pubmed-article:11369031 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0003290 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0031436 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0040615 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0949653 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C1416610 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0205464 | lld:lifeskim |
pubmed-article:11369031 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
pubmed-article:11369031 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:11369031 | pubmed:dateCreated | 2001-5-22 | lld:pubmed |
pubmed-article:11369031 | pubmed:abstractText | A stable CHO-K1 cell line was developed which expresses the human small conductance calcium-activated potassium channel hSK3. Immunofluorescence microscopy using an anti-SK3 antibody and radioligand binding using [(125)I]-apamin demonstrated the presence of hSK3 channel in the recombinant cell line. This cell line was utilised in a fluorescence assay using the membrane potential-sensitive dye DiBAC(4)(3) to functionally analyse and pharmacologically characterise this potassium channel. The analysis of known blockers of calcium-activated potassium channels revealed the highest potency for apamin (IC(50)=13.2 nM). This result was confirmed by direct recordings of SK3 currents using the whole-cell patch-clamp technique. Tricyclic antidepressants such as desipramine, imipramine and nortriptyline as well as phenothiazines such as fluphenazine, promethazine, chlorpromazine and trifluoperazine blocked the hSK3 channel with micromolar potencies. These compounds also displaced [(125)I]-apamin binding to the hSK3 channel thus suggesting direct and competitive channel blocking activity. Since these compounds share a common three-ring molecular core structure, this feature seems to be important for channel blocking activity. The serine/threonine protein phosphatase inhibitors okadaic acid and calyculin A were able to abolish channel activation with nanomolar potencies, but did not displace [(125)I]-apamin binding. Thus, phosphorylation of hSK3 or an accessory channel subunit seems to be involved in its modulation. | lld:pubmed |
pubmed-article:11369031 | pubmed:language | eng | lld:pubmed |
pubmed-article:11369031 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11369031 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11369031 | pubmed:month | May | lld:pubmed |
pubmed-article:11369031 | pubmed:issn | 0028-3908 | lld:pubmed |
pubmed-article:11369031 | pubmed:author | pubmed-author:EuraTT | lld:pubmed |
pubmed-article:11369031 | pubmed:author | pubmed-author:PulaGG | lld:pubmed |
pubmed-article:11369031 | pubmed:author | pubmed-author:TerstappenG... | lld:pubmed |
pubmed-article:11369031 | pubmed:author | pubmed-author:CarignaniCC | lld:pubmed |
pubmed-article:11369031 | pubmed:author | pubmed-author:RoncaratiRR | lld:pubmed |
pubmed-article:11369031 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11369031 | pubmed:volume | 40 | lld:pubmed |
pubmed-article:11369031 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11369031 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11369031 | pubmed:pagination | 772-83 | lld:pubmed |
pubmed-article:11369031 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:11369031 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11369031 | pubmed:articleTitle | Pharmacological characterisation of the human small conductance calcium-activated potassium channel hSK3 reveals sensitivity to tricyclic antidepressants and antipsychotic phenothiazines. | lld:pubmed |
pubmed-article:11369031 | pubmed:affiliation | Molecular Biology and Biochemistry Unit, GlaxoWellcome Medicines Research Centre, Via A. Fleming 4, 37135 Verona, Italy. gct66554@glaxowellcome.co.uk | lld:pubmed |
pubmed-article:11369031 | pubmed:publicationType | Journal Article | lld:pubmed |
entrez-gene:3782 | entrezgene:pubmed | pubmed-article:11369031 | lld:entrezgene |
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