The amyloid precursor protein is developmentally regulated and correlated with synaptogenesis.

Metabolism of the amyloid precursor protein (APP) may contribute to the molecular changes observed in Alzheimer's disease, but the function of the protein in the non-pathologic nervous system remains unknown. In vitro studies have suggested that APP can participate in cellular adhesion and may thus contribute to neuronal differentiation in cultured cells. Here we show, in the primary visual pathway of the hamster, that APPs are developmentally regulated proteins rapidly transported to the growing tips of nerve fibers. Transmembrane forms of higher molecular weight (120 and 140 kDa) are preferentially associated with the rapid elongation of axons. Interestingly, another full-length form of 110 kDa and a soluble form of 100 kDa which lacks the C-terminal domain increase at the time of end-arbor formation and synaptogenesis and then decline when mature connections are established, suggesting that target recognition and synaptic contact may result in a signal for APP cleavage in the CNS in vivo.