RyR1/SERCA1 cross-talk regulation of calcium transport in heavy sarcoplasmic reticulum vesicles
dc.contributor.author | Gilchrist, JSC | |
dc.contributor.author | Palahniuk, C | |
dc.contributor.author | Abrenica, B | |
dc.contributor.author | Rampersad, P | |
dc.contributor.author | Mutawe, M | |
dc.contributor.author | Cook, T | |
dc.date.accessioned | 2007-10-09T18:29:21Z | |
dc.date.available | 2007-10-09T18:29:21Z | |
dc.date.issued | 2003-03-31 | |
dc.description.abstract | We 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.extent | 2341902 bytes | |
dc.format.mimetype | application/pdf | |
dc.identifier.citation | 0008-4212; CAN J PHYSIOL PHARMACOL, MAR 2003, vol. 81, no. 3, p.301 to 310. | en |
dc.identifier.doi | http://dx.doi.org/10.1139/y03-035 | |
dc.identifier.uri | http://hdl.handle.net/1993/2914 | |
dc.language.iso | eng | en_US |
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dc.rights | open access | en_US |
dc.status | Peer reviewed | en |
dc.subject | Ca2+ | en |
dc.subject | RyR | en |
dc.subject | SERCA | en |
dc.subject | cell nucleus | en |
dc.subject | FK506 | en |
dc.subject | thapsigargin | en |
dc.subject | ryanodine | en |
dc.subject | INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR | en |
dc.subject | RYANODINE RECEPTOR | en |
dc.subject | CA2+ CHANNELS | en |
dc.subject | SARCOPLASMIC-RETICULUM | en |
dc.subject | ENDOPLASMIC-RETICULUM | en |
dc.subject | NUCLEAR CA2+ | en |
dc.subject | FK506-BINDING PROTEIN | en |
dc.subject | SKELETAL-MUSCLE | en |
dc.subject | RELEASE CHANNEL | en |
dc.subject | CYTOSOLIC CA2+ | en |
dc.title | RyR1/SERCA1 cross-talk regulation of calcium transport in heavy sarcoplasmic reticulum vesicles | en |
dc.type | journal article | en_US |