The regulation and function of two forms of the amyloid beta protein precursor (ABPP) that are released into the growth-conditioned medium of the PC12 nerve cell line were examined. Nerve growth factor increases the release of the form of ABPP without the protease-inhibitor domain relative to the protein containing the protease inhibitor and increases the overall rate of ABPP secretion 2-fold. In contrast, fibroblast growth factor increases the rate of ABPP secretion approximately 7-fold. Both forms of the secreted ABPP molecule are, in turn, able to stimulate adhesion of PC12 cells to substrata to which they are adsorbed about 10-fold more efficiently on a molar basis than Iaminin.