Location of profilin at presynaptic sites in the cerebellar cortex; implication for the regulation of the actin-polymerization state during axonal elongation and synaptogenesis.

Profilin is a 15 kDa protein that binds actin monomers and inhibits their polymerization in vitro. The actin-profilin complex can be rapidly dissociated in vitro by phosphatidylinositol-4,5-bis-phosphate, providing a mechanism for regulating actin assembly-disassembly cycles during cell motile events. We have used a polyclonal antibody to calf spleen profilin to analyse the developmental expression and cellular distribution of profilin in the rat cerebellum and cultured cortical neurons. Immature neurons contain large amount of profilin both in vivo and in vitro. Immunofluorescence showed it to be present in developing neurites and growth cones but not in the filopodia of cortical neurons in culture. Profilin immunoreactivity was intense in the parallel fibres, the granule cell axons of the cerebellar cortex, at the time when they are elongating. Purkinje cell dendrites were not labelled. Profilin immunostaining was present in presynaptic varicosities, but not in dendritic spines within the molecular layer of juvenile and adult rats. The profilin concentration was higher in synaptosomes than in the total cerebellum during the second and third postnatal weeks, a period of intense synaptogenesis. Thus, profilin may help regulate actin polymerization and depolymerization during axonal elongation and synaptogenesis. Its restriction to the presynaptic site in the adult suggests that it may also be involved in the regulation of the release of synaptic vesicles.