PubMed:16037488 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/16037488","sourcedb":"PubMed","sourceid":"16037488","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/16037488","text":"Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia.\nUntreated classic galactosemia (galactose-1-phosphate uridyltransferase [GALT] deficiency) is known as a secondary congenital disorders of glycosylation (CDG) characterized by galactose deficiency of glycoproteins and glycolipids (processing defect or CDG-II). The mechanism of this undergalactosylation has not been established. Here we show that in untreated galactosemia, there is also a partial deficiency of whole glycans of serum transferrin associated with increased fucosylation and branching as seen in genetic glycosylation assembly defects (CDG-I). Thus galactosemia seems to be a secondary \"dual\" CDG causing a processing as well as an assembly N-glycosylation defect. We also demonstrated that in galactosemia patients, transferrin N-glycan biosynthesis is restored upon dietary 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