<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rosker C</submitter><funding>Wellcome Trust</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>5186-94</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2643496</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>284(8)</volume><pubmed_abstract>Ryanodine receptors (RyR) are Ca(2+) channels that mediate Ca(2+) release from intracellular stores in response to diverse intracellular signals. In RINm5F insulinoma cells, caffeine, and 4-chloro-m-cresol (4CmC), agonists of RyR, stimulated Ca(2+) entry that was independent of store-operated Ca(2+) entry, and blocked by prior incubation with a concentration of ryanodine that inactivates RyR. Patch-clamp recording identified small numbers of large-conductance (gamma(K) = 169 pS) cation channels that were activated by caffeine, 4CmC or low concentrations of ryanodine. Similar channels were detected in rat pancreatic beta-cells. In RINm5F cells, the channels were blocked by cytosolic, but not extracellular, ruthenium red. Subcellular fractionation showed that type 3 IP(3) receptors (IP(3)R3)</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Functional ryanodine receptors in the plasma membrane of RINm5F pancreatic beta-cells.</pubmed_title><pmcid>PMC2643496</pmcid><funding_grant_id>BB/E004660/1</funding_grant_id><pubmed_authors>Rosker C</pubmed_authors><pubmed_authors>Taylor CW</pubmed_authors><pubmed_authors>Taylor EJ</pubmed_authors><pubmed_authors>Meur G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Functional ryanodine receptors in the plasma membrane of RINm5F pancreatic beta-cells.</name><description>Ryanodine receptors (RyR) are Ca(2+) channels that mediate Ca(2+) release from intracellular stores in response to diverse intracellular signals. In RINm5F insulinoma cells, caffeine, and 4-chloro-m-cresol (4CmC), agonists of RyR, stimulated Ca(2+) entry that was independent of store-operated Ca(2+) entry, and blocked by prior incubation with a concentration of ryanodine that inactivates RyR. Patch-clamp recording identified small numbers of large-conductance (gamma(K) = 169 pS) cation channels that were activated by caffeine, 4CmC or low concentrations of ryanodine. Similar channels were detected in rat pancreatic beta-cells. In RINm5F cells, the channels were blocked by cytosolic, but not extracellular, ruthenium red. Subcellular fractionation showed that type 3 IP(3) receptors (IP(3)R3)</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 Feb</publication><modification>2026-03-16T16:43:57.86Z</modification><creation>2019-03-27T00:20:46Z</creation></dates><accession>S-EPMC2643496</accession><cross_references><pubmed>19116207</pubmed><doi>10.1074/jbc.M805587200</doi></cross_references></HashMap>