Co-localization of glycine and calbindin D-28k in the vestibular ganglion of the rat.

Abstract

Bipolar neurons of the vestibular ganglion (VG) are biochemically heterogeneous. The calcium-binding protein calbindin D-28k (Calb) is present only in a subset of particularly large neurons, and the amino acid glycine (Gly) has been immunocytochemically detected in a group of similarly sized cells. The close correspondence in size and number of cells in these two subgroups suggests that the Calb- and Gly-positive populations may be identical. In order to test this hypothesis, we performed direct and indirect double-labeling for Calb and Gly in the VG of the rat. The results confirm the existence of a distinct subpopulation of Calb-immunoreactive neurons, consisting of the largest cells in the VG. In contrast, the vast majority of neurons in the VG display some degree of Gly immunoreactivity, which gradually decreases from intense to almost unlabeled. Direct evidence is provided that the fraction of cells most heavily labeled by Gly antibodies is not identical with the Calb-positive subpopulation. Although some correlation between soma diameter and labeling intensity exists, Gly immunoreactivity is clearly not restricted to large neurons. The findings imply that the functional mechanisms in which Gly is potentially involved may be shared by a large spectrum of primary vestibular afferents with a broad range of physiological properties.