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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-10-29
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pubmed:abstractText |
125I-Apamin and photolabile derivatives of the toxin have been used to investigate the binding properties and subunit composition of small conductance Ca2+-activated potassium channels (SK(Ca) channels) expressed on plasma membranes from rat brain, rabbit liver, or rat pheochromocytoma (PC12) cells. On all preparations, 125I-apamin recognized single classes of acceptor binding sites with similar high affinity (Kd approximately 3-6 pM). Gallamine, however, was found to readily discriminate between 125I-apamin acceptors present in these preparations, showing a maximal approx nine-fold difference in affinity for acceptors expressed by rabbit liver or PC12 cells. Affinity-labeling patterns revealed the expression of different hetero-oligomeric combinations of high (86 or 59 kDa) and low (33 or 30 kDa) molecular mass 125I-apamin-binding polypeptides, consistent with pharmacological differences. Alternative expression of either 86- or 59-kDa polypeptides appeared to be the most important factor influencing gallamine's affinity for SK(Ca) channel subtypes. Both high- and low-molecular-mass polypeptides are integral membrane proteins, the latter being glycosylated in a tissue-specific manner.
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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/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Apamin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Gallamine Triethiodide,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels...,
http://linkedlifedata.com/resource/pubmed/chemical/Small-Conductance...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
346
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
151-60
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pubmed:dateRevised |
2010-8-25
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pubmed:meshHeading |
pubmed-meshheading:9328295-Affinity Labels,
pubmed-meshheading:9328295-Animals,
pubmed-meshheading:9328295-Apamin,
pubmed-meshheading:9328295-Brain Chemistry,
pubmed-meshheading:9328295-Calcium,
pubmed-meshheading:9328295-Gallamine Triethiodide,
pubmed-meshheading:9328295-Ion Channel Gating,
pubmed-meshheading:9328295-Liver,
pubmed-meshheading:9328295-PC12 Cells,
pubmed-meshheading:9328295-Potassium Channels,
pubmed-meshheading:9328295-Potassium Channels, Calcium-Activated,
pubmed-meshheading:9328295-Rabbits,
pubmed-meshheading:9328295-Rats,
pubmed-meshheading:9328295-Small-Conductance Calcium-Activated Potassium Channels
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pubmed:year |
1997
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pubmed:articleTitle |
Structural diversity among subtypes of small-conductance Ca2+-activated potassium channels.
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pubmed:affiliation |
Department of Paediatrics and Neonatal Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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