cADP-ribose releases Ca2+ from cardiac sarcoplasmic reticulum independently of ryanodine receptor

Lahouratate, Philippe; Guibert, J.; Faivré, Jean-François

doi:10.1152/ajpheart.1997.273.3.h1082

Cited by 16 publications

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“…This fact and responsiveness of permeabilized 3T3 cells to cADPR seem to imply the occurrence in these cells of an unidentified type of cADPR receptor. In this respect, a recent report provides evidence for cADPRinduced, ryanodine receptor-independent calcium release from dog cardiac sarcoplasmic reticulum (37).…”

Section: Discussionmentioning

confidence: 97%

Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Zocchi

Daga²,

Usai

et al. 1998

Journal of Biological Chemistry

119

161

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CD38 is a bifunctional ectoenzyme, predominantly expressed on hematopoietic cells during differentiation, that catalyzes the synthesis (cyclase) and the degradation (hydrolase) of cyclic ADP-ribose (cADPR), a powerful calcium mobilizer from intracellular stores. Due to the well established role of calcium levels in the regulation of apoptosis, proliferation, and differentiation, the CD38/cADPR system seems to be a likely candidate involved in the control of these fundamental processes. CD38 is a type II transmembrane glycoprotein predominantly expressed on lymphocytes (1) but also present in a number of different cell types, including erythrocytes (2), hematopoietic progenitor cells (1), ␤-pancreatic cells (3), and cerebral (4) and cerebellar (5) neurons. Immunologically, CD38 can be defined as an "orphan receptor" since its binding by specific monoclonal antibodies directed against ectocellular epitopes elicits cellular responses in lymphocytes, including proliferation, activation, and rescue from apoptosis (6, 7). The signal transduction pathways implicated in these events are under study, but phosphorylation/dephosphorylation reactions of target kinases have been already demonstrated (6,8,9). Biochemically, CD38 is a bifunctional ectoenzyme that catalyzes the synthesis of cADPR 1 from NAD ϩ and also its hydrolysis to ADPR (2, 10). Cyclic ADPR is a potent Ca 2ϩ mobilizer from intracellular stores, in invertebrate as well as in mammalian cells (11), and its presence has been described in most mammalian tissues (12).The widespread tissue distribution of the CD38/cADPR system suggests its involvement in the control of pivotal Ca 2ϩ -controlled functions like contraction, secretion, cell proliferation/differentiation, and apoptosis. However, the topological paradox of the ectocellular production of an intracellular Ca 2ϩ mobilizer has raised questions on both the immunological and the biochemical functions of the CD38/cADPR system (13, 14). Cell death has been advocated as a means for local increase in extracellular NAD ϩ concentrations, sufficient to elicit the production of cADPR by the ectoenzyme CD38; in this respect, nanomolar concentrations of NAD ϩ have been detected in plasma (15) and cerebellar interstitial fluid (5) suggesting the theoretical possibility of an extracellular production of cADPR by CD38 "in vivo." In few selected cell systems, i.e. murine B-lymphocytes (10), rat cerebellar granule cells (5), and rat osteoclasts (16), extracellular, exogenously added cADPR was demonstrated to elicit functional responses in intact cells, but most reported effects of cADPR on cellular functions require permeabilization of target cells to ensure binding of the nucleotide to its intracellular receptor(s).Internalization of membrane-bound CD38, as observed in human Namalwa B-lymphocytes upon incubation with NAD ϩ or thiol reagents, is followed by an increase of intracellular cyclase activity (insensitive to protein synthesis inhibitors) and of intracellular cADPR concentration ([cADPR] i ) (17), suggesting that...

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Section: Discussionmentioning

confidence: 97%

Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Zocchi

Daga²,

Usai

et al. 1998

Journal of Biological Chemistry

119

161

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“…In some tissues cADPR might release Ca 2+ by a pathway which involves atypical RyR or does not involve RyR at all. For example, the release of Ca 2+ by cADPR was not prevented by depletion of the caffeine-sensitive store or by conventional RyR antagonists, and was inhibited by the InsP3 receptor blocker heparin (Morrissette et al, 1993;Thorn et al, 1994;Kannan et al, 1996;Lahouratate et al, 1997;Prakash et al, 2000). Indeed cADPR might interact with all isoforms of the InsP3 receptor, stimulate InsP3 binding to the type 1 InsP3 receptor (Vanlingen et al, 2001) or inhibit InsP3-mediated Ca 2+ release (Missiaen et al, 1998).…”

Section: Effect Of Cadpr On [Ca 2+ ]C Declinementioning

confidence: 99%

Cyclic ADP-ribose increases Ca2+ removal in smooth muscle

Bradley

Currie

MacMillan

et al. 2003

Journal of Cell Science

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Ca2+ release via ryanodine receptors (RyRs) is vital in cell signalling and regulates diverse activities such as gene expression and excitation-contraction coupling. Cyclic ADP ribose (cADPR), a proposed modulator of RyR activity, releases Ca2+ from the intracellular store in sea urchin eggs but its mechanism of action in other cell types is controversial. In this study, caged cADPR was used to examine the effect of cADPR on Ca2+ signalling in single voltage-clamped smooth muscle cells that have RyR but lack FKBP12.6, a proposed target for cADPR. Although cADPR released Ca2+ in sea urchin eggs (a positive control), it failed to alter global or subsarcolemma [Ca2+]c, to cause Ca2+-induced Ca2+ release or to enhance caffeine responses in colonic myocytes. By contrast, caffeine (an accepted modulator of RyR) was effective in these respects. The lack of cADPR activity on Ca2+ release was unaffected by the introduction of recombinant FKBP12.6 into the myocytes. Indeed in western blots, using brain membrane preparations as a source of FKBP12.6, cADPR did not bind to FKBPs, although FK506 was effective. However, cADPR increased and its antagonist 8-bromo-cADPR slowed the rate of Ca2+ removal from the cytoplasm. The evidence indicates that cADPR modulates [Ca2+]c but not via RyR; the mechanism may involve the sarcolemma Ca2+ pump

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“…These results provide direct evidence that cADPR activates RyR and therefore may serve as an endogenous activator or modulator of the RyR in these VSMCs. However, there is evidence indicating that cADPR releases Ca 2+ independently of RyR in neurons and cells from the myocardium and other smooth muscle [69][70][71]. The reason for these discrepancies remains unknown.…”

Section: Direct Action On Ca 2+ Release Via Ryr Activationmentioning

confidence: 99%

Vascular physiology of a Ca²⁺mobilizing second messenger - cyclic ADP - ribose

Zhang

2006

Journal of Cellular and Molecular Medicine

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Cyclic ADP-ribose (cADPR) is a novel Ca 2+ mobilizing second messenger, which is capable of inducing Ca 2+ release from the sarcoplasmic reticulum (SR) via activation of ryanodine receptors (RyR) in vascular cells. This signaling nucleotide has also been reported to participate in generation or modulation of intracellular Ca 2+ sparks, Ca 2+ waves or oscillations, Ca 2+ -induced Ca 2+ release (CICR) and spontaneous transient outward currents (STOCs) in vascular smooth muscle cells (VSMCs). With respect to the role of cADPR-mediated signaling in mediation of vascular responses to different stimuli, there is accumulating evidence showing that cADPR is importantly involved in the Ca 2+ response of vascular endothelial cells (ECs) and VSMCs to various chemical factors such as vasoactive agonists acetylcholine, oxotremorine, endothelin, and physical stimuli such as stretch, electrical depolarization and sheer stress. This cADPR-RyR-mediated Ca 2+ signaling is now recognized as a fundamental mechanism regulating vascular function. Here we reviewed the literature regarding this cADPR signaling pathway in vascular cells with a major focus on the production of cADPR and its physiological roles in the control of vascular tone and vasomotor response. We also summarized some publish results that unveil the underlying mechanisms mediating the actions of cADPR in vascular cells. Given the importance of Ca 2+ in the regulation of vascular function, the results summarized in this brief review will provide new insights into vascular physiology and circulatory regulation.

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cADP-ribose releases Ca2+ from cardiac sarcoplasmic reticulum independently of ryanodine receptor

Cited by 16 publications

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Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Cyclic ADP-ribose increases Ca2+ removal in smooth muscle

Vascular physiology of a Ca²⁺mobilizing second messenger - cyclic ADP - ribose

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cADP-ribose releases Ca2+ from cardiac sarcoplasmic reticulum independently of ryanodine receptor

Cited by 16 publications

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Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Expression of CD38 Increases Intracellular Calcium Concentration and Reduces Doubling Time in HeLa and 3T3 Cells

Cyclic ADP-ribose increases Ca2+ removal in smooth muscle

Vascular physiology of a Ca2+mobilizing second messenger - cyclic ADP - ribose

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Vascular physiology of a Ca²⁺mobilizing second messenger - cyclic ADP - ribose