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5-HT1A receptor-mediated G protein activation assessed by [35S]GTPgammaS binding in rat cerebral cortex.

Abstract：

:To date, 5-hydroxytryptamine1A (5-HT1A) receptor-mediated functional assays (adenylyl cyclase inhibition, high-affinity GTPase activity and [35S]guanosine-5'-O-(gamma-thio)-triphosphate ([35S]GTPgammaS) binding) have been performed mainly in hippocampal membranes. In the current study, 5-HT-stimulated G protein activation assays were carried out in rat cerebral cortical membranes. High-affinity GTPase activity was stimulated by 5-HT, but not by 8-hydroxy-2-(di-n-propylamino)tetralin (8-OH-DPAT). By contrast, 5-HT- and 8-OH-DPAT-stimulated [35S]GTPgammaS binding displayed sufficient dynamic range enough to warrant further pharmacological analysis. Under standard conditions, which were determined precisely in terms of the concentrations of GDP, MgCl2 and NaCl, the profile of 5-HT-stimulated [35S]GTPgammaS binding investigated using a series of 5-HT receptor agonists and antagonists clearly indicated the involvement of the 5-HT1A receptor subtype. There appeared to be no evidence supporting the presence of regional heterogeneity in coupling efficiency between 5-HT1A and G proteins in the hippocampus or cortex. This method is a useful tool for investigating functional coupling between postsynaptic 5-HT1A receptors and G proteins in cerebral cortical membranes.

journal_name

Eur J Pharmacol

journal_title

European journal of pharmacology

authors

Odagaki Y,Toyoshima R

doi

10.1016/j.ejphar.2005.07.018

keywords:

subject

Has Abstract

pub_date

2005-10-03 00:00:00

pages

49-58

issue

1-3

eissn

0014-2999

issn

1879-0712

pii

S0014-2999(05)00751-X

journal_volume

521

pub_type

杂志文章

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