Brooks S E, Hoffman L M, Adachi M, Amsterdam D, Schneck L
Acta Neuropathol. 1980;50(1):9-17. doi: 10.1007/BF00688529.
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.
当伴刀豆球蛋白A（Con A）与细胞膜结合时，它作为一种人工酶受体发挥作用，介导大量外源性己糖胺酶A（Hex A）与泰-萨克斯病（TSD）神经胶质细胞的结合并使其进入细胞内。在无Hex A的培养基中孵育3天后，经处理的细胞保留了近50%的掺入Hex A活性。Hex A在细胞内从Con A上释放出来，成为游离酶。对Con A和Hex A处理的细胞中神经节苷脂的生化分析表明，与对照组相比，储存的GM2神经节苷脂减少了50%以上，GM2标记（14C）减少了四倍。本文提供了GM2分解的超微结构证据，支持了生化和标记研究。
