Evidence for a high density of secretoneurin-like immunoreactivity in the extended amygdala of the rat.

Secretoneurin is a novel 33-amino-acid neuropeptide produced by endoproteolytic processing from secretogranin II, which is a member of the chromogranin/secretogranin family. In this immunocytochemical study, we compared the distribution pattern of secretoneurin immunoreactivity with that of tyrosine hydroxylase, calbindin, substance P, and Leu-enkephalin in adjacent sections of rat forebrain. Secretoneurin appeared mainly in varicosities and fibers. Only a few cell bodies were stained. In the nucleus accumbens, a partial overlap of secretoneurin-immunoreactive patches with enkephalin-immunopositive areas was found. Secretoneurin displayed low to moderate levels of immunoreaction in calbindin-rich as well as in calbindin-immunonegative areas of the caudate-putamen. In the globus pallidus, entopeduncular nucleus, and substantia nigra, secretoneurin immunoreactivity was oriented ventromedially preferentially in woolly fibers. The dense immunostaining in the medial nucleus accumbens was directly continuous with dense secretoneurin immunoreactivity in the bed nucleus of the stria terminalis. Two strongly secretoneurin-immunopositive bands, one in the sublenticular portion and a smaller one along the posterior limb of the anterior commissure, interconnected the highly secretoneurin-immunopositive centromedial amygdala with the bed nucleus of the stria terminalis. Thus, the distribution pattern of secretoneurin immunoreactivity provides a marker of the extended amygdala that forms a continuum between the centromedial amygdala and the bed nucleus of the stria terminalis.