Effects of matrix proteins on rabbit corneal epithelial cell adhesion and migration

Extracellular matrix and basement membrane proteins are important in promoting the adhesion and migration of various cell types. Laminin and type IV collagen are found in basement membranes throughout the body while fibronectin is found associated with some basal lamina, in loose connective tissue, and in all body fluids. In the current study fibronectin, laminin, and type IV collagen were assessed to determine their effect on the adhesion and migration of dissociated rabbit epithelial cells. In a kinetic analysis fibronectin was found to be the most effective of the three proteins in promoting cell adhesion. Cell adhesion promoted by fibronectin could be modulated by an arg-gly-asp-ser (RGDS) peptide, a sequence which is found within the fibronectin molecule. In dose-response experiments type IV collagen effectively promoted cell adhesion at concentrations as low as 4 x 10(-16) moles per well in 96 well tissue culture plates. Type IV collagen was the most effective protein tested in promoting chemotactic and haptotactic migration. These proteins, proteolytic fragments, and peptides derived from them, could prove useful as therapeutic agents, modifying corneal epithelial phenotypic behavior in wound healing, corneal transplantation and following ocular surgery or trauma.