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Braz. j. med. biol. res ; 26(6): 553-71, Jun. 1993. tab
Article in English | LILACS | ID: lil-148709

ABSTRACT

The nicotinic acetylcholine receptor (AChR) is still the paradigm of rapid ligand-gated ion channels. Since the early finding of a motionally restricted shell of lipids ( annulus ) in the immediate perimeter of the membrane-bound AChR, experimental evidence has supported the notion that the interface between the protein moiety and the adjacent lipid molecules is the site of action of a variety of pharmacologically relevant substances, including non-competitive inhibitors of the cholinergic system like some local anesthetics, short-chain alcohols, and steroids. Patch-clamp data on cells expressing the AChR protein add another dimension to this knowledge, enabling correlations to be established between the chemical composition of lipid-modified cells and the functional properties (ligand binding, channel gating) of the receptor protein in situ


Subject(s)
Animals , Ion Channel Gating , Membrane Lipids/metabolism , Receptors, Nicotinic/metabolism , Anesthetics/pharmacology , Cholesterol/metabolism , Cholesterol/pharmacology , Dexamethasone/pharmacology , Electron Spin Resonance Spectroscopy , Fatty Acids, Nonesterified/metabolism , Fatty Acids, Nonesterified/pharmacology , Ion Channel Gating , Kinetics , Membrane Lipids/pharmacology , Receptors, Nicotinic
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