title: Enzyme replacement treatment for Tay-Sachs disease brain cells in culture utilizing concanavalin A-mediated hexosaminidase A uptake: biochemical and morphological evidence of GM2 mobilization.
abstract: When Concanavalin A (Con A) is bound to the cell membrane, it functions as an artificial enzyme receptor, mediating the binding and intracellular incorporation of significant amounts of exogenous hexosaminidase A (Hex A) into Tay-Sachs disease (TSD) glia cells. The treated cells retained almost 50% of incorporated Hex A activity after 3 days incubation in Hex A free medium. Hex A was released from Con A within the cell and was available as free enzyme. Biochemical analysis of gangliosides in Con A and Hex A treated cells depicted a greater than 50% reduction in stored GM2 ganglioside and a fourfold reduction in GM2 label (14C) when compared to controls. Ultrastructural evidence of GM2 breakdown is presented which supports the biochemical and labeling studies.
mesh_terms: D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D003208:Concanavalin A / Q000494:pharmacology*; D005678:G(M2) Ganglioside / Q000378:metabolism; D006596:Hexosaminidases; D006801:Humans; D009457:Neuroglia / Q000378:metabolism; D011485:Protein Binding; D013661:Tay-Sachs Disease / Q000201:enzymology*
chemical_list: D003208:Concanavalin A; D005678:G(M2) Ganglioside; D006596:Hexosaminidases