Redox potential and the response of cardiac ryanodine receptors to CLIC-2, a member of the glutathione S-transferase structural family

dc.contributor.authorJalilian , Chris
dc.contributor.authorGallant, Esther
dc.contributor.authorBoard, Philip
dc.contributor.authorDulhunty, Angela
dc.date.accessioned2015-12-08T22:29:51Z
dc.date.issued2008
dc.date.updated2015-12-08T09:24:47Z
dc.description.abstractThe type 2 chloride intracellular channel, CLIC-2, is a member of the glutathione S-transferase structural family and a suppressor of cardiac ryanodine receptor (RyR2) Ca2+ channels located in the membrane of the sarcoplasmic reticulum (SR). Modulators of RyR2 activity can alter cardiac contraction. Since both CLIC-2 and RyR2 are modified by redox reactions, we speculated that the action of CLIC-2 on RyR2 may depend on redox potential. We used a GSH:GSSG buffer system to produce mild changes in redox potential to influence redox sensors in RyR2 and CLIC-2. RyR2 activity was modified only when both luminal and cytoplasmic solutions contained the GSH:GSSG buffer and the effects were reversed by removing the buffer from one of the solutions. Channel activity increased with an oxidizing redox potential and decreased when the potential was more reducing. Addition of cytoplasmic CLIC-2 inhibited RyR2 with oxidizing redox potentials, but activated RyR2 under reducing conditions. The results suggested that both RyR2 and CLIC-2 contain redox sensors. Since cardiac ischemia involves a destructive Ca2+ overload that is partly due to oxidation-induced increase in RyR2 activity, we speculate that the properties of CLIC-2 place it in an ideal position to limit ischemia-induced cellular damage in cardiac muscle.
dc.identifier.issn1557-7716
dc.identifier.urihttp://hdl.handle.net/1885/34254
dc.publisherMary Ann Liebert Inc.
dc.sourceAntioxidants & redox signaling
dc.subjectKeywords: buffer; calcium channel; calcium ion; chloride channel; glutathione transferase; ryanodine receptor 2; article; calcium cell level; cell damage; cytoplasm; heart contraction; heart muscle; heart muscle ischemia; human; human cell; oxidation reduction reac
dc.titleRedox potential and the response of cardiac ryanodine receptors to CLIC-2, a member of the glutathione S-transferase structural family
dc.typeJournal article
local.bibliographicCitation.issue10
local.bibliographicCitation.lastpage86
local.bibliographicCitation.startpage1675
local.contributor.affiliationJalilian , Chris, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationGallant, Esther, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationDulhunty, Angela, College of Medicine, Biology and Environment, ANU
local.contributor.authoremailu4141180@anu.edu.au
local.contributor.authoruidJalilian , Chris, u4077374
local.contributor.authoruidGallant, Esther, u4141180
local.contributor.authoruidBoard, Philip, u7701651
local.contributor.authoruidDulhunty, Angela, u8404877
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor060110 - Receptors and Membrane Biology
local.identifier.ariespublicationu4020362xPUB111
local.identifier.citationvolume10
local.identifier.doi10.1089/ars.2007.1994
local.identifier.scopusID2-s2.0-49749085189
local.identifier.thomsonID000258625900001
local.identifier.uidSubmittedByu4020362
local.type.statusPublished Version

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