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Temperature-dependent increase in the calcium sensitivity and acceleration of activation of ANO6 chloride channel variants

DC Field Value Language
dc.contributor.author이민구-
dc.contributor.author전익현-
dc.date.accessioned2019-09-20T07:35:01Z-
dc.date.available2019-09-20T07:35:01Z-
dc.date.issued2019-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/170960-
dc.description.abstractAnoctamin-6 (ANO6) belongs to a family of calcium (Ca2+)-activated chloride channels (CaCCs), with three splicing variants (V1, V2, and V5) showing plasma membrane expression. Unlike other CaCCs, ANO6 requires a non-physiological intracellular free calcium concentration ([Ca2+]i > 1 μM) and several minutes for full activation under a whole-cell patch clamp. Therefore, its physiological role as an ion channel is uncertain and it is more commonly considered a Ca2+-dependent phospholipid scramblase. Here, we demonstrate that physiological temperature (37 °C) increases ANO6 Ca2+ sensitivity under a whole-cell patch clamp; V1 was activated by 1 μM [Ca2+]i, whereas V2 and V5 were activated by 300 nM [Ca2+]i. Increasing the temperature to 42 °C led to activation of all ANO6 variants by 100 nM [Ca2+]i. The delay time for activation of the three variants was significantly shortened at 37 °C. Notably, the temperature-dependent Ca2+-sensitisation of ANO6 became insignificant under inside-out patch clamp, suggesting critical roles of unknown cytosolic factors. Unlike channel activity, 27 °C but not 37 °C (physiological temperature) induced the scramblase activity of ANO6 at submicromolar [Ca2+]i (300 nM), irrespective of variant type. Our results reveal a physiological ion conducting property of ANO6 at 37 °C and suggest that ANO6 channel function acts separately from its scramblase activity.-
dc.description.statementOfResponsibilityopen-
dc.languageEnglish-
dc.publisherNature Publishing Group-
dc.relation.isPartOfScientific Reports-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.titleTemperature-dependent increase in the calcium sensitivity and acceleration of activation of ANO6 chloride channel variants-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Pharmacology (약리학교실)-
dc.contributor.googleauthorHaiyue Lin-
dc.contributor.googleauthorIkhyun Jun-
dc.contributor.googleauthorJoo Han Woo-
dc.contributor.googleauthorMin Goo Lee-
dc.contributor.googleauthorSung Joon Kim-
dc.contributor.googleauthorJoo Hyun Nam-
dc.identifier.doi10.1038/s41598-019-43162-1-
dc.contributor.localIdA02781-
dc.contributor.localIdA03541-
dc.relation.journalcodeJ02646-
dc.identifier.eissn2045-2322-
dc.identifier.pmid31040335-
dc.contributor.alternativeNameLee, Min Goo-
dc.contributor.affiliatedAuthor이민구-
dc.contributor.affiliatedAuthor전익현-
dc.citation.volume9-
dc.citation.number1-
dc.citation.startPage6706-
dc.identifier.bibliographicCitationScientific Reports, Vol.9(1) : 6706, 2019-
dc.identifier.rimsid64205-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Ophthalmology (안과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers

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