Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.13.12.5 (aequorin)
 1,451 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Effects of beta-adrenoceptor stimulation on intracellular Ca2+ transients and tension were explored in rat ventricular muscles injected with aequorin. Adrenaline (0.05-5.0 microM) and isoproterenol (0.05-1.0 microM) increased the peak of twitch tension and accelerated relaxation. The former effect depended on Ca2+ concentration in Tyrode's solution ([Ca2+]o) and the stage of the experiment. Low concentrations of these drugs added to normal Tyrode's solution containing 2 mM [Ca2+]o did not potentiate twitch tension in the early stage of the experiments. These drugs increased the peak of the aequorin light signal and slightly accelerated the falling phase of the light especially the tail. Effects of dibutyryl-cyclic AMP (DB-cAMP)(0.1-5.0 mM) and 3-isobutyl-1-methylxanthine (IBMX) (0.01-0.5 mM) were qualitatively similar to those of adrenaline and isoproterenol. Isoproterenol applied at the peak of Na-deficient contracture decreased tension without significantly changing the light signal; similar results were obtained in the presence of ryanodine (1 microM). The results were interpreted as follows: The increase of intracellular cAMP induced by beta-adrenoceptor stimulation facilitated Ca2+ uptake by sarcoplasmic reticulum (SR) and decreased Ca2+ sensitivity of contractile elements. Faster relaxation induced by cAMP was considered to be due to the decrease of Ca2+ sensitivity of contractile elements and faster Ca2+ uptake by SR. The slightly faster falling phase of light transient might be due to the faster Ca2+ uptake by SR, which predominates over the slower fall of [Ca2+]i induced by the decreased Ca2+ sensitivity of the contractile element.
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PMID:Effects of beta-adrenoceptor stimulation on intracellular Ca transients and tension in rat ventricular muscle. 244 10

Activation of protein kinase C (PKC), as revealed by phosphorylation of a 47 kd protein (p47), occurs in platelets stimulated by some agonists (eg, thrombin or phorbol esters). It is not known if activation of PKC occurs with pairs of agonists, such as epinephrine and A23187, that do not individually phosphorylate p47, nor is it known what role the concentration of cytoplasmic Ca++ ([Ca++]i) plays in these events. We stimulated aequorin-loaded platelets with subaggregating concentrations of epinephrine and A23187, neither of which by itself phosphorylated p47. The combination of agonists resulted in p47 phosphorylation, an increase in platelet-bound fibrinogen, and aggregation, but only if the concentration of each agonist was sufficient to increase [Ca++]i if it was added separately. Subaggregating concentrations of A23187 alone released platelet fibrinogen and increased platelet membrane binding of [3H]-phorbol dibutyrate, but these were not enhanced by epinephrine. Epinephrine and A23187 did not increase production of diacylglycerol. Thus, epinephrine and A23187 together activate PKC by a mechanism that does not require phospholipase C or enhanced binding of PKC to the plasma membrane; PKC activation in turn is correlated with enhanced platelet fibrinogen binding and aggregation. These events require an initial elevation of [Ca++]i above a threshold.
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PMID:Activation of protein kinase C in platelets by epinephrine and A23187: correlation with fibrinogen binding. 250 93