Both proteins are potent activators of PTH receptor-coupled adenylate cyclase in bone cells.

It couples to stimulatory G protein and activates adenylate cyclase upon agonist stimulation.

These results suggest that DIDS acts at multiple sites on alpha 2-adrenoceptor-adenylate cyclase complex.

The mechanism of impairment appears to be localized to the adenylate cyclase moiety itself.

But the number of cells with reaction products of the adenylate cyclase activity were decreased.

The role of the beta-adrenoceptor-G-protein-adenylate cyclase system in the pathogenesis of cardiac hypertrophy was studied.

Cell viability was assessed by determination of adenylate kinase (AK) release.

This compound has no significant effect on adenylate cyclase in concentrations of up to 100 microM.

In contrast, fluoride-stimulated adenylate cyclase activity was markedly increased only in the end stage of hypertrophy.

The findings suggest an uncoupling of beta-adrenoceptors from the catalytic site of the adenylate cyclase complex.

Conclusions: Superposition of these structures allows a common reaction mechanism for seryl-adenylate and Ap4A formation to be proposed.

Further, in hypertrophy, the reduced creatine kinase and adenylate kinase activities limited energy delivery to the nuclear pore.

In the first step of this two-step reaction, Mg.ATP and serine react to form the activated intermediate, seryl-adenylate.

Leech secretion stimulates adenylate cyclase of platelet membranes in a receptor-mediated fashion and increases the level of cAMP.

In cytochemical investigations no reaction of the adenylate cyclase activity was found in the centre of the necroses.

Moreover, a difference in responsiveness to the inhibitory effects to epinephrine on adenylate cyclase was also observed between donors.