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Apolipoprotein C‐III O ‐glycoform profiling of 500 serum samples by matrix‐assisted laser desorption/ionization mass spectrometry for diagnosis of congenital disorders of glycosylation
Author(s) -
Wada Yoshinao,
Okamoto Nobuhiko
Publication year - 2021
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.4597
Subject(s) - chemistry , glycosylation , mass spectrometry , apolipoprotein b , matrix assisted laser desorption/ionization , glycan , glycoconjugate , glycation , biochemistry , fucosylation , chromatography , glycoprotein , desorption , adsorption , organic chemistry , receptor , cholesterol
Congenital disorders of glycosylation (CDG) are caused by defects in various genes governing glycoconjugate biosynthesis. Several responsible genes have been identified in the protein N ‐glycosylation process. Analyses of mucin‐type core‐1 O ‐glycoform of apolipoprotein C‐III (apoCIII) have recently revealed combined N ‐ and O ‐glycosylation defects. We applied matrix‐assisted laser desorption/ionization mass spectrometry profiling of apoCIII glycoforms to 500 serum samples for CDG screening, and reference values were determined. The content of unglycosylated apoCIII was low in early infancy, indicating that the O ‐glycan occupancy should be assessed based on age‐matched reference values. The samples from patients with mutations in the ALG1 , ATP6V0A2 , B4GALT1 , COG2 , GCS1 , PGM1 , SLC35A2 , and TRAPPC11 genes were analyzed. B4GALT1‐ and TRAPPC11‐CDG were accompanied by under‐sialylation of O ‐glycans and are now recognized as combined N ‐ and O ‐glycosylation disorders.