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• W1977520596 abstract "<b><i>Background/Aims:</i></b> Estrogens are important effectors of reproduction and are critical for upregulating female reproductive behavior or lordosis in females. In addition to the importance of transcriptional regulation of genes by 17β-estradiol-bound estrogen receptors (ER), extranuclear signal transduction cascades such as protein kinase A (PKA) are also important in regulating female sexual receptivity. GPR30 (G-protein coupled receptor 30), also known as GPER1, a putative membrane ER (mER), is a G protein-coupled receptor that binds 17β-estradiol with an affinity that is similar to that possessed by the classical nuclear ER and activates both PKA and extracellular-regulated kinase signaling pathways. The high expression of GPR30 in the ventromedial hypothalamus, a region important for lordosis behavior as well as kinase cascades activated by this receptor, led us to hypothesize that GPR30 may regulate lordosis behavior in female rodents. <b><i>Method:</i></b> In this study, we investigated the ability of G-1, a selective agonist of GPR30, to regulate lordosis in the female mouse by administering this agent prior to progesterone in an estradiol-progesterone priming paradigm prior to testing with stud males. <b><i>Results:</i></b> As expected, 17β-estradiol benzoate (EB), but not sesame oil, increased lordosis behavior in female mice. G-1 also increased lordosis behavior in female mice and decreased the number of rejective responses towards male mice, similar to the effect of EB. The selective GPR30 antagonist G-15 blocked these effects. <b><i>Conclusion:</i></b> This study demonstrates that activation of the mER GPR30 stimulates social behavior in a rodent model in a manner similar to EB." @default.
• W1977520596 created "2016-06-24" @default.
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• W1977520596 date "2014-01-01" @default.
• W1977520596 modified "2023-10-18" @default.
• W1977520596 title "Activation of the GPR30 Receptor Promotes Lordosis in Female Mice" @default.
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• W1977520596 doi "https://doi.org/10.1159/000365574" @default.
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