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β1整合素糖基化改变,与对纤连蛋白和层粘连蛋白的黏附性降低相关。

Altered glycosylation of beta 1 integrins associated with reduced adhesiveness to fibronectin and laminin.

作者信息

Kawano T, Takasaki S, Tao T W, Kobata A

机构信息

Department of Biochemistry, University of Tokyo, Japan.

出版信息

Int J Cancer. 1993 Jan 2;53(1):91-6. doi: 10.1002/ijc.2910530118.

DOI:10.1002/ijc.2910530118
PMID:7677933
Abstract

The carbohydrate structures of the beta 1 integrins obtained from a mouse metastatic melanoma B16 F1 and its weakly metastatic wheat-germ agglutinin-resistant mutant Wa4-b1 were studied comparatively. The results indicated that the integrins from both cells contain high mannose-type and bi-, tri- and tetra-antennary complex-type sugar chains. No significant difference was found in the outer chain branching between both integrins, but sialylation of the sugar chains of the mutant's integrin was markedly decreased and almost all the outer chain moieties of tri- and tetra-antennary oligosaccharides of the mutant's integrin were fucosylated, resulting in the formation of X-antigenic determinants, Gal beta 1-->4 (Fuc alpha 1-->3) GlcNAc. In contrast, the integrin from parental cell contained no X-antigenic determinant. These structural differences found in the integrin are thought to account for the reduction in the metastatic potential of the mutant which also shows reduced adhesion to fibronectin and laminin as compared with the parental cell.

摘要

对从小鼠转移性黑色素瘤B16 F1及其低转移性抗麦芽凝集素突变体Wa4-b1中获得的β1整合素的碳水化合物结构进行了比较研究。结果表明,两种细胞的整合素均含有高甘露糖型以及双天线、三天线和四天线复合型糖链。两种整合素在外链分支上未发现显著差异,但突变体整合素糖链的唾液酸化明显减少,且突变体整合素三天线和四天线寡糖的几乎所有外链部分都被岩藻糖基化,导致形成X抗原决定簇,即Galβ1→4(Fucα1→3)GlcNAc。相比之下,亲本细胞的整合素不含X抗原决定簇。整合素中发现的这些结构差异被认为是突变体转移潜能降低的原因,与亲本细胞相比,突变体对纤连蛋白和层粘连蛋白的粘附也有所降低。

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