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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6335
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pubmed:dateCreated |
1991-9-12
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pubmed:abstractText |
Purification of skeletal muscle dihydropyridine binding sites has enabled protein complexes to be isolated from which Ca2+ currents have been reconstituted. Complementary DNAs encoding the five subunits of the dihydropyridine receptor, alpha 1, beta, gamma, alpha 2 and delta, have been cloned and it is now recognized that alpha 2 and delta are derived from a common precursor. The alpha 1 subunit can itself produce Ca2+ currents, as was demonstrated using mouse L cells lacking alpha 2 delta, beta and gamma (our unpublished results). In L cells, stable expression of skeletal muscle alpha 1 alone was sufficient to generate voltage-sensitive, high-threshold L-type Ca2+ channel currents which were dihydropyridine-sensitive and blocked by Cd2+, but the activation kinetics were about 100 times slower than expected for skeletal muscle Ca2+ channel currents. This could have been due to the cell type in which alpha 1 was being expressed or to the lack of a regulatory component particularly one of the subunits that copurifies with alpha 1. We show here that coexpression of skeletal muscle beta with skeletal muscle alpha 1 generates cell lines expressing Ca2+ channel currents with normal activation kinetics as evidence for the participation of the dihydropyridine-receptor beta subunits in the generation of skeletal muscle Ca2+ channel currents.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Barium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nicotinic
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
352
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1650913-Animals,
pubmed-meshheading:1650913-Barium,
pubmed-meshheading:1650913-Calcium Channel Blockers,
pubmed-meshheading:1650913-Calcium Channels,
pubmed-meshheading:1650913-Cell Line,
pubmed-meshheading:1650913-Genetic Vectors,
pubmed-meshheading:1650913-L Cells (Cell Line),
pubmed-meshheading:1650913-Macromolecular Substances,
pubmed-meshheading:1650913-Membrane Potentials,
pubmed-meshheading:1650913-Mice,
pubmed-meshheading:1650913-Receptors, Nicotinic,
pubmed-meshheading:1650913-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
Normalization of current kinetics by interaction between the alpha 1 and beta subunits of the skeletal muscle dihydropyridine-sensitive Ca2+ channel.
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pubmed:affiliation |
Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, Texas 77030.
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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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