Soong H K
Arch Ophthalmol. 1987 Aug;105(8):1129-32. doi: 10.1001/archopht.1987.01060080131043.
Vinculin is a specialized protein with a molecular weight of 130 kilodaltons that is localized to focal regions of cell-to-substrate attachment. It is located precisely at the termini of actin-containing intracytoplasmic stress fibers, which appear to insert into the inner surface of the cell membrane via the vinculin junctions. By double-labeling corneal epithelial cells in tissue culture simultaneously for vinculin and actin, the intimate association of stress fibers and cell-to-substrate adhesion foci was demonstrated. At the leading edge of the migrating epithelial sheet, discrete vinculin patches were numerous in the direction of cell movement, while vinculin was less polarized and often diffusely distributed in the cytoplasm in the less motile cells toward the center of the cell colony. This study shows that corneal epithelial cell migration and spreading during wound healing is characterized by relatively firm substrate attachments at the advancing edge, with the cells behind the edge possibly being pulled forward via cytoskeletal contractile mechanisms.
纽蛋白是一种分子量为130千道尔顿的特殊蛋白质,定位于细胞与底物附着的焦点区域。它精确地位于含肌动蛋白的胞质内应力纤维的末端,这些应力纤维似乎通过纽蛋白连接插入细胞膜的内表面。通过在组织培养中同时对角膜上皮细胞进行纽蛋白和肌动蛋白的双重标记,证明了应力纤维与细胞-底物粘附焦点的密切关联。在迁移上皮片的前沿,离散的纽蛋白斑块在细胞运动方向上大量存在,而在朝向细胞集落中心的运动较少的细胞中,纽蛋白的极化程度较低,且常分散分布在细胞质中。这项研究表明,角膜上皮细胞在伤口愈合过程中的迁移和铺展的特征是在前进边缘有相对牢固的底物附着,边缘后面的细胞可能通过细胞骨架收缩机制被向前拉动。