Immunohistochemical localization of a novel acidic calmodulin-binding protein, NAP-22, in the rat brain.

NAP-22 is a neuronal tissue-enriched acidic calmodulin-binding protein with a molecular mass of 22,000 and is recovered in the membrane fraction during biochemical fractionation. We observed the distribution pattern of this protein in the rat brain using an immunohistochemical method by light and electron microscopy. NAP-22 immunoreactivity was detected through the whole brain, and the most dense staining was observed in the forebrain including cerebral cortex, hippocampal formation, olfactory bulb, basal ganglia and thalamus. Immunoreactivity was distributed densely at the neuropil, whereas nerve cells and nerve fibres had little or no reaction. In the brain stem, immunonegative large nerve cell bodies were surrounded by immunopositive varicosities. In the cerebellar cortex, mossy fibre terminals and parallel fibres showed immunoreactivity, whereas Purkinje cells did not. Intracellular distribution was observed in the cerebral and cerebellar cortices. NAP-22 immunoreactivity was noted in the axon terminals, dendritic spines and thin nerve fibres. In these structures, reaction products were associated mainly with synaptic vesicles, pre- and postsynaptic membranes and microtubules. This study demonstrates that the immunoreactivity of NAP-22 is distributed widely in the brain, especially in the synapse, and suggests that this protein is involved in synaptic transmission both in the pre- and postsynaptic region.