刀豆球蛋白A介导的法布里病成纤维细胞对纯化的α-半乳糖苷酶A的结合与摄取。

ConA-mediated binding and uptake of purified alpha-galactosidase A in Fabry fibroblasts.

作者信息

Hasholt L, Sørensen S A

出版信息

Exp Cell Res. 1983 Oct 15;148(2):405-11. doi: 10.1016/0014-4827(83)90162-3.

Abstract

In most human tissues there are at least two different alpha-galactosidases, A and B. The former is deficient in patients hemizygous for Fabry disease. We have isolated it from human placenta and found that it was labile even at culture conditions, but was stabilized after binding to concanavalin A (conA). The alpha-galactosidase activity was markedly increased in Fabry fibroblasts when these were treated with conA and exposed to alpha-galA at 37 degrees C. The maximum activity was obtained after 1/2-2 h of incubation and was maintained for at least 4 h. The binding and uptake of conA into Fabry cells was followed by microscopical studies of fluorescein-labelled conA. We assume that alpha-galA is taken up by endocytosis of the enzyme-conA complex.

摘要

在大多数人体组织中，至少存在两种不同的α-半乳糖苷酶，即A和B。前者在法布里病半合子患者中缺乏。我们已从人胎盘中分离出该酶，发现其即使在培养条件下也不稳定，但与伴刀豆球蛋白A（伴刀豆凝集素A，conA）结合后会变得稳定。当法布里成纤维细胞用conA处理并在37℃下暴露于α-半乳糖苷酶A（α-galA）时，α-半乳糖苷酶活性显著增加。孵育1/2 - 2小时后可获得最大活性，并至少维持4小时。通过对荧光素标记的conA进行显微镜研究，追踪conA与法布里细胞的结合和摄取情况。我们推测α-galA是通过酶 - conA复合物的内吞作用被摄取的。