{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T05:24:36Z","timestamp":1788326676024,"version":"build-2803163510"},"reference-count":46,"publisher":"Oxford University Press (OUP)","issue":"2","funder":[{"DOI":"10.13039\/100000065","name":"NINDS","doi-asserted-by":"publisher","award":["NS121718"],"award-info":[{"award-number":["NS121718"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>We have previously characterized the molecular mechanisms for variants in \u03b3-aminobutyric acid transporter 1-encoding solute carrier family 6-member 1 (SLC6A1) in vitro and concluded that a partial or complete loss of \u03b3-aminobutyric acid uptake due to impaired protein trafficking is the primary aetiology. Impairment of \u03b3-aminobutyric acid transporter 1 function could cause compensatory changes in the expression of \u03b3-aminobutyric acid receptors, which, in turn, modify disease pathophysiology and phenotype. Here we used different approaches including radioactive 3H \u03b3-aminobutyric acid uptake in cells and synaptosomes, immunohistochemistry and confocal microscopy as well as brain slice surface protein biotinylation to characterize Slc6a1+\/A288V and Slc6a1+\/S295L mice, representative of a partial or a complete loss of function of SLC6A1 mutations, respectively. We employed the \u03b3-aminobutyric acid transporter 1-specific inhibitor [3H]tiagabine binding and GABAA receptor subunit-specific radioligand binding to profile the \u03b3-aminobutyric acid transporter 1 and GABAA receptor expression in major brain regions such as cortex, cerebellum, hippocampus and thalamus. We also determined the total and surface expression of \u03b3-aminobutyric acid transporter 1, \u03b3-aminobutyric acid transporter 3 and expression of GABAA receptor in the major brain regions in the knockin mice. We found that \u03b3-aminobutyric acid transporter 1 protein was markedly reduced in cortex, hippocampus, thalamus and cerebellum in both mutant mouse lines. Consistent with the findings of reduced \u03b3-aminobutyric acid uptake for both \u03b3-aminobutyric acid transporter 1(A288V) and \u03b3-aminobutyric acid transporter 1(S295L), both the total and the \u03b3-aminobutyric acid transporter 1-mediated 3H \u03b3-aminobutyric acid reuptake was reduced. We found that \u03b3-aminobutyric acid transporter 3 is only abundantly expressed in the thalamus and there was no compensatory increase of \u03b3-aminobutyric acid transporter 3 in either of the mutant mouse lines. \u03b3-Aminobutyric acid transporter 1 was reduced in both somatic regions and nonsomatic regions in both mouse models, in which a ring-like structure was identified only in the Slc6a1+\/A288V mouse, suggesting more \u03b3-aminobutyric acid transporter 1 retention inside endoplasmic reticulum in the Slc6a1+\/A288V mouse. The [3H]tiagabine binding was similar in both mouse models despite the difference in \u03b3-aminobutyric acid uptake function and \u03b3-aminobutyric acid transporter 1 protein expression for both mutations. There were no differences in GABAA receptor subtype expression, except for a small increase in the expression of \u03b15 subunits of GABAA receptor in the hippocampus of Slc6a1S295L homozygous mice, suggesting a potential interaction between the expression of this GABAA receptor subtype and the mutant \u03b3-aminobutyric acid transporter 1. The study provides the first comprehensive characterization of the SLC6A1 mutations in vivo in two representative mouse models. Because both \u03b3-aminobutyric acid transporter 1 and GABAA receptors are targets for anti-seizure medications, the findings from this study can help guide tailored treatment options based on the expression and function of \u03b3-aminobutyric acid transporter 1 and GABAA receptor in SLC6A1 mutation-mediated neurodevelopmental and epileptic encephalopathies.<\/jats:p>","DOI":"10.1093\/braincomms\/fcae110","type":"journal-article","created":{"date-parts":[[2024,4,20]],"date-time":"2024-04-20T21:01:50Z","timestamp":1713646910000},"source":"Crossref","is-referenced-by-count":13,"title":["\u03b3-Aminobutyric acid transporter and GABAA receptor mechanisms in <i>Slc6a1+\/A288V<\/i> and <i>Slc6a1+\/S295L<\/i> mice associated with developmental and epileptic encephalopathies"],"prefix":"10.1093","volume":"6","author":[{"given":"Wangzhen","family":"Shen","sequence":"first","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerald","family":"Nwosu","sequence":"additional","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"},{"name":"Neuroscience Graduate Program, Vanderbilt University , Nashville, TN 37232 , USA"},{"name":"Vanderbilt Brain Institute , Nashville, TN 37240 , USA"},{"name":"Department of Biochemistry, Cancer Biology, Neuroscience and Pharmacology, Meharry Medical College , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Honer","sequence":"additional","affiliation":[{"name":"Pharma Research and Early Development, Roche Innovation Center Basel, F. Hoffmann-La Roche , Basel 4070 , Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jerome","family":"Clasadonte","sequence":"additional","affiliation":[{"name":"Early Solutions, Neuroscience TA, UCB Biopharma SRL , Braine l\u2019Alleud 1420 , Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svenja","family":"Schmalzbauer","sequence":"additional","affiliation":[{"name":"Pharma Research and Early Development, Roche Innovation Center Basel, F. Hoffmann-La Roche , Basel 4070 , Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marshall","family":"Biven","sequence":"additional","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherine","family":"Langer","sequence":"additional","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carson","family":"Flamm","sequence":"additional","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4151-3991","authenticated-orcid":false,"given":"Sarah","family":"Poliquin","sequence":"additional","affiliation":[{"name":"Neuroscience Graduate Program, Vanderbilt University , Nashville, TN 37232 , USA"},{"name":"Vanderbilt Brain Institute , Nashville, TN 37240 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felicia","family":"Mermer","sequence":"additional","affiliation":[{"name":"Department of Neurology, Vanderbilt University Medical Center , Nashville, TN 37232 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefanie","family":"Dedeurwaerdere","sequence":"additional","affiliation":[{"name":"Early Solutions, Neuroscience TA, UCB Biopharma SRL , Braine l\u2019Alleud 1420 , Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria-Clemencia","family":"Hernandez","sequence":"additional","affiliation":[{"name":"Pharma Research and Early Development, Roche Innovation Center Basel, F. 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