Chammas R, Veiga S S, Travassos L R, Brentani R R
Ludwig Institute for Cancer Research, São Paulo, Brazil.
Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1795-9. doi: 10.1073/pnas.90.5.1795.
Laminin interaction with gp120/140, a B16-F10 laminin-binding protein immunologically related to alpha 6 beta 1 integrin, has been shown to be dependent on oligosaccharides from both ligand and receptor. Lectin analysis of gp120/140 led to the conclusion that this integrin is a sialoglycoprotein bearing mainly complex antennary structures. By means of exoglycosidase treatment, it was possible to identify alpha-galactosyl residues on the integrin alpha chain as the laminin-binding determinants. These residues are involved in cell adhesion to laminin. On the other hand, beta-chain complex antennary structures, whose synthesis could be inhibited by swainsonine, were associated with cell spreading rather than cell adhesion. Thus, it was possible to modulate integrin-mediated cell adhesion and spreading through changes in the glycosylation state of integrin alpha and beta chains.
层粘连蛋白与gp120/140的相互作用已被证明依赖于来自配体和受体的寡糖。gp120/140是一种与α6β1整合素免疫相关的B16-F10层粘连蛋白结合蛋白。对gp120/140的凝集素分析得出结论，这种整合素是一种主要带有复杂天线状结构的唾液糖蛋白。通过外切糖苷酶处理，有可能确定整合素α链上的α-半乳糖基残基为层粘连蛋白结合决定簇。这些残基参与细胞与层粘连蛋白的粘附。另一方面，其合成可被苦马豆素抑制的β链复杂天线状结构与细胞铺展而非细胞粘附相关。因此，通过改变整合素α链和β链的糖基化状态，可以调节整合素介导的细胞粘附和铺展。
