The adhesive glycoprotein laminin is an agglutinin
The adhesive glycoprotein laminin is an agglutinin
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粘附糖蛋白层粘连蛋白是一种凝集素
DOI：
10.1002/jcp.1041140302
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发表时间：
1983
影响因子：
5.6
通讯作者：
K. Yamada
中科院分区：
文献类型：
--
作者：
D. Kennedy;D. H. Rohrbach;G. Martin;T. Momoi;K. Yamada
糖蛋白层粘连蛋白似乎在各种上皮细胞与基底膜的附着中发挥作用。我们研究了是否可以在一个简单的单组分模型系统中分析其推定的细胞粘附活性-红细胞凝集。层粘连蛋白是醛固定绵羊和人红细胞的强效凝集素，在标准血凝试验中的半最大凝集为0.8 μg/ml。这种血凝活性的抑制剂包括神经节苷脂和某些带电磷脂。分子谱与粘附糖蛋白纤连蛋白的血凝活性抑制剂相似但不相同。层粘连蛋白在其他三种纤连蛋白生物活性测定中的生物活性要低得多，所述测定涉及组织培养基质上的细胞铺展、成纤维细胞与I型胶原的附着以及转化成纤维细胞的正常形态的恢复。因此，粘附糖蛋白层粘连蛋白和纤连蛋白在几个特定的粘附试验中的生物活性显着不同;然而，它们在与肝素、胶原和细胞表面的结合以及它们的凝集素活性方面彼此相似。
The glycoprotein laminin appears to function in the attachment of various epithelial cells to basement membranes. We examined whether its putative cell‐adhesive activity could be analyzed in a simple, one‐component model system—the agglutination of erythrocytes. Laminin is a potent agglutinin of aldehyde‐fixed sheep and human erythrocytes, with half‐maximal agglutination of 0.8 μg/ml in a standard hemagglutination assay. Inhibitors of this hemagglutinating activity include gangliosides and certain charged phospholipids. The spectrum of molecules is similar but not identical to inhibitors of the hemagglutinating activity of the adhesive glycoprotein fibronectin. Laminin is much less biologically active in three other assays for fibronectin biological activity involving cell spreading on tissue culture substrates, attachment of fibroblastic cells to type I collagen, and restoration of normal morphology to transformed fibroblasts. The adhesive glycoproteins laminin and fibronectin therefore differ markedly in biological activities in several specific adhesion assays; however, they resemble one another in binding to heparin, collagen, and cell surfaces and in their agglutinin activity.