RyR1/SERCA1 cross-talk regulation of calcium transport in heavy sarcoplasmic reticulum vesicles

dc.contributor.authorGilchrist, JSC
dc.contributor.authorPalahniuk, C
dc.contributor.authorAbrenica, B
dc.contributor.authorRampersad, P
dc.contributor.authorMutawe, M
dc.contributor.authorCook, T
dc.date.accessioned2007-10-09T18:29:21Z
dc.date.available2007-10-09T18:29:21Z
dc.date.issued2003-03-31
dc.description.abstractWe investigated the functional interdependence of sarco-endoplasmic reticulum Ca2+ ATPase isoform 1 and ryanodine receptor isoform 1 in heavy sarcoplasmic reticulum membranes by synchronous fluorescence determination of extravesicular Ca2+ transients and catalytic activity. Under conditions of dynamic Ca2+ exchange ATPase catalytic activity was well coordinated to ryanodine receptor activation/inactivation states. Ryanodine-induced activation of Ca2+ release channel leaks also produced marked ATPase activation in the absence of measurable increases in bulk free extravesicular Ca2+. This suggested that Ca2+ pumps are highly sensitive to Ca2+ release channel leak status and potently buffer Ca2+ ions exiting cytoplasmic openings of ryanodine receptors. Conversely, ryanodine receptor activation was dependent on Ca2+-ATPase pump activity. Ryanodine receptor activation by cytosolic Ca2+ was (i) inversely proportional to luminal Ca2+ load and (ii) dependent upon the rate of presentation of cytosolic Ca2+. Progressive Ca2+ filling coincided with progressive loss of Ca2+ sequestration rates and at a threshold loading, ryanodine-induced Ca2+ release produced small transient reversals of catalytic activity. These data indicate that attainment of threshold luminal Ca2+ loads coordinates sensitization of Ca2+ release channels with autogenic inhibition of Ca2+ pumping. This suggests that Ca2+-dependent control of Ca2+ release in intact heavy sarcoplasmic reticulum membranes involves a Ca2+-mediated "cross-talk" between sarco-endoplasmic reticulum Ca2+ ATPase isoform 1 and ryanodine receptor isoform 1.en
dc.format.extent2341902 bytes
dc.format.mimetypeapplication/pdf
dc.identifier.citation0008-4212; CAN J PHYSIOL PHARMACOL, MAR 2003, vol. 81, no. 3, p.301 to 310.en
dc.identifier.doihttp://dx.doi.org/10.1139/y03-035
dc.identifier.urihttp://hdl.handle.net/1993/2914
dc.language.isoengen_US
dc.rightsNo part of the NRC Research Press electronic journals may be reproduced, stored, or transmitted in any form or by any means, without the written permission of the publisher, except as stated below. Under the Canadian Copyright Act, individuals may download or print single copies of articles for personal research or study. Any person may reproduce short excerpts from articles in the journals for any purpose that respects the moral rights of authors, provided that the source is fully acknowledged. As a courtesy, the consent of authors of such material should be obtained directly from the author. Authorization to reproduce items for other than personal research or study, as stated above, may be obtained via Access © upon payment of the copyright fee of $10.00 per copy. NRC Research Press also extends certain additional rights to authors. The above rights do not extend to copying or reproduction for general distribution, for advertising or promotional purposes, for creating new collective works, or for resale. For such copying or reproduction, arrangements must be made with NRC Research Press.en
dc.rightsopen accessen_US
dc.statusPeer revieweden
dc.subjectCa2+en
dc.subjectRyRen
dc.subjectSERCAen
dc.subjectcell nucleusen
dc.subjectFK506en
dc.subjectthapsigarginen
dc.subjectryanodineen
dc.subjectINOSITOL 1,4,5-TRISPHOSPHATE RECEPTORen
dc.subjectRYANODINE RECEPTORen
dc.subjectCA2+ CHANNELSen
dc.subjectSARCOPLASMIC-RETICULUMen
dc.subjectENDOPLASMIC-RETICULUMen
dc.subjectNUCLEAR CA2+en
dc.subjectFK506-BINDING PROTEINen
dc.subjectSKELETAL-MUSCLEen
dc.subjectRELEASE CHANNELen
dc.subjectCYTOSOLIC CA2+en
dc.titleRyR1/SERCA1 cross-talk regulation of calcium transport in heavy sarcoplasmic reticulum vesiclesen
dc.typejournal articleen_US
Files