Mislav Novokmet

TL;DR: 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.

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.

TL;DR: This study has revealed very extensive and complex changes in IgG glycosylation with age, and the combined index composed of only three glycans explained up to 58% of variance in age, considerably more than other biomarkers of age like telomere lengths.

TL;DR: A novel approach combining genome-wide association and high-throughput glycomics analysis of 2,705 individuals in three population cohorts showed that common variants in the Hepatocyte Nuclear Factor 1α (HNF1α) and fucosyltransferase genes FUT6 and FUT8 influence N-glycan levels in human plasma.

TL;DR: Only a small fraction of the variability in glycan levels observed in a population was explained by age and other measured parameters, indicating that even in the absence of a genetic template, gly can levels are mostly determined by genetic background and/or specific pathophysiological processes.