CHANGES IN INTEGRIN RECEPTORS ON ONCOGENICALLY TRANSFORMED-CELLS
CHANGES IN INTEGRIN RECEPTORS ON ONCOGENICALLY TRANSFORMED-CELLS
复制标题
DOI：
10.1016/0092-8674(89)90902-1
复制
发表时间：
1989-01-27
期刊：
影响因子：
64.5
通讯作者：
HYNES, RO
中科院分区：
文献类型：
--
作者：
PLANTEFABER, LC;HYNES, RO
致癌转化的细胞表现为富含纤维连接蛋白的细胞外基质的组装减少，与纤维连接蛋白的黏附能力减弱。这些表型改变的分子基础还不完全清楚。我们在这里报告了包括两个纤维连接蛋白受体在内的整合素在啮齿动物细胞致癌转化中的光谱变化。Rous肉瘤病毒或编码ras癌基因的小鼠肉瘤病毒对RAT1、NRK和Nil8细胞的转化导致整合素α5β1水平降低，整合素α5β1是一种明确定义的纤维连接蛋白受体，以及其他两种整合素受体。相反，另一种受体α3β1，是纤维连接蛋白、层粘连蛋白和胶原的多特异性受体，被转化的细胞保留。这些结果为早期关于细胞外基质蛋白与肿瘤细胞表面相互作用的结果提供了解释，并为进一步了解恶性肿瘤细胞改变的黏附和迁移行为提供了线索。
Oncogenically transformed cells show reduced assembly of fibronectin-rich extracellular matrixes and diminished ability to adhere to fibronectin. The molecular bases of these phenotypic alterations are not fully understood. We report here alterations in the spectrum of integrins, including two fibronectin receptors, on oncogenic transformation of rodent cells. Transformation of rat1, NRK, and Nil8 cells by Rous sarcoma virus or by murine sarcoma viruses encoding ras oncogenes leads to reductions in the level of integrin .alpha.5.beta.1, which is a well-defined fibronectin receptor, and of two other integrin receptors. In contrast, another receptor, .alpha.3.beta.1, which is a polyspecific receptor for fibronectin, laminin, and collagen, is retained by transformed cells. These results provide explanations for earlier results concerning the interactions of extracellular matrix proteins with the surfaces of tumor cells and offer leads to further understanding of the altered adhesive and migratory behavior of malignant cells.