Concanavalin A promotes the uptake of lysosomal hydrolases by human fibroblasts.
Biochim Biophys Acta, 1978/11/02;513(2):285-91.
Juliano RL, Moore MR, Callahan JW, Lowden JA
PMID: 102347
Abstract
Human placental hexosaminidase B and beta-galactosidase are taken up very poorly by human fibroblasts in culture. However, if fibroblasts manifesting genetically determined deficiencies of these lysosomal hydrolases are first treated with concanavalin A, then enzyme uptake is markedly increased. Enzyme activity which becomes associated with concanavalin A-treated fibroblasts maintained at 4 degrees C can be greatly removed by treatment with haptene sugar, while enzyme activity which becomes associated with cells maintained at 37 degrees C is refractory to haptens treatment. These results are interpreted as an initial binding of enzyme to concanvalin A molecules located at the cell surface, followed by an active cellular process leading to internalization of the lectin-enzyme complexes.
MeSH terms
Biological Transport, Active; Cell Survival; Cells, Cultured; Concanavalin A; Fibroblasts; Galactosidases; Glycoproteins; Hexosaminidases; Humans; Lysosomes; Stimulation, Chemical; beta-Galactosidase
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