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• W2067509719 abstract "Since all 5‐HT 1 receptors couple to G i –type G proteins and inhibit adenylyl cyclase, the functional significance of five distinct subtypes of 5‐HT 1 receptors has been unclear. In previous studies we have used transfected cells to demonstrate that 5‐HT 1B receptors can couple more efficiently than 5‐HT 1A receptors to activation of extracellular signal‐regulated kinase (ERK) and to inhibition of adenylyl cyclase. These findings suggested the possibility that individual 5‐HT 1 receptors differentially couple to isoforms of G iα . In the present study we utilized a model system in which pertussis toxin resistant forms of human G iα1 , G iα2 , and G iα3 were used to directly compare the coupling of human 5‐HT 1A , 5‐HT 1B , and 5‐HT 1D receptors to each G iα in transfected human HeLa cells. 5‐HT 1A receptors displayed a preference for G iα1 and G iα2 , relative to G iα3 . Pertussis toxin resistant forms of G iα1 , G iα2 , and G iα3 rescued 73%, 76%, and 44%, respectively, of the ERK activation stimulated by 5‐HT in the absence of pertussis toxin. In contrast, pertussis toxin resistant forms of G iα1 , G iα2 , and G iα3 rescued 32%, 118%, and 35% of 5‐HT 1B receptor‐stimulated activity, respectively, indicating that 5‐HT 1B receptors coupled primarily through G iα2 . A similar preference for G iα2 was found in studies of the 5‐HT 1D receptor, where toxin resistant G iα1 , G iα2 , and G iα3 rescued 30%, 70%, and 40% of activity, respectively. In conclusion, the observed differential coupling of 5‐HT 1 receptors to isoforms of G iα , provides additional evidence for our previous findings that the subtypes of 5‐HT 1 receptors exhibit similar, but distinct, functions. British Journal of Pharmacology (2002) 136 , 1072–1078. doi: 10.1038/sj.bjp.0704809" @default.
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• W2067509719 date "2002-08-01" @default.
• W2067509719 modified "2023-10-17" @default.
• W2067509719 title "Differential coupling of 5‐HT₁ receptors to G proteins of the G_i family" @default.
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• W2067509719 doi "https://doi.org/10.1038/sj.bjp.0704809" @default.
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