Abstract
Although the enzyme defects in mucopolysaccharidoses are corrected with crude enzyme preparations from normal cells, those in sphingolipidoses are not. We tested the effect of several lectins on the uptake of β-hexosaminidase by Sandhoff fibroblasts and of β-galactosidase by fibroblasts from type 1 GM1-gangliosidosis. The cells were incubated in phosphate-buffered saline in 2 cm2 limbro wells for 16 hrs at 37° with various lectins and the specific purified human placental enzyme. Of the lectins tested Concanavalin A (Con A) was most effective. After incubation, the previously deficient cells had acquired enzyme activity. It was not removed by haptene treatment, suggesting an intra-cellular location. For example, when 2 × 105 GM1 fibroblasts were treated with Con A followed by β-galactosidase, 10% of the enzyme remaining after incubation was associated with the cells. After treatment with mannose, 85% of this activity remained with the cells. In the absence of Con A only 0.5% of the enzyme was cell-associated. When the cells were incubated at 4°C, there was an increase in enzyme activity similar to that in the 37° cells but almost all activity was removed by the haptene. This technique should prove useful in manipulating the enzymatic complement of deficient cells.
Supported by a grant from the Medical Research Council of Canada.
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Juliano, R., Moore, M., Gravel, R. et al. LECTIN-MEDIATED UPTAKE OF LYSOSOMAL HYDROLASES BY HUMAN FIBROBLASTS. Pediatr Res 11, 458 (1977). https://doi.org/10.1203/00006450-197704000-00528
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DOI: https://doi.org/10.1203/00006450-197704000-00528