Huntington's-chorea fibroblasts. Cellular protein glycosylation
- 15 September 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 190 (3) , 711-719
- https://doi.org/10.1042/bj1900711
Abstract
Cell cultures (5) of Huntington''s chorea human skin fibroblasts exhibit greater than normal protein and lipid glycosylation when labeled with [U-14C]glucosamine. Oligosaccharide-polypeptide chains from all MW ranges are labeled differentially on sodium dodecyl sulfate/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.This publication has 19 references indexed in Scilit:
- Glycoprotein synthesis in a temperature‐sensitive Chinese hamster cell cycle mutantJournal of Cellular Physiology, 1977
- Neurobiology and pharmacology of Huntington's diseaseLife Sciences, 1977
- The sialic acids. XVIII. Subcellular distribution of seven glycosyltransferases in embryonic chicken brainJournal of Biological Chemistry, 1975
- HUNTINGTON'S CHOREABrain, 1974
- Transport and metabolism of glucosamine by cultured Novikoff rat hepatoma cells and effects on nucleotide pools.1973
- Huntington's ChoreaNew England Journal of Medicine, 1973
- Properties of Some Glycosyltransferases in Embryonic Chicken BrainJournal of Biological Chemistry, 1970
- The Effect of d-Glucosamine on the Adenine and Uridine Nucleotides of Sarcoma 180 Ascites Tumor CellsJournal of Biological Chemistry, 1969
- Cellular membranes: The biosynthesis of glycoprotein and glycolipid in HeLa cell membranesArchives of Biochemistry and Biophysics, 1969
- The defect in Hurler's and Hunter's syndromes: faulty degradation of mucopolysaccharide.Proceedings of the National Academy of Sciences, 1968