Chen W T, Chen J M, Parsons S J, Parsons J T
Nature. 1985;316(6024):156-8. doi: 10.1038/316156a0.
Local degradation of extracellular fibronectin, a major extracellular adhesive protein, is believed to play an important part in the migration of cells through the extracellular matrix during tumour invasion, morphogenetic movement and trophoblast implantation. Fibronectin is lost from the cell surface after transformation with Rous sarcoma virus (RSV). By using fluorescent and radiolabelled probes covalently coupled to the surface of substrata, we have recently identified a proteolytic activity that is expressed in RSV-transformed cells and is involved in the local degradation of fibronectin at cell-substratum contact sites. Here, we extend the relevance of these findings and gain some insight into the cellular functions of pp60src, the transforming gene product of RSV. We show that newly expressed viral pp60src is localized at the cytoplasmic surface of the cell membrane, corresponding to the cell contact sites where degradation of extracellular fibronectin occurs.
细胞外纤连蛋白是一种主要的细胞外黏附蛋白,其在肿瘤侵袭、形态发生运动和滋养层植入过程中,细胞通过细胞外基质迁移时的局部降解被认为起着重要作用。用劳氏肉瘤病毒(RSV)转化后,纤连蛋白会从细胞表面丢失。通过使用与基质表面共价偶联的荧光和放射性标记探针,我们最近鉴定出一种蛋白水解活性,该活性在RSV转化的细胞中表达,并参与细胞-基质接触部位纤连蛋白的局部降解。在此,我们扩展了这些发现的相关性,并对RSV的转化基因产物pp60src的细胞功能有了一些了解。我们表明,新表达的病毒pp60src定位于细胞膜的细胞质表面,对应于细胞外纤连蛋白发生降解的细胞接触部位。