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      Participation of GABA A Chloride Channels in the Anxiolytic-Like Effects of a Fatty Acid Mixture

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          Human amniotic fluid and a mixture of eight fatty acids (FAT-M) identified in this maternal fluid (C12:0, lauric acid, 0.9  μ g%; C14:0, myristic acid, 6.9  μ g%; C16:0, palmitic acid, 35.3  μ g%; C16:1, palmitoleic acid, 16.4  μ g%; C18:0, stearic acid, 8.5  μ g%; C18:1 cis, oleic acid, 18.4  μ g%; C18:1 trans, elaidic acid, 3.5  μ g%; C18:2, linoleic acid, 10.1  μ g%) produce anxiolytic-like effects that are comparable to diazepam in Wistar rats, suggesting the involvement of γ -aminobutyric acid-A (GABA A) receptors, a possibility not yet explored. Wistar rats were subjected to the defensive burying test, elevated plus maze, and open field test. In different groups, three GABA A receptor antagonists were administered 30 min before FAT-M administration, including the competitive GABA binding antagonist bicuculline (1 mg/kg), GABA A benzodiazepine antagonist flumazenil (5 mg/kg), and noncompetitive GABA A chloride channel antagonist picrotoxin (1 mg/kg). The FAT-M exerted anxiolytic-like effects in the defensive burying test and elevated plus maze, without affecting locomotor activity in the open field test. The GABA A antagonists alone did not produce significant changes in the behavioral tests. Picrotoxin but not bicuculline or flumazenil blocked the anxiolytic-like effect of the FAT-M. Based on the specific blocking action of picrotoxin on the effects of the FAT-M, we conclude that the FAT-M exerted its anxiolytic-like effects through GABA A receptor chloride channels.

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          Most cited references 35

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          Endogenous neurosteroids regulate GABAA receptors through two discrete transmembrane sites.

          Inhibitory neurotransmission mediated by GABA(A) receptors can be modulated by the endogenous neurosteroids, allopregnanolone and tetrahydro-deoxycorticosterone. Neurosteroids are synthesized de novo in the brain during stress, pregnancyand after ethanol consumption, and disrupted steroid regulation of GABAergic transmission is strongly implicated in several debilitating conditions such as panic disorder, major depression, schizophrenia, alcohol dependence and catamenial epilepsy. Determining how neurosteroids interact with the GABA(A) receptor is a prerequisite for understanding their physiological and pathophysiological roles in the brain. Here we identify two discrete binding sites in the receptor's transmembrane domains that mediate the potentiating and direct activation effects of neurosteroids. They potentiate GABA responses from a cavity formed by the alpha-subunit transmembrane domains, whereas direct receptor activation is initiated by interfacial residues between alpha and beta subunits and is enhanced by steroid binding to the potentiation site. Thus, significant receptor activation by neurosteroids relies on occupancy of both the activation and potentiation sites. These sites are highly conserved throughout the GABA(A )receptor family, and their identification provides a unique opportunity for the development of new therapeutic, neurosteroid-based ligands and transgenic disease models of neurosteroid dysfunction.
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            Guide for the Care and Use of Laboratory Animal

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              The 'ABC' of GABA receptors.

               J Bormann (1999)
              In the conventional view, GABA acts at either ionotropic GABAA or metabotropic GABAB receptors. Recently, novel ionotropic GABA receptors that are composed of rho-subunits have been identified in the vertebrate retina. These bicuculline- and baclofen-insensitive GABA receptors are frequently called GABAC, following an early suggestion by Graham Johnston and colleagues. An IUPHAR committee has recommended that the term GABAC be avoided and subclassifies the retinal receptors as GABAA0r. However, new evidence regarding the pharmacology, structure, function, genetics and cellular localization of ionotropic GABA receptors strengthens the case for the existence of two major classes of these receptors, GABAA and GABAC.

                Author and article information

                Biomed Res Int
                Biomed Res Int
                BioMed Research International
                Hindawi Publishing Corporation
                19 September 2013
                : 2013
                1Laboratorio de Neurofarmacología, Instituto de Neuroetología, Universidad Veracruzana, 91190 Xalapa, VER, Mexico
                2Unidad Periférica Xalapa, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, 91190 Xalapa, VER, Mexico
                Author notes
                *Carlos M. Contreras: ccontreras@ 123456uv.mx

                Academic Editor: Brynn Levy

                Copyright © 2013 Juan Francisco Rodríguez-Landa et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                Research Article


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