Immunocytochemical localization of synapsin I in the adrenal medulla of rats.

The localization of synapsin I in the rat adrenal medulla was studied using the light- and electronmicroscopic immunohistochemistry. By light microscopy, many dot-like reaction products for synapsin I were recognized to be distributed throughout the medullary tissue. The immunoelectron microscopy clearly revealed that gold particles for synapsin I accumulated in abundance in the nerve terminals forming synapses with the chromaffin cell, while the particles were not localized in the chromaffin cells at all. In the nerve terminal, the gold particles were localized exclusively in the region occupied by synaptic vesicles except for the region just beneath the presynaptic plasma membrane. The synaptic vesicles were frequently linked with the adjacent ones by filamentous structures implicated in synapsin I. It is concluded morphologically that synapsin I is a highly-specific protein for the genuine neuron, and is not detected even in the chromaffin cell which originates from the neural crest.