Solitary magnocellular neurons in the homozygous Brattleboro rat have vasopressin and glycopeptide immunoreactivity.

A small but distinctive population (about 1 in 600) of magnocellular neurosecretory neurons in homozygous Brattleboro rats are immunoreactive for vasopressin, and a similar number for the carboxy-terminal glycopeptide of the vasopressin prohormone. These solitary cells are found in all animals and in all parts of the magnocellular system, but not in the suprachiasmatic or other hypothalamic nuclei. The majority of the solitary cells do not differ morphologically from the remainder of the magnocellular neurons. The immunoreactivity is markedly denser in the Nissl bodies than in the Golgi region. Serial sections show that the vasopressin and glycopeptide immunoreactive material is co-localized in the same cells, and that these cells are not immunoreactive for oxytocin. A published sequence for the Brattleboro vasopression gene mutation indicates a base-deletion upstream from the glycopeptide-encoding portion, and implies a frameshift that would cause translation of incorrect protein continuing into the poly-A tail of the mRNA. Although this could apply to the majority of the Brattleboro presumptive vasopressin neurons, the co-localization in our solitary cells of material immunoreactive with antibodies to both the amino- and carboxy-terminals of the vasopressin prohormone suggest that in these cases an additional mechanism may be operating.