Abstract
We transfected rat pheochromocytoma (PC12) cells with a cDNA encoding chicken integrin β1 subunit. The chicken integrin β1 subunit produced in stable transfectants associated with two major α subunits of rat integrins to form interspecific chimeric receptors. These receptors mediated cell spreading and initial neurite outgrowth on laminin as did corresponding endogenous integrins, although they were slightly less effective in inducing cell adhesion to laminin. These results indicate that chicken integrin β1 may functionally substitute for β1 subunit of rat integrins in PC12 cells. Apparently, the structure of the integrin β1 subunit is highly conserved in the evolution of these species.
