| pubmed-article:18581036 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0327698 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0034830 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
| pubmed-article:18581036 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:18581036 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18581036 | pubmed:dateCreated | 2008-7-21 | lld:pubmed |
| pubmed-article:18581036 | pubmed:abstractText | The nicotinic acetylcholine receptor (nAChR) of Torpedo electric rays has been extensively characterized over the last three decades. However, high-resolution structural studies have been hampered by the lack of mechanistic molecular models that describe how detergents influence membrane protein stability and function. Furthermore, elucidation of the dynamic detergent-lipid-protein interactions of solubilized membrane proteins is a largely unexplored research field. This study examines the effects of nine detergents on: (1) nAChR-lipid composition (gas chromatography with flame ionization; GC-FID and/or mass selective detectors; GC-MSD), (2) stability and aggregation state (analytical size exclusion chromatography; A-SEC and electron microscopy; EM) and (3) ion channel function (planar lipid bilayers). Detergent solubilization of nAChR-enriched membranes did not result in significant native lipid depletion or destabilization. Upon purification, native lipid depletion occurred in all detergents, with lipid-analogue detergents CHAPS {(3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate}, FC-12 (n-dodecylphosphocholine) and sodium cholate (3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oic acid) maintaining stability and supporting ion channel function, and non-lipid-analogue detergents Cymal-6 (6-cyclohexyl-1-hexyl-beta-D-maltoside), DDM (n-dodecyl-beta-D-maltopyranoside), LDAO (lauryldimethylamine-N-oxide) and OG (n-octyl-beta-d-glucopyranoside) decreasing stability and significantly reducing or completely suppressing ion channel function. Anapoe-C(12)E(9 )(polyoxyethylene-[9]-dodecyl ether) and BigCHAP (N,N'-bis-[3-d-gluconamidopropyl] cholamide) retained residual amounts of native lipid, maintaining moderate stability and ion channel function compared to lipid-analogue detergents. Therefore, the nAChR can be stable and functional in lipid-analogue detergents or in detergents that retain moderate amounts of residual native lipids, but not in non-lipid-analogue detergents. | lld:pubmed |
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| pubmed-article:18581036 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18581036 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18581036 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18581036 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18581036 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18581036 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18581036 | pubmed:month | May | lld:pubmed |
| pubmed-article:18581036 | pubmed:issn | 0022-2631 | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:StevensRaymon... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:ChengAnchiA | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:HansonMichael... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:Lasalde-Domin... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:Asseo-GarcíaA... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:Asmar-RoviraG... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:QuesadaOreste... | lld:pubmed |
| pubmed-article:18581036 | pubmed:author | pubmed-author:NoguerasCarlo... | lld:pubmed |
| pubmed-article:18581036 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18581036 | pubmed:volume | 223 | lld:pubmed |
| pubmed-article:18581036 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18581036 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18581036 | pubmed:pagination | 13-26 | lld:pubmed |
| pubmed-article:18581036 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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| pubmed-article:18581036 | pubmed:meshHeading | pubmed-meshheading:18581036... | lld:pubmed |
| pubmed-article:18581036 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18581036 | pubmed:articleTitle | Biophysical and ion channel functional characterization of the Torpedo californica nicotinic acetylcholine receptor in varying detergent-lipid environments. | lld:pubmed |
| pubmed-article:18581036 | pubmed:affiliation | Departments of Cell Biology and Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:18581036 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18581036 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18581036 | lld:pubmed |
