{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T06:05:56Z","timestamp":1790229956386,"version":"4.1.0"},"reference-count":35,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2009,2,2]],"date-time":"2009-02-02T00:00:00Z","timestamp":1233532800000},"content-version":"vor","delay-in-days":3260,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[2000,3]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item>\n<jats:p>Three genes encode the small\u2010conductance Ca<jats:sup>2+<\/jats:sup>\u2010activated K<jats:sup>+<\/jats:sup> channels (SK channels). We have stably expressed hSK1 and rSK2 in HEK 293 cells and addressed the pharmacology of these subtypes using whole\u2010cell patch clamp recordings.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>The bee venom peptide apamin blocked hSK1 as well as rSK2 with IC<jats:sub>50<\/jats:sub> values of 3.3\u2003n<jats:sc>M<\/jats:sc> and 83\u2003pM, respectively.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>The pharmacological separation between the subtypes was even more prominent when applying the scorpion peptide blocker scyllatoxin, which blocked hSK1 with an IC<jats:sub>50<\/jats:sub> value of 80\u2003n<jats:sc>M<\/jats:sc> and rSK2 at 287\u2003pM.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>The potent small molecule blockers showed little differentiation between the channel subtypes. The bis\u2010quinolinium cyclophane UCL 1684 blocked hSK1 with an IC<jats:sub>50<\/jats:sub> value of 762\u2003pM and rSK2 at 364\u2003pM. The antiseptic compound dequalinium chloride blocked hSK1 and rSK2 with IC<jats:sub>50<\/jats:sub> values of 444\u2003n<jats:sc>M<\/jats:sc> and 162\u2003n<jats:sc>M<\/jats:sc>, respectively.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>The nicotinic acetylcholine receptor antagonist d\u2010tubocurarine was found to block hSK1 and rSK2 with IC<jats:sub>50<\/jats:sub> values of 27\u2003\u03bc<jats:sc>M<\/jats:sc> and 17\u2003\u03bc<jats:sc>M<\/jats:sc> when measured at +80\u2003mV. The inhibition by d\u2010tubocurarine was voltage\u2010dependent with increasing affinities at more hyperpolarized potentials.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>The GABA<jats:sub>A<\/jats:sub> receptor antagonist bicuculline methiodide also blocked hSK1 and rSK2 in a voltage\u2010dependent manner with IC<jats:sub>50<\/jats:sub> values of 15 and 25\u2003\u03bc<jats:sc>M<\/jats:sc> when measured at +80\u2003mV.<\/jats:p>\n<\/jats:list-item>\n<jats:list-item>\n<jats:p>In conclusion, the pharmacological separation between SK channel subtypes expressed in mammalian cells is too small to support the notion that the apamin\u2010insensitive afterhyperpolarization of neurones is mediated by hSK1.<\/jats:p>\n<\/jats:list-item>\n<\/jats:list>\n<\/jats:p><jats:p><jats:italic>British Journal of Pharmacology<\/jats:italic> (2000) <jats:bold>129<\/jats:bold>, 991\u2013999; doi:<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" xlink:href=\"10.1038\/sj.bjp.0703120\">10.1038\/sj.bjp.0703120<\/jats:ext-link><\/jats:p>","DOI":"10.1038\/sj.bjp.0703120","type":"journal-article","created":{"date-parts":[[2005,1,28]],"date-time":"2005-01-28T20:46:58Z","timestamp":1106945218000},"page":"991-999","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":162,"title":["Pharmacological characterization of small\u2010conductance Ca<sup>2+<\/sup>\u2010activated K<sup>+<\/sup> channels stably expressed in HEK 293 cells"],"prefix":"10.1111","volume":"129","author":[{"given":"Dorte","family":"Str\u00f8b\u00e6k","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tino D","family":"J\u00f8rgensen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Palle","family":"Christophersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip K","family":"Ahring","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u00f8ren\u2010Peter","family":"Olesen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,2,2]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/379545a0"},{"key":"e_1_2_7_3_1","doi-asserted-by":"crossref","first-page":"4753","DOI":"10.1016\/S0021-9258(19)39626-7","article-title":"Leirotoxin I (Scyllatoxin), a peptide ligand for Ca2+\u2010activated K+ channels","volume":"256","author":"AUGUSTE P.","year":"1990","journal-title":"J. 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