Involvement of gangliosides and glycoprotein fibronectin receptors in cellular adhesion to fibronectin.
Involvement of gangliosides and glycoprotein fibronectin receptors in cellular adhesion to fibronectin.
复制标题
神经节苷脂和糖蛋白纤连蛋白受体参与细胞粘附纤连蛋白。
DOI:
10.1016/0014-4827(88)90027-4
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发表时间:
1988
影响因子:
3.7
通讯作者:
Stallcup,WB
中科院分区:
文献类型:
--
作者:
Stallcup,WB
We have used a rat neural cell line, B65, to investigate the relative contributions of gangliosides and glycoprotein receptors in adhesion to fibronectin. Monoclonal antibodies against two neuroectoderm-associated gangliosides, D1.1 and GD3, inhibit the rate of B65 attachment to fibronectin, suggesting that these gangliosides are involved in the adhesion process. Adhesion to fibronectin is not affected by a third monoclonal antibody against a separate, unidentified cell-surface component of B65 cells. Furthermore, B65 cells lacking D1.1 adhere to fibronectin at a slower rate than B65 cells that express D1.1. The involvement of glycoprotein receptors in adhesion is demonstrated by the ability of antibodies against human fibronectin receptor to inhibit B65 attachment to fibronectin. In addition, adhesion is blocked by a hexapeptide containing the ArgGlyAsp fibronectin sequence which is necessary for binding to the receptor. Trypsin treatment of B65 cells in the absence of divalent cations results in proteolysis of the fibronectin receptor with an accompanying loss of ability of the cells to attach to fibronectin. D1.1 and GD3expression is not affected by this trypsinization, indicating that the gangliosides alone are incapable of mediating attachment. The glycoprotein receptors must be primarily responsible for adhesion to fibronectin with the gangliosides playing a secondary role as enhancers or modulators.