Glycosylation of immunoglobulin G is regulated by a large network of genes pleiotropic with inflammatory diseases
Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide assoc...
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| Published in | Science advances Vol. 6; no. 8; p. eaax0301 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article Web Resource |
| Language | English |
| Published |
United States
American Association for the Advancement of Science (AAAS)
01.02.2020
American Association for the Advancement of Science |
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| Abstract | Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation (
= 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of
decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. |
|---|---|
| AbstractList | Variation in key transcription factors and glycogenes modifies IgG glycosylation and has an influence on inflammatory diseases.
Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation (
N
= 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of
IKZF1
decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. Variation in key transcription factors and glycogenes modifies IgG glycosylation and has an influence on inflammatory diseases. Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation ( N = 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of IKZF1 decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation (N = 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of IKZF1 decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation (N = 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of IKZF1 decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases.Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation (N = 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of IKZF1 decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant glycosylation of IgG has been observed in many diseases, but little is understood about the underlying mechanisms. We performed a genome-wide association study of IgG N-glycosylation ( = 8090) and, using a data-driven network approach, suggested how associated loci form a functional network. We confirmed in vitro that knockdown of decreases the expression of fucosyltransferase FUT8, resulting in increased levels of fucosylated glycans, and suggest that RUNX1 and RUNX3, together with SMARCB1, regulate expression of glycosyltransferase MGAT3. We also show that variants affecting the expression of genes involved in the regulation of glycoenzymes colocalize with variants affecting risk for inflammatory diseases. This study provides new evidence that variation in key transcription factors coupled with regulatory variation in glycogenes modifies IgG glycosylation and has influence on inflammatory diseases. |
| Author | Timofeeva, Maria Polasek, Ozren Trbojević-Akmačić, Irena Pakhomov, Eugene Georges, Michel Colhoun, Helen M Bermingham, Mairead L Zoldoš, Vlatka Salo, Perttu Štambuk, Jerko Grishchenko, Alexander K Fischer, Krista Sharapov, Sodbo Zh Stanton, Chloe M Deelen, Joris Keser, Toma Spector, Tim Drake, Camilla Rudan, Igor Dunlop, Malcolm G McGurnaghan, Stuart J Esko, Tõnu Pavić, Tamara Sikka, Timo Tõnis Beekman, Marian Dmitrieva, Julia Pučić-Baković, Maja Aulchenko, Yurii S Wuhrer, Manfred Mlinarec, Jelena Wilson, James F Mangino, Massimo Hayward, Caroline Campbell, Harry Klarić, Lucija Vilaj, Marija Ugrina, Ivo Vitart, Veronique Uh, Hae-Won Perola, Markus Dobrinić, Paula Lauc, Gordan Tsepilov, Yakov A Farrington, Susan M Vučković, Frano Plomp, Rosina Louis, Edouard Jelušić, Barbara Richmond, Anne Gudelj, Ivan Theodoratou, Evropi Krištić, Jasminka Slagboom, Eline P |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32128391$$D View this record in MEDLINE/PubMed |
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| Snippet | Effector functions of immunoglobulin G (IgG) are regulated by the composition of a glycan moiety, thus affecting activity of the immune system. Aberrant... Variation in key transcription factors and glycogenes modifies IgG glycosylation and has an influence on inflammatory diseases. Effector functions of... |
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| SubjectTerms | Algorithms Alleles Computational Biology - methods Gastroenterology & hepatology Gastroentérologie & hépatologie Gene Expression Regulation Genetic Loci Genome-Wide Association Study Glycosylation Human Genetics Human health sciences Humans Immunoglobulin G - immunology Immunoglobulin G - metabolism Immunoglobulin G/immunology/metabolism Immunology Inflammation - genetics Inflammation - metabolism Inflammation/genetics/metabolism Linkage Disequilibrium Models, Genetic Phenotype Polymorphism, Single Nucleotide Polysaccharides - metabolism SciAdv r-articles Sciences de la santé humaine |
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| Title | Glycosylation of immunoglobulin G is regulated by a large network of genes pleiotropic with inflammatory diseases |
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