Abstract
The lectin affinities of β-N-acetyl-d-hexosaminidase (E.C.3.2.1.52) from an acute lymphoblastic leukaemic cell-line (CCRF/CEM), a non-malignant lymphoblastic cell-line (SM1) and normal human fibroblasts were studied for both mature and precursor forms of the enzyme. Four immobilised lectins concanavalin A-Sepharose wheat germ agglutinin-Agarose,Ricinus communis agglutinin I-Agarose,Phaseolus vulgaris erythroagglutinin-Agarose and a column of serotonin-Sepharose were used. The activities of β-hexosaminidase from fibroblasts and SM1 cells generally behaved similarly while the CCRF/CEM enzyme exhibited different binding patterns. Differences were also noted between precursor and mature enzyme from each cell type consistent with changes in glycosylation between the precursor form and the mature form appearing in the lysosome. These results suggest that changes in the glycosylation of β-hexosaminidase, and possibly other lysosomal enzymes, may be associated with malignancy.
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Abbreviations
- Con A:
-
concanavalin A-Sepharose
- RCA-I:
-
Ricinus communis agglutinin I-Agarose
- WGA:
-
wheat germ agglutinin-Agarose
- PHA-E:
-
Phaseolus vulgaris erythroagglutinin-Agarose
- SER:
-
serotonin-Sepharose: non-T
- non-B ALL:
-
non-T, non-B cell acute lyphoblastic leukaemia
- 4-MU-GLcNAc:
-
4-methylumbelliferyl 2-acetamido-2-deoxy-β-D-glucopyranoside
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Moss, S.E., Besley, G.T.N. Evidence from lectin-binding studies for abnormal glycosylation ofβ-hexosaminidase in the leukaemic cell-line CCRF/CEM. Glycoconjugate J 2, 267–277 (1985). https://doi.org/10.1007/BF01049273
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DOI: https://doi.org/10.1007/BF01049273