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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-12-9
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pubmed:abstractText |
Neuronal nicotinic acetylcholine receptors (nAChR) are made from different combinations of subunits encoded by a diverse family of genes. However, the recently cloned alpha 7 gene codes for subunits that can form homooligomeric nAChR complexes when expressed in Xenopus oocytes. Electrophysiological studies reveal that these alpha 7-nAChR function as alpha-bungarotoxin (Bgt)-sensitive, quickly activating/inactivating ion channels with a unique pharmacological profile and an unusually high permeability to calcium ions. Although similar observations have been made in studies of Bgt-sensitive, functional nAChR subtypes that are naturally expressed in neuronal cells, all attempts until now to reconstitute functional alpha 7-nAChR in cell lines have failed. Here we report the successful use of SH-SY5Y human neuroblastoma cells, which naturally express low levels of endogenous alpha 7 transcripts, to stably overexpress heterologous rat nAChR alpha 7 transgenes. These transgenes are expressed as the appropriately-sized alpha 7 messages and protein, and stably transfected SH-SY5Y cells have over 30-times higher levels of specific Bgt binding sites than do wild-type cells. Whole cell current recordings confirm that transfected cells express functional nAChR that are sensitive to blockade by Bgt and display the typical physiological and pharmacological profiles of alpha 7-nAChR. We conclude that stable, functional expression of alpha 7 transgenes in a mammalian cell line has been achieved for the first time.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bungarotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nicotinic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
354
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
155-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7957916-Animals,
pubmed-meshheading:7957916-Binding Sites,
pubmed-meshheading:7957916-Bungarotoxins,
pubmed-meshheading:7957916-DNA, Complementary,
pubmed-meshheading:7957916-Electrophysiology,
pubmed-meshheading:7957916-Gene Expression,
pubmed-meshheading:7957916-Humans,
pubmed-meshheading:7957916-Neuroblastoma,
pubmed-meshheading:7957916-RNA, Messenger,
pubmed-meshheading:7957916-Rats,
pubmed-meshheading:7957916-Receptors, Nicotinic,
pubmed-meshheading:7957916-Recombinant Proteins,
pubmed-meshheading:7957916-Transfection,
pubmed-meshheading:7957916-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
Functional expression of nicotinic acetylcholine receptors containing rat alpha 7 subunits in human SH-SY5Y neuroblastoma cells.
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pubmed:affiliation |
Division of Neurobiology, Barrow Neurological Institute, Phoenix, AZ 85013.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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