Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?

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...

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Detalles Bibliográficos
Autores principales: Baur, Roland, Gertsch, Jürg, Sigel, Erwin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2013
Materias:
Biochemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3775635/
https://www.ncbi.nlm.nih.gov/pubmed/24058880
http://dx.doi.org/10.7717/peerj.149
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author Baur, Roland
Gertsch, Jürg
Sigel, Erwin
author_facet Baur, Roland
Gertsch, Jürg
Sigel, Erwin
author_sort Baur, Roland
collection PubMed
description 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 α(1)β(2)γ(2) GABA(A) receptors. Here we characterize in more detail this modulation and investigate the relationship of its binding site with that of the endocannabinoid 2-AG.
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spelling pubmed-37756352013-09-20 Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors? Baur, Roland Gertsch, Jürg Sigel, Erwin PeerJ Biochemistry 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 α(1)β(2)γ(2) GABA(A) receptors. Here we characterize in more detail this modulation and investigate the relationship of its binding site with that of the endocannabinoid 2-AG. PeerJ Inc. 2013-09-10 /pmc/articles/PMC3775635/ /pubmed/24058880 http://dx.doi.org/10.7717/peerj.149 Text en © 2013 Baur et al. http://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Biochemistry
Baur, Roland
Gertsch, Jürg
Sigel, Erwin
Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title_full Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title_fullStr Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title_full_unstemmed Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title_short Do N-arachidonyl-glycine (NA-glycine) and 2-arachidonoyl glycerol (2-AG) share mode of action and the binding site on the β(2) subunit of GABA(A) receptors?
title_sort do n-arachidonyl-glycine (na-glycine) and 2-arachidonoyl glycerol (2-ag) share mode of action and the binding site on the β(2) subunit of gaba(a) receptors?
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3775635/
https://www.ncbi.nlm.nih.gov/pubmed/24058880
http://dx.doi.org/10.7717/peerj.149
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