Synthesis and characterization of antagonists of cyclic-ADP-ribose-induced Ca2+ release

Walseth, Timothy F.; Lee, Hon Cheung

doi:10.1016/0167-4889(93)90199-y

Cited by 267 publications

(211 citation statements)

References 18 publications

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“…The effect of β-NAD + was antagonized by 8-Br-cADPR, which eliminates the ability of cADPR to activate Ca# + release [22], or by nicotinamide, which inhibits ADP-ribosyl cyclase activitiy [24]. Since ADPR has no facilitating effect, the action of β-NAD + seems to be mediated by cADPR [23,24], after conversion of β-NAD + to cADPR by ADP-ribosyl cyclase in NG108-15 cells.…”

Section: Scheme 1 Models For Reciprocal Interactions Between Ryrs Andmentioning

confidence: 99%

“…To confirm that the β-NAD + -induced potentiation of [Ca# + ] i elevation is mediated through its conversion to cADPR, 8-BrcADPR, a cADPR competitor [22], was used. [Ca# + ] i at 0 mV in cells injected with both 100 µM β-NAD + and 10 µM 8-BrcADPR was 159p8 % (n l 4) of the value at k40 mV ( Figure 3B).…”

Section: Effect Of β-Nad + On [Ca 2 + ] I Increases Produced Via Nifementioning

confidence: 99%

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cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

Hashii

Minabe

Higashida

2000

Biochemical Journal

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The effects of cADP-ribose (cADPR), a metabolite of β-NAD + , on the elevation of cytoplasmic free Ca# + concentration ([Ca# + ] i ) and Ca# + influx through voltage-activated Ca# + channels (VACCs) were studied in NG108-15 neuroblastomaiglioma hybrid cells. NG108-15 cells were pre-loaded with fura-2 and whole-cell patch-clamped. Application of cADPR through patch pipettes did not by itself trigger any [Ca# + ] i rise at the resting membrane potential. A rise in [Ca# + ] i was evoked upon sustained membrane depolarization, and was significantly larger in cADPR-infused cells than in non-infused cells. This potentiation in the [Ca# + ] i elevation was reproduced by infusion of β-NAD + , and was blocked by 8-bromo-cADPR and antagonized by external application of ryanodine or by pretreatment of cells with FK506. Nicotinamide inhibited β-NAD + -induced, but not cADPR-elicited, potentiation. [Ca# + ] i increases or Ca# + influx,

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Section: Scheme 1 Models For Reciprocal Interactions Between Ryrs Andmentioning

confidence: 99%

Section: Effect Of β-Nad + On [Ca 2 + ] I Increases Produced Via Nifementioning

confidence: 99%

cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

Hashii

Minabe

Higashida

2000

Biochemical Journal

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“…4,5-Diaminofluorescein diacetate (DAF-2 DA), 3-amino-4-aminomethyl-2Ј,7Ј-difluorofluorescein diacetate (DAF-FM DA), sodium nitroprusside, and adenosine cyclic 3Ј,5Ј-monophosphorothioate, R p isomer ((R p )-cAMP-S) were purchased from Calbiochem. 8-Bromo-cADPR was synthesized as described previously (36). All other chemicals were from Sigma.…”

Section: P]nadmentioning

confidence: 99%

The NO Pathway Acts Late during the Fertilization Response in Sea Urchin Eggs

Leckie

Empson

Becchetti

et al. 2003

Journal of Biological Chemistry

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Both the inositol 1,4,5-trisphosphate (InsP 3 ) and ryanodine receptor pathways contribute to the Ca 2؉ transient at fertilization in sea urchin eggs. To date, the precise contribution of each pathway has been difficult to ascertain. Evidence has accumulated to suggest that the InsP 3 receptor pathway has a primary role in causing Ca 2؉ release and egg activation. However, this was recently called into question by a report implicating NO as the primary egg activator. In the present study we pursue the hypothesis that NO is a primary egg activator in sea urchin eggs and build on previous findings that an NO/cGMP/cyclic ADP-ribose (cADPR) pathway is active at fertilization in sea urchin eggs to define its role. Using a fluorescence indicator of NO levels, we have measured both NO and Ca 2؉ at fertilization and establish that NO levels rise after, not before, the Ca 2؉ wave is initiated and that this rise is Ca 2؉ -dependent. By inhibiting the increase in NO at fertilization, we find not that the Ca 2؉ transient is abolished but that the duration of the transient is significantly reduced. The latency and rise time of the transient are unaffected. This effect is mirrored by the inhibition of cGMP and cADPR signaling in sea urchin eggs at fertilization. We establish that cADPR is generated at fertilization, at a time comparable to the time of the rise in NO levels. We conclude that NO is unlikely to be a primary egg activator but, rather, acts after the initiation of the Ca 2؉ wave to regulate the duration of the fertilization Ca 2؉ transient.

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“…Since to date there is no total chemical synthesis of cADPR (although fl-NAD ÷ has been cyclised chemically using NaBr in dimethyl sulphoxide to yield cADPR [13]), we, like others [14], have relied upon a chemo-enzymatic approach both to prepare cADPR itself and to generate structural diversity (Fig. 3) [15].…”

Section: Introductionmentioning

confidence: 99%

Cyclic aristeromycin diphosphate ribose: A potent and poorly hydrolysable Ca²⁺‐mobilising mimic of cyclic adenosine diphosphate ribose

et al. 1996

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Cyclic aristeromycin diphosphate ribose, a carbocyclic analogue of cyclic adenosine diphosphate ribose, was syntbesised using a chemo-enzymatic route involving activation of aristeromycin 5'-phosphate by diphenyl phosphochloridate. The calcium-releasing properties of this novel analogue were investigated in sea urchin egg homogenates. While cyclic aristeromycin diphosphate ribose has a calcium release profile similar to that of cyclic adenosine diphosphate ribose (ECso values are 80 nM and 30 riM, respectively), it is degraded significantly more slowly (tu2 values are 170 rain and 15 rain, respectively) and may, therefore, be a useful tool to investigate the activities of cyclic adenosine diphosphate ribose.

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Synthesis and characterization of antagonists of cyclic-ADP-ribose-induced Ca2+ release

Cited by 267 publications

References 18 publications

cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

The NO Pathway Acts Late during the Fertilization Response in Sea Urchin Eggs

Cyclic aristeromycin diphosphate ribose: A potent and poorly hydrolysable Ca²⁺‐mobilising mimic of cyclic adenosine diphosphate ribose

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Synthesis and characterization of antagonists of cyclic-ADP-ribose-induced Ca2+ release

Cited by 267 publications

References 18 publications

cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

cADP-ribose potentiates cytosolic Ca2+ elevation and Ca2+ entry via L-type voltage-activated Ca2+ channels in NG108-15 neuronal cells

The NO Pathway Acts Late during the Fertilization Response in Sea Urchin Eggs

Cyclic aristeromycin diphosphate ribose: A potent and poorly hydrolysable Ca2+‐mobilising mimic of cyclic adenosine diphosphate ribose

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Cyclic aristeromycin diphosphate ribose: A potent and poorly hydrolysable Ca²⁺‐mobilising mimic of cyclic adenosine diphosphate ribose