TISSUE FIBRONECTIN IS AN ENDOGENOUS LIGAND FOR GALECTIN-1
TISSUE FIBRONECTIN IS AN ENDOGENOUS LIGAND FOR GALECTIN-1
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DOI：
10.1093/glycob/5.2.255
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发表时间：
1995-03-01
期刊：
影响因子：
4.3
通讯作者：
TITANI, K
中科院分区：
文献类型：
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作者：
OZEKI, Y;MATSUI, T;TITANI, K
14 K β-半乳糖苷结合凝集素（galectin-1）存在于多种动物组织中。为了寻找内源性配体，我们对人胎盘中galectin-1结合蛋白进行了研究。两个主要的蛋白质洗脱与100 mM乳糖从柱结合的馏分显示表观分子量为220和180 kDa的SDS-PAGE在还原条件下。用单克隆抗体进行的Western印迹分析表明，这些蛋白分别是纤连蛋白和层粘连蛋白。大多数胎盘和羊膜纤连蛋白强烈结合的列，而几乎所有的血浆纤连蛋白通过列。半乳糖凝集素-1、纤连蛋白和层粘连蛋白在胎盘组织的细胞外基质中共定位。在细胞附着测定中，即使在GRGDS肽存在下，如果半乳糖凝集素-1也存在，横纹肉瘤细胞也粘附到用胎盘纤连蛋白包被的板上。半乳糖凝集素-1的这种粘附作用被乳糖抑制。这些结果表明，组织纤连蛋白以及层粘连蛋白充当半乳糖凝集素-1的内源性配体，表明半乳糖凝集素-1可能在细胞外基质的组装中起作用。或基于凝集素-细胞外基质相互作用控制细胞粘附。
A 14K beta-galactoside-binding lectin (galectin-1) is present in many animal tissues, In a search for endogenous ligands, we surveyed galectin-1-binding proteins in human placenta, Extract of human placenta with 2 M urea was applied to a Sepharose 4B column conjugated with galectin-1 purified from frog (Rana catesbeiana) eggs. Two major proteins eluted with 100 mM lactose from the column-bound fraction showed apparent molecular masses of 220 and 180 kDa on SDS-PAGE under reducing conditions. Western blotting analysis using monoclonal antibodies indicated that these proteins were fibronectin and laminin, respectively. Most placental and amniotic fibronectins bound strongly to the column, whereas almost all plasma fibronectin passed through the column. The galectin-1, fibronectin and laminin were immunohistochemically shown to be co-localized in the extracellular matrix of placental tissue. In a cell attachment assay, rhabdosarcoma cells adhered to a plate coated with placental fibronectin, even in the presence of GRGDS peptide, if galectin-1 were also present, This adhesive effect of galectin-1 was inhibited by lactose, These results indicate that tissue fibronectin, as well as laminin, serve as endogenous ligands for galectin-1, suggesting that galectin-1 may play a role in assembly of the extracellular matrix, or in the control of cell adhesion based on lectin-extracellular matrix interaction.