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Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate
Anandamide (N-arachidonoylethanolamine, AEA) belongs to an emerging class of endogenous lipids, called "endocannabinoids". A specific AEA membrane transporter (AMT) allows the import of this lipid and its degradation by the intracellular enzyme AEA hydrolase. Here, we show that synaptosome...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2002
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139962/ https://www.ncbi.nlm.nih.gov/pubmed/12617751 http://dx.doi.org/10.1186/1476-511X-1-1 |
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author | Battista, Natalia Bari, Monica Finazzi-Agrò, Alessandro Maccarrone, Mauro |
author_facet | Battista, Natalia Bari, Monica Finazzi-Agrò, Alessandro Maccarrone, Mauro |
author_sort | Battista, Natalia |
collection | PubMed |
description | Anandamide (N-arachidonoylethanolamine, AEA) belongs to an emerging class of endogenous lipids, called "endocannabinoids". A specific AEA membrane transporter (AMT) allows the import of this lipid and its degradation by the intracellular enzyme AEA hydrolase. Here, we show that synaptosomes from human, mouse and rat brain might be an ideal ex vivo system for the study of: i) the accumulation of AEA in brain, and ii) the pharmacological properties of AMT inhibitors. Using this ex vivo system, we demonstrate for the first time that glutamine and glutamate act as non-competitive inhibitors of AEA uptake by human, mouse and rat brain AMT. |
format | Text |
id | pubmed-139962 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-1399622003-01-20 Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate Battista, Natalia Bari, Monica Finazzi-Agrò, Alessandro Maccarrone, Mauro Lipids Health Dis Short Paper Anandamide (N-arachidonoylethanolamine, AEA) belongs to an emerging class of endogenous lipids, called "endocannabinoids". A specific AEA membrane transporter (AMT) allows the import of this lipid and its degradation by the intracellular enzyme AEA hydrolase. Here, we show that synaptosomes from human, mouse and rat brain might be an ideal ex vivo system for the study of: i) the accumulation of AEA in brain, and ii) the pharmacological properties of AMT inhibitors. Using this ex vivo system, we demonstrate for the first time that glutamine and glutamate act as non-competitive inhibitors of AEA uptake by human, mouse and rat brain AMT. BioMed Central 2002-09-03 /pmc/articles/PMC139962/ /pubmed/12617751 http://dx.doi.org/10.1186/1476-511X-1-1 Text en Copyright © 2002 Battista et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. |
spellingShingle | Short Paper Battista, Natalia Bari, Monica Finazzi-Agrò, Alessandro Maccarrone, Mauro Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title | Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title_full | Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title_fullStr | Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title_full_unstemmed | Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title_short | Anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
title_sort | anandamide uptake by synaptosomes from human, mouse and rat brain: inhibition by glutamine and glutamate |
topic | Short Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139962/ https://www.ncbi.nlm.nih.gov/pubmed/12617751 http://dx.doi.org/10.1186/1476-511X-1-1 |
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