The nature of lysosomal enzyme glycosylation in ALL: relevance to abnormal beta-hexosaminidase expression.
The glycosylation of beta-hexosaminidase was investigated in the transformed cell-line, CCRF/CEM, derived from a human acute lymphoblastic leukaemia, and comparisons were made with enzyme from normal human skin fibroblasts. A series of studies including neuraminidase sensitivity, lectin chromatography, Biogel P4 chromatography of [3H]-mannose-labelled glycopeptides and endoglycosidase susceptibility, provided clear evidence that in CCRF/CEM cells, beta-hexosaminidase was abnormally glycosylated. The results indicate that leukemia-associated changes in beta-hexosaminidase expression are probably due to increased sialylation of highly-branched complex oligosaccharides.
Moss
S E
SE
Department of Pathology, Royal Hospital for Sick Children, Edinburgh, Scotland.
Besley
G T
GT
D000118:Acetylglucosaminidase / Q000494:pharmacology; D002461:Cell Line, Transformed; D002850:Chromatography, Gel; D006020:Glycopeptides / Q000302:isolation & purification; D006031:Glycosylation; D006801:Humans; D007945:Leukemia, Lymphoid / Q000201:enzymology* / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D012685:Sepharose / Q000031:analogs & derivatives; D001619:beta-N-Acetylhexosaminidases / Q000302:isolation & purification / Q000378:metabolism*
D006020:Glycopeptides; C028326:concanavalin A-sepharose; D012685:Sepharose; D000118:Acetylglucosaminidase; D001619:beta-N-Acetylhexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase