Huntington's-chorea fibroblasts. Cellular protein glycosylation.
Five cell cultures of Huntington's-chorea fibroblasts exhibit greater than normal protein and lipid glycosylation when labelled with [U-14C]glucosamine. Oligosaccharide--polypeptide chains from all molecular-weight ranges are labelled differentially on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. This difference in protein glycosylation is not accompanied by any apparent difference in general cellular protein synthesis or by a differential rate of glucosamine uptake or decreased degradation of [14C]glycosylated macromolecules. Additionally [U-14C]glucosamine exclusively labels hexosamines and sialic acid of cellular macromolecules.
D000328:Adult; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D005944:Glucosamine / Q000378:metabolism; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D046911:Macromolecular Substances; D008875:Middle Aged; D011506:Proteins / Q000378:metabolism*
D046911:Macromolecular Substances; D011506:Proteins; D007930:Leucine; D005944:Glucosamine