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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
1997-11-20
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pubmed:abstractText |
We have characterized the alpha-bungarotoxin receptors (BgtRs) found on the cell surface of undifferentiated pheochromocytoma (PC12) cells. The PC12 cells express a homogeneous population of alpha7-containing receptors that bind alpha-Bgt with high affinity (Kd = 94 pM). The BgtRs mediate most of the response elicited by nicotine, because the BgtR-specific antagonists methyllycaconitine and alpha-Bgt block approximately 90% of the whole-cell current. The binding of nicotinic agonists to cell-surface BgtRs was highly cooperative with four different agonists showing Hill coefficients in the range of 2.3-2.4. A similar agonist binding cooperativity was observed for BgtR homomers formed from chimeric alpha7/5HT3 subunits expressed in tsA 201 cells. Two classes of agonist binding sites, in the ratio of 4:1 for PC12 cell BgtRs and 3:1 for alpha7/5HT3 BgtRs, were revealed by bromoacetylcholine alkylation of the reduced sites on both PC12 BgtRs and alpha7/5HT3 BgtRs. We conclude from this data that PC12 BgtRs and alpha7/5HT3 homomers contain at least three distinguishable agonist binding sites and thus are different from other nicotinic receptors.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3,3'-dithiobis(sulfosuccinimidyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Aconitine,
http://linkedlifedata.com/resource/pubmed/chemical/Bungarotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholinergic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nicotine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nicotinic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin, 5-HT3,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Succinimides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha7 nicotinic acetylcholine...,
http://linkedlifedata.com/resource/pubmed/chemical/methyllycaconitine
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0270-6474
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8201-12
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pubmed:dateRevised |
2010-6-4
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pubmed:meshHeading |
pubmed-meshheading:9334396-Acetylcholine,
pubmed-meshheading:9334396-Aconitine,
pubmed-meshheading:9334396-Alkylation,
pubmed-meshheading:9334396-Animals,
pubmed-meshheading:9334396-Binding Sites,
pubmed-meshheading:9334396-Bungarotoxins,
pubmed-meshheading:9334396-Centrifugation, Density Gradient,
pubmed-meshheading:9334396-Cholinergic Agents,
pubmed-meshheading:9334396-Cross-Linking Reagents,
pubmed-meshheading:9334396-Neoplasm Proteins,
pubmed-meshheading:9334396-Nerve Tissue Proteins,
pubmed-meshheading:9334396-Nicotine,
pubmed-meshheading:9334396-PC12 Cells,
pubmed-meshheading:9334396-Patch-Clamp Techniques,
pubmed-meshheading:9334396-Rats,
pubmed-meshheading:9334396-Receptors, Nicotinic,
pubmed-meshheading:9334396-Receptors, Serotonin,
pubmed-meshheading:9334396-Receptors, Serotonin, 5-HT3,
pubmed-meshheading:9334396-Recombinant Fusion Proteins,
pubmed-meshheading:9334396-Structure-Activity Relationship,
pubmed-meshheading:9334396-Succinimides
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pubmed:year |
1997
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pubmed:articleTitle |
Neuronal alpha-bungarotoxin receptors differ structurally from other nicotinic acetylcholine receptors.
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pubmed:affiliation |
Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, IL 60637, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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