Autor: |
Rebeka Kodríková, Zuzana Pakanová, Maroš Krchňák, Mária Šedivá, Sergej Šesták, Filip Květoň, Gábor Beke, Anna Šalingová, Katarína Skalická, Katarína Brennerová, Emília Jančová, Peter Baráth, Ján Mucha, Marek Nemčovič |
Jazyk: |
angličtina |
Rok vydání: |
2023 |
Předmět: |
|
Zdroj: |
Biomedicines, Vol 11, Iss 2, p 580 (2023) |
Druh dokumentu: |
article |
ISSN: |
2227-9059 |
DOI: |
10.3390/biomedicines11020580 |
Popis: |
Congenital disorders of glycosylation (CDG) are a group of rare inherited metabolic disorders caused by a defect in the process of protein glycosylation. In this work, we present a comprehensive glycoprofile analysis of a male patient with a novel missense variant in the SLC35A2 gene, coding a galactose transporter that translocates UDP-galactose from the cytosol to the lumen of the endoplasmic reticulum and Golgi apparatus. Isoelectric focusing of serum transferrin, which resulted in a CDG type II pattern, was followed by structural analysis of transferrin and serum N-glycans, as well as the analysis of apolipoprotein CIII O-glycans by mass spectrometry. An abnormal serum N-glycoprofile with significantly increased levels of agalactosylated (Hex3HexNAc4-5 and Hex3HexNAc5Fuc1) and monogalactosylated (Hex4HexNAc4 ± NeuAc1) N-glycans was observed. Additionally, whole exome sequencing and Sanger sequencing revealed de novo hemizygous c.461T > C (p.Leu154Pro) mutation in the SLC35A2 gene. Based on the combination of biochemical, analytical, and genomic approaches, the set of distinctive N-glycan biomarkers was characterized. Potentially, the set of identified aberrant N-glycans can be specific for other variants causing SLC35A2-CDG and can distinguish this disorder from the other CDGs or other defects in the galactose metabolism. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
|