Primary neuronal cell cultures from P6 mice were investigated in order
to study amyloid protein precursor (APP) gene expression in different
iating neurons. Cerebellar granule cells which strongly express APP 69
5 allowed the identification of three distinct isoforms of neuronal AP
P 695. The high-molecular-weight form of APP 695 is sialylated. The ex
pression pattern of neuronal APP 695 changes during in vitro different
iation. Sialylated forms become more abundant upon longer cultivation
time. The secreted forms of sialylated, neuronal APP 695 are shown to
comigrate with APP isolated from cerebrospinal fluid. We suggest that
the different sialylation states of APP 695 may reflect the modulation
of cell-cell and cell-substrate interactions during in vitro differen
tiation and regeneration.