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- W110413360 abstract "In this article, we describe a new endogenous phosphorylation mechanism of the ionotropic γ-aminobutyric acid receptor (GABAAR). The kinase involved in this process – the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) – is closely associated with the receptor at the plasma membrane and phosphorylates the α1 subunit of the receptor. This phosphorylation maintains GABAAR function. A reduction in GABAergic neurotransmission has been suggested as a pathophysiological mechanism for human epilepsy. Here we show both reduced efficacy of this glycolysis-dependent GABAAR phosphorylation mechanism and of GABAergic inhibition in epileptogenic cortical tissue samples obtained during curative surgery on patients with partial seizures (as compared with nonepileptogenic human cortical tissue). These changes are not due to a reduction in the density of GABAAR α1 subunits in the epileptogenic tissue, as shown by photoaffinity labeling of the receptors. The decreased GABAAR function can account for transient failures of GABAergic inhibition and may favor seizure initiation and propagation. Maintaining the receptor in a phosphorylated state sustains the GABAAR responses in the human epileptogenic cortex. These findings indicate a functional link between epileptic pathology and the regional cerebral glucose hypometabolism observed in patients with partial epilepsies. They also point to new molecular targets for developing compounds active in drug-resistant epilepsies." @default.
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- W110413360 date "2009-01-01" @default.
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- W110413360 title "METABOLIC CHANGES | Glucose Metabolism and GABAA Receptor Dysfunction in Human Partial Epilepsy" @default.
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- W110413360 doi "https://doi.org/10.1016/b978-012373961-2.00153-3" @default.
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