Functional properties of the ryanodine receptor type3 (RyR3) Ca2+ release channel

Sonnleitner, Alois; Conti, Antonio; Bertocchini, Federica; Schindler, Hansgeorg; Sorrentino, Vincenzo

doi:10.1093/emboj/17.10.2790

Cited by 116 publications

(95 citation statements)

References 55 publications

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“…14) but not Jurkat cell Ca 2ϩ uptake is also consistent with properties of the ryanodine receptor. The skeletal muscle ryanodine receptor is known to be Ca 2ϩ -sensitive at high concentrations, but the RyR3 is not (36). These facts are, thus, consistent with the ryanodine receptor serving as the other half of the dual-channel uptake for Ca 2ϩ into the ER as proposed here.…”

Section: Complications Of the Existing Cce Models-supporting

confidence: 89%

A Direct Mass-action Mechanism Explains Capacitative Calcium Entry in Jurkat and Skeletal L6 Muscle Cells

Narayanan

Islam

Bartelt

et al. 2003

Journal of Biological Chemistry

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We examined capacitative calcium entry (CCE) in Jurkat and in L6 skeletal muscle cells. We found that extracellular Ca 2؉ can enter the endoplasmic reticulum (ER) of both cell types even in the presence of thapsigargin, which blocks entry into the ER from the cytosol through the CaATPase. Moreover, extracellular Ca 2؉ entry into the ER was evident even when intracellular flow of Ca 2؉ was in the direction of ER to cytosol due to the presence of caffeine. ER Ca 2؉ content was assessed by two separate means. First, we used the Mag-Fura fluorescent dye, which is sensitive only to the relatively high concentrations of Ca 2؉ found in the ER. Second, we transiently expressed an ER-targeted derivative of aequorin, which reports Ca 2؉ by luminescence. In both cases, the Ca 2؉ concentration in the ER increased in response to extracellular Ca 2؉ after the ER had been previously depleted despite blockade by thapsigargin. We found two differences between the Jurkat and L6 cells. L6, but not Jurkat cells, inhibited Ca 2؉ uptake at very high Ca 2؉ concentrations. Second, ryanodine receptor blockers inhibited the appearance of cytosolic Ca 2؉ during CCE if added before Ca 2؉ in both cases, but the L6 cells were much more sensitive to ryanodine. Both of these can be explained by the known difference in ryanodine receptors between these cell types. These findings imply that the origin of cytosolic Ca 2؉ during CCE is the ER. Furthermore, kinetic data demonstrated that Ca 2؉ filled the ER before the cytosol during CCE. Our results suggest a plasma membrane Ca 2؉ channel and an ER Ca 2؉ channel joined in tandem, allowing Ca 2؉ to flow directly from the extracellular space to the ER. This explains CCE; any decrease in ER [Ca 2؉ ] relative to extracellular [Ca 2؉ ] would provide the gradient for refilling the ER through a mass-action mechanism.Ca 2ϩ is a critical regulator for a large number of cells, and it is known that for many, the key signaling event is the release of this ion from the ER 1 (1, 2). After release most of the Ca 2ϩ is re-sequestered to the ER through the CaATPase, although some is lost through the plasma membrane to the cell exterior. Maintaining the ER pool of Ca 2ϩ requires re-entry from outside the cell. Casteels and Droogmans (3) first reported a correlation between depletion of ER [Ca 2ϩ ] and entry of Ca 2ϩ from extracellular sources into the cell. This phenomenon was then extensively studied by Putney (4) and named "store-operated" or capacitative calcium entry (CCE).The mechanism for CCE remains unknown, although two general models have been proposed. One, borrowed from the known association of the skeletal muscle plasma membrane potential sensor (L channel) and ER protein (ryanodine receptor), posits a direct connection in which Ca 2ϩ depletion within the ER is sensed by an ER protein, transmitted by proteinprotein interaction to the plasma membrane protein, which then allows entry of Ca 2ϩ into the cytosol. A second, based on second messenger signaling systems such as that for cyclic AMP, posits a mess...

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Section: Complications Of the Existing Cce Models-supporting

confidence: 89%

A Direct Mass-action Mechanism Explains Capacitative Calcium Entry in Jurkat and Skeletal L6 Muscle Cells

Narayanan

Islam

Bartelt

et al. 2003

Journal of Biological Chemistry

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“…As stated previously, mouse parotid acinar cells express predominantly RyR 3 (62), whereas rat parotid acinar cells (revealed by reverse transcription-PCR) express predominantly RyR 1 (21). Because RyR 1 exhibit a lower threshold for activation by Ca 2ϩ (63), any potentiation of Ca 2ϩ release by cAMP would be amplified under conditions of elevated resting [Ca 2ϩ ] i (18,21,22). Such species differences could also explain the lack of effect of caffeine in mouse acinar cells, as RyR 3 are thought to be caffeineinsensitive (64,65).…”

Section: Discussionmentioning

confidence: 75%

Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors in Parotid Acinar Cells

Bruce

Shuttleworth

Giovannucci

et al. 2002

Journal of Biological Chemistry

139

142

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“…Other studies suggest that RyR2 may not be affected by cyclic ADP ribose (Fruen et al, 1994). In some studies (Chen et al, 1997b;Sonnleitner et al, 1998) cyclic ADP ribose did not affect RyR3 but in others an effect was observed. It is possible that activation by cyclic ADP-ribose depends on the presence of calmodulin andlor phosphorylation by Ca~lcalmodulin dependent kinase, as is the case for RyRs in sea urchins eggs and rat pancreatic islets (Lee et al, 1994;Tanaka and Tashjian, 1995;Takasawa et al, 1995).…”

Section: Modulation Of Ryanodine Receptorsmentioning

confidence: 96%

Complex interactions between skeletal muscle ryanodine receptor and dihydropyridine receptor proteins

Leong¹,

MacLennan²

1998

Biochem. Cell Biol.

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Evidence for functional interactions between the Ca2+ release channel in the skeletal muscle sarcoplasmic reticulum (the ryanodine receptor) and the L-type Ca2+ channel in the sarcolemma (the dihydropyridine receptor), leading to excitation-contraction coupling, is reviewed and experimental systems used to identify candidate sites of interaction are outlined.Key words: sarcoplasmic reticulum, excitation-contraction coupling.

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Functional properties of the ryanodine receptor type3 (RyR3) Ca2+ release channel

Cited by 116 publications

References 55 publications

A Direct Mass-action Mechanism Explains Capacitative Calcium Entry in Jurkat and Skeletal L6 Muscle Cells

A Direct Mass-action Mechanism Explains Capacitative Calcium Entry in Jurkat and Skeletal L6 Muscle Cells

Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors in Parotid Acinar Cells

Complex interactions between skeletal muscle ryanodine receptor and dihydropyridine receptor proteins

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