PubMed · 214839
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A D Petrescu. [Fructose in pediatrics].. https://pubmed.ncbi.nlm.nih.gov/214839/
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Fibroblasts of Carbohydrate Deficient Glycoprotein Syndrome (CDGS) patients synthesize smaller lipid-linked oligosaccharides and incorporate less [3H]-mannose into glycoproteins than controls. Adding mannose, but not glucose, to the culture medium simultaneously corrects both lesions, suggesting that CDGS cells lack sufficient mannose for normal glycosylation. Since mannose for glycoprotein synthesis is assumed to come from glucose, CDGS patients could have defective enzymes in this pathway. Here we show that these enzymes are normal in five CDGS cell lines. This suggests that much of the mannose for glycoprotein synthesis in fibroblasts may come from other, as yet unidentified, pathways.
We describe seven children with the carbohydrate-deficient glycoprotein syndrome, an autosomal recessive inborn error of protein glycosylation characterised by failure to thrive, neurological dysfunction and a unique pattern of physical abnormalities. Neuro-radiological investigations revealed cerebellar hypoplasia in all seven children. Two children also developed supratentorial atrophy following episodes of neurological deterioration.
The structure of the defective transferrin in carbohydrate-deficient glycoprotein syndrome was characterized. Structurally abnormal sugar chains were not found in reversed phase chromatograms of pyridylaminated derivatives from the transferrin of two patients in different families. Electrospray ionization mass spectrometry of the whole transferrin molecules revealed an abnormal species that was smaller than normal tetrasialotransferrin by 2,200 daltons, just the size of the disialylated biantennary sugar chain. These data indicated that the disialotransferrin specifically found in this syndrome is missing either of two N-linked sugar chains, suggesting a metabolic error in the early steps of protein glycosylation.