Abstract
The mouse 5-HT 2C receptor and its third and fourth (C-terminal) cytoplasmic domain have been expressed as fusion proteins in bacteria. After purification antisera were generated against the fusion proteins. Characterization by immunoblotting using eukaryotic cells expressing the 5-HT 2C and 5-HT 2A receptors showed that high titer antibodies could be obtained only against the third and fourth cytoplasmic domain but not the entire receptor. Affinity purified antibodies were used to study the location of 5-HT 2C receptors in rat and human brain sections. This distribution was compared with the location of 5-HT 2C receptor binding sites as determined by [ 3H]mesulergine, a 5-HT 2C receptor radioligand. The antibodies recognized sites in the rat choroid plexus, hippocampus, cerebral cortex, striatum and substantia nigra with a similar distribution as the 5-HT 2C binding sites. One antiserum directed against the 5-HT 2C receptor C-terminus crossreacted with the human receptor protein in immunoblots. In human brain sections it labelled sites including cerebral cortex, substantia nigra and cerebellum. Our results demonstrate that the antibodies are suitable to identify 5-HT 2C receptors in rat and human brain. They visualize a protein distribution which correlates well with the location of the 5-HT 2C receptor binding sites as would be expected if affinity states do not influence the binding pattern.
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