The basic property of Lys385 is important for potentiation of the human α1 glycine receptor by ethanol

Ethanol alters the function of several members of the Cys-loop ligand-gated ion channel superfamily. Recent studies have shown that the sensitivity of the α1 glycine receptor (GlyR) to ethanol can be affected by the state of G protein activation mediated by the interaction of Gβγ with intracellular...

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Veröffentlicht in:	The Journal of pharmacology and experimental therapeutics 2012-02, Vol.340 (2), p.339-349
Hauptverfasser:	Castro, Patricio A, Figueroa, Maximiliano, Yevenes, Gonzalo E, San Martin, Loreto S, Aguayo, Luis G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Cell Membrane - metabolism Cellular and Molecular Chemical Phenomena Cysteine - chemistry Cysteine - genetics Dose-Response Relationship, Drug Drug Synergism Electrophysiological Phenomena - drug effects Electrophysiological Phenomena - physiology Ethanol - pharmacology Ethyl Methanesulfonate - analogs & derivatives Ethyl Methanesulfonate - chemistry Glycine - pharmacology GTP-Binding Protein beta Subunits - metabolism GTP-Binding Protein gamma Subunits - metabolism Guanosine 5'-O-(3-Thiotriphosphate) - metabolism Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology HEK293 Cells Humans Ion Channel Gating - drug effects Ion Channel Gating - physiology Lysine - chemistry Lysine - genetics Models, Molecular Neurotransmitter Agents - pharmacology Patch-Clamp Techniques Propofol - pharmacology Protein Interaction Domains and Motifs - physiology Receptors, Glycine - chemistry Receptors, Glycine - drug effects Receptors, Glycine - genetics Receptors, Glycine - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Static Electricity Surface Properties Transfection
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