| Popis: |
Cell-substratum interaction and recognition is essential for cellular adherence and protein synthesis. To understand the mechanisms underlying diseases related to corneal erosion, it is necessary to examine the role integral proteins play in cellular adherence and spreading. In the current study, we used antibodies to evaluate the accumulation of integrin by corneal epithelial cells in tissue culture. We demonstrated that while the protein was incorporated into the cell layer at 6, 24, 48, and 72 hr, a far greater amount was secreted into the media. The total amount of integrin did not change with time, and the level of mRNA did not increase from 24 to 48 hr. During this time period, fibronectin was not detected. Antibodies to the fibronectin-binding receptor inhibited cellular spreading over a period of 18 hr. These results indicate that rabbit corneal epithelial cells do synthesize integrin and that integrin plays a critical role in cellular spreading. |
