Activation of the skeletal muscle Ca2+ release channel by the triazine dyes Cibacron Blue F3A-G and reactive Red 120

Xu, Le; Jones, Rodney V.; Meissner, Gerhard

doi:10.1016/0003-9861(89)90476-1

Cited by 5 publications

(6 citation statements)

References 36 publications

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“…When microsomes were challenged with either NAADP (2 μ M ) or RR120 (100 μ M ), a similar amount of Ca 2+ release was evoked. It has been previously shown that RR120 and Reactive Blue 2 are capable of activating the ryanodine receptor ( Xu et al ., 1989 ) and that Reactive Blue 2 is capable of inducing Ca 2+ oscillations in HeLa cells ( Okuda et al ., 2001 ). Furthermore, CB and Patent blue have been shown to compete for IP 3 binding in rat liver ( Bootman et al ., 1990 ) Therefore, further analysis was required to prove whether NAADP and RR120 released Ca 2+ via the same mechanism.…”

Section: Resultsmentioning

confidence: 99%

“…This is substantiated by the residual Ca 2+ release induced by RR120 when NAADP receptors are inactivated (Figure 2). Although it has been previously shown that in other systems these dyes activate the ryanodine receptor ( Xu et al ., 1989 ), the absence of a reduction in the Ca 2+ release in the presence of ruthenium red suggests that the ryanodine receptors in the sea urchin egg are not activated by RR120. Furthermore, similar data obtained with heparin would also seem to exclude the possibility that RR120 can activate IP 3 receptors, as has been shown for other triazine dyes ( Bootman et al ., 1990 ).…”

Section: Discussionmentioning

confidence: 99%

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Triazine dyes are agonists of the NAADP receptor

Billington

Bak

Martínez-Coscollá

et al. 2004

British J Pharmacology

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1 NAADP has been shown to be a potent calcium-releasing second messenger in a wide variety of cell types to date. However, research has been hampered by a lack of pharmacological agents, with which to investigate NAADP-induced calcium release, and by the molecular identity of its cellular target protein being unknown. 2 In the present paper, the sea urchin egg model was used to investigate whether triazine dyes, which can act as nucleotide mimetics, can bind to the NAADP receptor, induce Ca 2 þ release and be used for affinity chromatography of the receptor. 3 Indeed, all the triazine dyes tested (Reactive Red 120 (RR120), Reactive Green 19 (RG19), Reactive Green 5 (RG5), Cibacron Blue 3GA and Reactive Yellow 86) displayed micromolar affinities, except for Reactive Orange 14. Furthermore, unlike NAADP, RR120, RG19 and RG5 did not bind in an irreversible manner. 4 The compound that displayed the highest affinity, RR120, was tested in a 45 Ca 2 þ efflux assay. This compound released Ca 2 þ via the NAADP receptor, as shown by the ability of subthreshold NAADP concentrations to inhibit this release. Furthermore, heparin and ruthenium red were unable to block RR120-induced Ca 2 þ release. 5 We have also shown that RG5 and RG19, immobilised on resins, retain the ability to bind to the receptor, and that this interaction can be disrupted by high salt concentrations. As a proof of principle, we have shown that this can be used to partially purify the NAADP receptor by at least 75-fold. 6 In conclusion, triazine dyes interact with the NAADP receptor, and this could be exploited in future to create a new generation of pharmacological tools to investigate this messenger and, in combination with other techniques, to purify the receptor.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Triazine dyes are agonists of the NAADP receptor

Billington

Bak

Martínez-Coscollá

et al. 2004

British J Pharmacology

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“…CB (Xu et al, 1989) and other anthraquinone-based compounds (Abramson et al, 1988) have been shown to interact with sarcoplasmic reticulum calcium channels, causing release of stored calcium. Calcium plays a central regulatory role in the functional life of the sperm cell.…”

Section: Discussionmentioning

confidence: 99%

“…13.3% (mean 5 S.D., n = 3). cium channel (Xu et al, 1989). Since bovine sperm motility and adenyl cyclase activity are both sensitive to calcium, the effect of calcium on the ability of CB-V to stimulate sperm metabolism was tested.…”

Section: Effect Of External Calcium On Cb-v Stimulationmentioning

confidence: 99%

“…Attachment of CB to agarose or similar nonreactive substrates has produced versatile affinity adsorbents for the purification of nucleotide-binding enzymes (Clonis, 1990). The dye has also been studied as an effector of calcium channel activity in sarcoplasmic reticulum (Xu et al, 1989). Here we report that CB stimulated motility and oxida- …”

Section: Introductionmentioning

confidence: 99%

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Stimulation of bovine sperm motility and respiration by the triazine dye cibacron blue F3GA

Schoff

First

1995

Molecular Reproduction Devel

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Bovine sperm motility and respiration were stimulated by the triazine dye Cibacron Blue F3GA (CB), which may operate as a nucleotide mimic. CB stimulation of respiration was half-maximal at about 35 microM and respiration reached maximal levels about 1.5 minutes after CB addition. Respiratory stimulation was preceded by a transient increase in cytosolic cAMP. Sperm cAMP titers were elevated from 5 to 10 pmoles/10(8) cells within 30 seconds of CB addition, but rapidly dropped to a stable level of about 7.5 pmoles/10(8) cells. CB was a potent inhibitor of sperm membrane adenylyl cyclase and inhibited respiration in permeabilized cells. Taken together, the data indicated that CB stimulation was not manifested via the cytosol. In addition, a nonpermeant blue dextran preparation synthesized with CB also stimulated sperm respiration and motility. CB inhibited sperm membrane phosphodiesterase activity, suggesting that the transient pulse of cAMP resulted from CB interaction with this enzyme in the sperm membrane.

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Modulation of ricin toxicity in mice by biologically active substances

Muldoon

Stohs

1994

J of Applied Toxicology

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Ricin is a highly toxic protein produced by the castor bean (Ricinus communis). It is one of various protein toxins that consist of two subunits joined by a disulfide bridge. One chain facilitates entry of the toxin into the cell while the other chain exhibits RNA N-glycosidase activity, which attacks a specific site on 28S rRNA, preventing polypeptide elongation and leading to cell death. Although ricin and other protein toxins are potential health hazards, no antidote against these toxins exists. Thus, a number of selected compounds were screened for their ability to alter ricin lethality in mice, based on percentage survival and time to death following a ricin LD100 of 25 micrograms kg-1 i.p. While no compound tested prevented lethality, dexamethasone and difluoromethylornithine (DFMO) significantly extended survival time. The effects of DFMO on ricin toxicity were markedly influenced by altering various pharmacokinetic parameters. The antioxidants butylated hydroxyanisole and vitamin E succinate also extended survival time in response to a lethal dose of ricin, but to a lesser extent than did dexamethasone and DFMO. The Golgi apparatus inhibitors monensin, swainsonine and tunicamycin enhanced ricin toxicity, as evidenced by shortened survival times. In addition, various nucleoside analogs, including acyclovir and trifluridine as well as adenosine, guanosine and dibutyryl cyclic AMP, also potentiated the toxicity of ricin. The results demonstrate that the toxicity of ricin is modulated by a wide variety of structurally distinct chemicals and may involve different mechanisms. Furthermore, the extent and direction of the modulation of ricin toxicity is highly dependent upon pharmacokinetic variables, including dose and dosing interval.

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Activation of the skeletal muscle Ca2+ release channel by the triazine dyes Cibacron Blue F3A-G and reactive Red 120

Cited by 5 publications

References 36 publications

Triazine dyes are agonists of the NAADP receptor

Triazine dyes are agonists of the NAADP receptor

Stimulation of bovine sperm motility and respiration by the triazine dye cibacron blue F3GA

Modulation of ricin toxicity in mice by biologically active substances

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