The nature of lysosomal enzyme glycosylation in ALL: relevance to abnormal beta-hexosaminidase expression.

Abstract:

: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.

journal_name

Leuk Res

journal_title

Leukemia research

authors

Moss SE,Besley GT

doi

10.1016/0145-2126(88)90146-4

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

267-75

issue

3

eissn

0145-2126

issn

1873-5835

journal_volume

12

pub_type

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