The effects of functional odour deprivation on three different proteins associated with the membrane of the synaptic vesicle were examined in the rat olfactory bulb. Six weeks after neonatal unilateral nostril closure, Rab3a, a ras-like GTPase, was down-regulated in the odour-deprived bulb in the same manner as tyrosine hydroxylase. In contrast, synaptophysin, a protein of the channel family, and SV2, a putative transporter protein, were not altered. These results suggest that afferent activity is a factor controlling the level of some, but not all, proteins associated with presynaptic vesicles.
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