Abstract
NA-glycine is an endogenous lipid molecule with analgesic properties, which is structurally similar to the endocannabinoids 2-AG and anandamide but does not interact with cannabinoid receptors. NA-glycine has been suggested to act at the G-protein coupled receptors GPR18 and GPR92. Recently, we have described that NA-glycine can also modulate recombinant α1β2γ2 GABAA receptors. Here we characterize in more detail this modulation and investigate the relationship of its binding site with that of the endocannabinoid 2-AG.
Highlights
GABA is the major inhibitory neurotransmitter in mammalian brain
We have previously demonstrated that NA-glycine allosterically potentiates GABAA receptors (Baur et al, 2013), but it remained unclear whether this occurred via the same binding site as 2-arachidonoyl glycerol (2-AG)
Experiments were performed in triplicates in three independent experiments and data are mean values ± S.D. Both NA-glycine and 2-AG allosterically potentiate recombinant α1β2γ2 GABAA receptors expressed in Xenopus oocytes
Summary
Its fast effects are mediated by synaptic and extrasynaptic GABAA receptors. These receptors are composed of five subunits that surround a central chloride ion channel (Macdonald & Olsen, 1994; Sieghart, 1995; Sieghart & Sperk, 2002; Sigel & Steinmann, 2012). The pharmacological properties are dependent on subunit composition (Sigel et al, 1990) and arrangement (Minier & Sigel, 2004)
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