Abstract
The serotonin 2c (5-HT 2C) receptor mediates its cellular effects by interacting with heterotrimeric guanine nucleotide binding proteins (G proteins). To characterize which G proteins are involved in functional coupling to the receptor, a mouse 5-HT 2C receptor was expressed in Xenopus oocytes, and antisense oligonucleotides complementary to the mRNA sequence of the endogenous Xenopus G protein α subunits were used to inhibit G protein synthesis. Antisense oligonucleotide against the Xenopus G o α subunit inhibited the 5-HT 2C receptor function, and coexpression of a rat G o α subunit reversed the inhibition by the anti- Xenopus G o oligonucleotide. Furthermore, antisense oligonucleotides against both the G o and G il α subunits inhibited the electrophysiologic response induced by stimulation of the 5-HT 2C receptor. These data suggest that both G o and G il are involved in functional coupling of the 5-HT 2C receptor to phospholipase C in Xenopus oocytes.
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