Cholesterol effects on nicotinic acetylcholine receptor
نویسندگان
چکیده
منابع مشابه
Transient Cholesterol Effects on Nicotinic Acetylcholine Receptor Cell-Surface Mobility
To what extent do cholesterol-rich lipid platforms modulate the supramolecular organization of the nicotinic acetylcholine receptor (AChR)? To address this question, the dynamics of AChR particles at high density and its cholesterol dependence at the surface of mammalian cells were studied by combining total internal reflection fluorescence microscopy and single-particle tracking. AChR particle...
متن کاملEmbedded cholesterol in the nicotinic acetylcholine receptor.
The nicotinic acetylcholine receptor (nAChR) is a cation-selective channel central to both neuronal and muscular processes and is considered the prototype for ligand-gated ion channels, motivating a structural determination effort that spanned several decades [Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4 A resolution. J Mol Biol 346:967-989]. Purified nAChR must...
متن کاملIdentifying the cholesterol binding domain in the nicotinic acetylcholine receptor with [125I]azido-cholesterol.
A novel photoreactive analog of cholesterol, 3alpha-(4-azido-3-[125I]iodosalicylic)-cholest-5-ene ([125I]azido-cholesterol), was used to label both native acetylcholine receptor (AChR)-rich membranes from Torpedo californica and affinity-purified Torpedo AChRs reconstituted into lipid vesicles. In both cases all four AChR subunits incorporated [125I]azido-cholesterol on an equal molar basis and...
متن کاملDiversity of insect nicotinic acetylcholine receptor subunits.
Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that mediate fast synaptic transmission in the insect nervous system and are targets of a major group of insecticides, the neonicotinoids. They consist of five subunits arranged around a central ion channeL Since the subunit composition determines the functional and pharmacological properties of the receptor the presence o...
متن کاملConformation of acetylcholine bound to the nicotinic acetylcholine receptor.
We report here the biologically active conformation of acetylcholine when bound to the high-affinity state of the receptor from Torpedo californica. The acetylcholine conformation was determined in the free and bound states by proton NMR two-dimensional nuclear Overhauser effects. In agreement with x-ray crystallographic data, acetylcholine in solution has an extended conformation with an avera...
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ژورنال
عنوان ژورنال: Journal of Neurochemistry
سال: 2007
ISSN: 0022-3042,1471-4159
DOI: 10.1111/j.1471-4159.2007.04719.x