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Frkatović-Hodžić, Azra; Mijakovac, Anika; Miškec, Karlo; Nostaeva, Arina; Sharapov, Sodbo Z; Landini, Arianna; Haller, Toomas; Akker, Erik van den; Sharma, Sapna; Cuadrat, Rafael R C; Mangino, Massimo; Li, Yong; Keser, Toma; Rudman, Najda; Štambuk, Tamara; Pučić-Baković, Maja; Trbojević-Akmačić, Irena; Gudelj, Ivan; Štambuk, Jerko; Pribić, Tea; Radovani, Barbara; Tominac, Petra; Fischer, Krista; Beekman, Marian; Wuhrer, Manfred; Gieger, Christian; Schulze, Matthias B; Wittenbecher, Clemens; Polasek, Ozren; Hayward, Caroline; Wilson, James F; Spector, Tim D; Köttgen, Anna; Vučković, Frano; Aulchenko, Yurii S; Vojta, Aleksandar; Krištić, Jasminka; Klarić, Lucija; Zoldoš, Vlatka; Lauc, Gordan
Aging (Albany, NY.), 12/2023, Letnik: 15, Številka: 24Journal Article
Glycans are an essential structural component of immunoglobulin G (IgG) that modulate its structure and function. However, regulatory mechanisms behind this complex posttranslational modification are not well known. Previous genome-wide association studies (GWAS) identified 29 genomic regions involved in regulation of IgG glycosylation, but only a few were functionally validated. One of the key functional features of IgG glycosylation is the addition of galactose (galactosylation), a trait which was shown to be associated with ageing. We performed GWAS of IgG galactosylation (N=13,705) and identified 16 significantly associated loci, indicating that IgG galactosylation is regulated by a complex network of genes that extends beyond the galactosyltransferase enzyme that adds galactose to IgG glycans. Gene prioritization identified 37 candidate genes. Using a recently developed CRISPR/dCas9 system we manipulated gene expression of candidate genes in the IgG expression system. Upregulation of three genes, and , changed the IgG glycome composition, which confirmed that these three genes are involved in IgG galactosylation in this expression system.
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in: SICRIS
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