomarkers.
TL;DR: The ability to distinguish differences in the glycosylation of proteins between cancer and control patients emphasizes glycobiology as a promising field for potential biomarker identification.
Journal ArticleDOI
Mucins: A biologically relevant glycan barrier in mucosal protection
TL;DR: Mucin biology is dynamic and the processes of degradation and turnover are well integrated with biosynthesis to maintain a continuous mucosal protection against all external aggressive forces.
Journal ArticleDOI
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,Lina Zgaga,Barbara Adamczyk,Ana Mužinić,Mislav Novokmet,Ozren Polasek,Olga Gornik,Jasminka Krištić,Toma Keser,Veronique Vitart,Blanca Scheijen,Hae-Won Uh,Mariam Molokhia,Alan L. Patrick,Paul M. McKeigue,Ivana Kolcic,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,Wei Wang,Wei Wang,Nicholas D. Hastie,Ulf Gyllensten,James F. Wilson,Manfred Wuhrer,Alan F. Wright,Pauline M. Rudd,Caroline Hayward,Yurii S. Aulchenko,Harry Campbell,Igor Rudan +41 more
TL;DR: This study shows that it is possible to identify new loci that control glycosylation of a single plasma protein using genome-wide association study (GWAS), and may provide an explanation for the reported pleiotropy and antagonistic effects of loci involved in autoimmune diseases and haematological cancer.
Journal ArticleDOI
MS-Based Allotype-Specific Analysis of Polyclonal IgG-Fc N-Glycosylation
Thomas Sénard,Andrea F.G. Gargano,Andrea F.G. Gargano,David Falck,Steven W. de Taeye,Theo Rispens,Gestur Vidarsson,Manfred Wuhrer,Govert W. Somsen,Elena Domínguez-Vega +9 more
TL;DR: This paper proposes a middle-up strategy for the analysis of the intact fragment crystallizable (Fc) region of human plasma IgGs, with the aim of acquiring integrated information of the N-glycosylation and other PTMs of subclasses and allotypes.
References
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