An ultrasensitive method for the simultaneous determination of cyclic AMP and cyclic GMP in small-volume samples from blood and tissue

Honma, Mamoru; Satoh, Tomokazu; Takezawa, Junichi; Ui, Michio

doi:10.1016/0006-2944(77)90060-6

Cited by 678 publications

(161 citation statements)

References 16 publications

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“…The results obtained with these substances from different origins, however, were the same. We concluded, therefore, that dbcGMP ac These results, however, are not decisive since there is a possibility that dbcGMP and mono butyryl cyclic GMP in both the intracellular and extracellular spaces may cross-react with cyclic GMP-antiserum and disturb the determination (23).…”

Section: Discussionmentioning

confidence: 72%

Failure of dibutyryl and 8-bromo-cyclic gmp to mimic the antagonistic action of carbachol on the positive inotropic effects of sympathomimetic amines in the canine isolated ventricular myocardium

Endoh

Shimizu

1979

Japanese Journal of Pharmacology

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Abstract-Effects of carbachol, dbcGMP and 8-bromo-cyclic GMP on the positive inotropic actions of sympathomimetic amines and dbcAMP were studied on the canine isolated right ventricular myocardium.Carbachol alone did not substantially change the developed tension of the muscle, but did markedly shift the dose response curve for isoprenaline on the developed tension to the right and depressed the maximal response to the drug in a concentration dependent manner. The positive inotropic action of phenylephrine was affected by carbachol in the same manner as that of isoprenaline. DbcGMP in concentrations of 10-3 M and higher produced a significant increase in the developed tension. The positive inotropic action of dbcGMP was partly inhibited by a Q-adrenoceptor blocking agent, pindolol. In the presence of dbcGMP, isoprenaline produced an action similar to that seen in the control experiment, but this action was not maintained on such a steady level as in the control.This rapid decline of the effect of isoprenaline in the presence of dbcGMP was prevented by adding ascorbic acid to the organ bath. The positive inotropic actions of phenylephrine and of dbcAMP were not substantially affected by dbcGMP.8-Bromo-cyclic GMP in a concentration of 10-' M did not change either the basal developed tension or the positive inotropic actions of noradrenaline and of isoprenaline.The present results indicate that these cyclic GMP derivatives are not able to mimic the antagonistic action of cholinergic stimulation on the positive inotropic action of adrenergic stimulation on the canine ventricular myocardium.

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Section: Discussionmentioning

confidence: 72%

Failure of dibutyryl and 8-bromo-cyclic gmp to mimic the antagonistic action of carbachol on the positive inotropic effects of sympathomimetic amines in the canine isolated ventricular myocardium

Endoh

Shimizu

1979

Japanese Journal of Pharmacology

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“…Trichloroacetic acid in the supernatant was extracted twice with 2 ml of diethyl ether saturated with distilled water, and the extracted solution was used for the CAMP assay. CAMP content was measured by the radioimmunoassay method with a Yamasa CAMP assay kit as reported by Honma et al [9].…”

Section: Cyclic Amp Measurementmentioning

confidence: 99%

Adenosine 3′,5′‐cyclic monophosphate (cAMP) inhibits phorbol ester‐induced growth of an IL‐2‐dependent T cell line

1988

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We previously established a human T cell line, TPA‐Mat, which can proliferate in response to not only interleukin‐2 (IL‐2), but also phorbol esters such as 12‐O‐tetradecanoylphorbol‐13‐acetate (TPA) and phorbol‐12,13‐dibutyrate (PDBu). The present study demonstrated that the PDBu‐dependent growth of TPA‐Mat cells was inhibited up to 90% by adenosine 3′,5′‐cyclic monophosphate (cAMP) raising agents such as forskolin, cholera toxin and 1‐methyl‐3‐isobutylxanthine, and cAMP analogues, whereas the IL‐2‐stimulated TPA‐Mat growth was slightly inhibited. These findings suggest that the signal transduction pathway of PDBu‐induced growth, which should involve activation of protein kinase C, is sensitive to cAMP, and that it cannot be exactly identical to the signal transduction pathway of Il‐2‐induced growth in TPA‐Mat cells.

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“…After the medium was collected to measure arachidonic acid release, the cells were extracted with 500 ,ul of 0.2 M HCl. The cAMP content in the acid extract was measured by a specific radioimmunoassay as described previously [14]. Results are expressed as nmol/100 mg of cellular protein.…”

Section: Measurement Of Camp Accumulationmentioning

confidence: 99%

Permissive stimulation of Ca(2+)-induced phospholipase A2 by an adenosine receptor agonist in a pertussis toxin-sensitive manner in FRTL-5 thyroid cells: a new ‘cross-talk’ mechanism in Ca2+ signalling.

Shimegi

Okajima

Kondo

1994

Biochemical Journal

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We have described the pertussis toxin (PTX)-sensitive potentiation of P2-purinergic agonist-induced phospholipase C activation, Ca2+ mobilization and arachidonic acid release by an adenosine receptor agonist, N6-(L-2-phenylisopropyl)adenosine (PIA), which alone cannot influence any of these cellular activities [Okajima, Sato, Nazarea, Sho and Kondo (1989) J. Biol. Chem. 264, 13029-13037]. In the present study we have found that arachidonic acid release was associated with lysophosphatidylcholine production, and conclude that arachidonic acid is produced by phospholipase A2 in FRTL-5 thyroid cells. This led us to assume that PIA augments P2-purinergic arachidonic acid release by increasing [Ca2+]i which, in turn, activates Ca(2+)-sensitive phospholipase A2. The arachidonic acid-releasing response to PIA was, however, always considerably higher (3.1-fold increase) than the Ca2+ response (1.3-fold increase) to the adenosine derivative. In addition, arachidonic acid release induced by the [Ca2+]i increase caused by thapsigargin, an endoplasmic-reticulum Ca(2+)-ATPase inhibitor, or calcium ionophores was also potentiated by PIA without any effect on [Ca2+]i and phospholipase C activity. This action of PIA was also PTX-sensitive, but not affected by the forskolin- or cholera toxin-induced increase in the cellular cyclic AMP (cAMP), suggesting that a PTX-sensitive G-protein(s) and not cAMP mediates the PIA-induced potentiation of Ca(2+)-generated phospholipase A2 activation. Although acute phorbol ester activation of protein kinase C induced arachidonic acid release, P2-purinergic and alpha 1-adrenergic stimulation of arachidonic acid release was markedly increased by the protein kinase C down-regulation caused by the phorbol ester. This suggests a suppressive role for protein kinase C in the agonist-induced activation of arachidonic acid release. We conclude that PIA (and perhaps any of the G1-activating agonists) augments an agonist (maybe any of the Ca(2+)-mobilizing agents)-induced arachidonic acid release by activation of Ca(2+)-dependent phospholipase A2 in addition to enhancement of agonist-induced phospholipase C followed by an increase in [Ca2+]i.

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An ultrasensitive method for the simultaneous determination of cyclic AMP and cyclic GMP in small-volume samples from blood and tissue

Cited by 678 publications

References 16 publications

Failure of dibutyryl and 8-bromo-cyclic gmp to mimic the antagonistic action of carbachol on the positive inotropic effects of sympathomimetic amines in the canine isolated ventricular myocardium

Failure of dibutyryl and 8-bromo-cyclic gmp to mimic the antagonistic action of carbachol on the positive inotropic effects of sympathomimetic amines in the canine isolated ventricular myocardium

Adenosine 3′,5′‐cyclic monophosphate (cAMP) inhibits phorbol ester‐induced growth of an IL‐2‐dependent T cell line

Permissive stimulation of Ca(2+)-induced phospholipase A2 by an adenosine receptor agonist in a pertussis toxin-sensitive manner in FRTL-5 thyroid cells: a new ‘cross-talk’ mechanism in Ca2+ signalling.

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