Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output

Simple item page
dc.contributor.authorDulhunty, Angela
dc.contributor.authorWium, Elize
dc.contributor.authorLi, Linwei
dc.contributor.authorHanna, Amy
dc.contributor.authorMirza, Shamaruh
dc.contributor.authorTalukder, Sadik
dc.contributor.authorGhazali, Nuur
dc.contributor.authorBeard, Nicole
dc.date.accessioned2015-12-10T22:28:39Z
dc.date.issued2012
dc.date.updated2016-02-24T10:27:49Z
dc.description.abstractThe contractile function of the heart requires the release of Ca2+ from intracellular Ca2+ stores in the sarcoplasmic reticulum (SR) of cardiac muscle cells. The efficacy of Ca2+ release depends on the amount of Ca2+ loaded into the Ca2+ store and the way in which this 'Ca2+ load' influences the activity of the cardiac ryanodine receptor Ca2+ release channel (RyR2). The effects of the Ca2+ load on Ca2+ release through RyR2 are facilitated by: (i) the sensitivity of RyR2 itself to luminal Ca2+ concentrations; and (ii) interactions between the cardiac Ca2+-binding protein calsequestrin (CSQ) 2 and RyR2, transmitted through the 'anchoring' proteins junctin and/or triadin. Mutations in RyR2 are linked to catecholaminergic polymorphic ventricular tachycardia (CPVT) and sudden cardiac death. The tachycardia is associated with changes in the sensitivity of RyR2 to luminal Ca2+. Triadin-, junctin- or CSQ-null animals survive, but their longevity and ability to tolerate stress is compromised. These studies reveal the importance of the proteins in normal muscle function, but do not reveal the molecular nature of their functional interactions, which must be defined before changes in the proteins leading to CPVT and heart disease can be understood. Herein, we discuss known interactions between the RyR, triadin, junctin and CSQ with emphasis on the cardiac isoforms of the proteins. Where there is little known about the cardiac isoforms, we discuss evidence from skeletal isoforms.
dc.identifier.issn0305-1870
dc.identifier.urihttp://hdl.handle.net/1885/54552
dc.publisherBlackwell Science Asia
dc.sourceClinical and Experimental Pharmacology and Physiology
dc.subjectKeywords: calcium ion; calsequestrin; junctin; protein; ryanodine receptor 2; sarcoplasmic reticulum calcium transporting adenosine triphosphatase; triadin; unclassified drug; article; binding affinity; binding site; calcium cell level; calcium transport; catechola Calcium signalling; Calsequestrin; Cardiac muscle; Junctin; Luminal calcium dependence of calcium release; Protein-protein interactions; Ryanodine receptor calcium release channel; Sarcoplasmic reticulum; Triadin
dc.titleProteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output
dc.typeJournal article
local.bibliographicCitation.lastpage484
local.bibliographicCitation.startpage477
local.contributor.affiliationDulhunty, Angela, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationWium, Elize, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationLi, Linwei, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHanna, Amy, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationMirza, Shamaruh, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationTalukder, Sadik, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationGhazali, Nuur, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBeard, Nicole, College of Medicine, Biology and Environment, ANU
local.contributor.authoremailu8404877@anu.edu.au
local.contributor.authoruidDulhunty, Angela, u8404877
local.contributor.authoruidWium, Elize, u4305417
local.contributor.authoruidLi, Linwei, u4609614
local.contributor.authoruidHanna, Amy, u4498566
local.contributor.authoruidMirza, Shamaruh, u4284865
local.contributor.authoruidTalukder, Sadik, u4932063
local.contributor.authoruidGhazali, Nuur, u4371631
local.contributor.authoruidBeard, Nicole, u9802885
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor060110 - Receptors and Membrane Biology
local.identifier.ariespublicationu4020362xPUB304
local.identifier.citationvolume39
local.identifier.doi10.1111/j.1440-1681.2012.05704.x
local.identifier.scopusID2-s2.0-84860261837
local.identifier.thomsonID000303118600013
local.identifier.uidSubmittedByu4020362
local.type.statusPublished Version

Downloads

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
01_Dulhunty_Proteins_within_the_2012.pdf
Size:
3.09 MB
Format:
Adobe Portable Document Format
Download

Collections

ANU Research Publications

DSpace software copyright © 2002-2024 LYRASIS