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Cyclase
About: Cyclase is a research topic. Over the lifetime, 10162 publications have been published within this topic receiving 388566 citations.
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139 citations
TL;DR: The frog erythrocyte membrane provides an excellent model system for the study of beta-adrenergic receptor-adenylate cyclase interactions since it possesses an adenylate Cyclase enzyme which is very responsive to catecholamines.
139 citations
TL;DR: Dopamine‐stimulated adenylate cyclase activity was potently antagonised by various neuroleptic drugs including fluphenazine, α‐flupenthixol and α‐piflutixol, and to a lesser extent by the butyrophenone derivatives haloperidol and spiperone.
Abstract: A specific dopamine-sensitive adenylate cyclase has been identified in homogenates of the teleost (carp) retina. Maximal stimulation by 100 microM-dopamine resulted in a 5--10-fold increase in adenylate cyclase activity with half-maximal stimulation occurring at a concentration of 1 microM. l-Noradrenaline and l-adrenaline were some 10 times less potent than dopamine whilst the alpha- and beta-adrenoreceptor agonists, l-phenylephrine and dl-isoprenaline were inactive. Apomorphine elicited a partial stimulation of adenylate cyclase activity whilst various ergot alkaloids produced mixed agonist/antagonist responses. Dopamine-stimulated adenylate cyclase activity was potently antagonised by various neuroleptic drugs including fluphenazine, alpha-flupenthixol and alpha-piflutixol, and to a lesser extent by the butyrophenone derivatives haloperidol and spiperone. The benzamide derivatives, metoclopramide and sulpiride, together with the alpha- and beta-adrenoreceptor blocking agents, phentolamine and propranolol respectively were essentially inactive at blocking dopamine-stimulated adenylate cyclase activity. These data suggest the presence of a highly specific dopamine-sensitive adenylate cyclase in homogenates of teleost retina possessing similar pharmacological properties to the dopamine-sensitive adenylate cyclase observed in the mammalian central nervous system.
139 citations
TL;DR: It is suggested that benzyl alcohol effects a fluidization of the bilayer, which is clearly demonstrated by its ability to lower the temperature of a lipid phase separation occurring at 28 degrees C in the outer half of the Bilayer to around 22 degrees C.
Abstract: 1. The local anaesthetic benzyl alcohol progressively activated glucagon-stimulated adenylate cyclase activity up to a maximum at 50 mM-benzyl alcohol. Further increases in benzyl alcohol concentration inhibited the activity. The fluoride-stimulated adenylate cyclase activity was similarly affected except for an inhibition of activity occurring at low benzyl alcohol concentrations (approx. 10 mM. 2. The fluoride-stimulated adenylate cyclase activity of a solubilized enzyme preparation was unaffected by any of the benzyl alcohol concentrations tested. 3. Increases in 3-phenylpropan-1-ol and 5-phenylpentan-1-ol concentrations progressively activated both the fluoride- and glucagon-stimulated adenylate cyclase activities up to a maximum, above which further increases in alcohol concentration inhibited the activities. 4. The ‘break’ points in Arrhenius plots of glucagon-stimulated adenylate cyclase activity in native plasma membranes, and in plasma membranes fused with synthetic dimyristoyl phosphatidylcholine so as to constitute 60% of the total lipid pool, were decreased by approx. 6 degrees C by addition of 40 mM-benzyl alcohol. This was accompanied by a fall in the associated activation energies. 6. Arrhenius plots of fluoride-stimulated adenylate cyclase activity in the presence and absence of 40 mM-benzyl alcohol were linear, although addition of benzyl alcohol caused a dramatic decrease in the associated activation energy of the reaction. 7. 5′-Nucleotidase activity was stimulated by benzyl alcohol, and the ‘break’ point in the Arrhenius plot of its activity was decreased by about 6 degrees C by addition of 40 mM-benzyl alcohol to the assay. 8. It is suggested that benzyl alcohol effects a fluidization of the bilayer, which is clearly demonstrated by its ability to lower the temperature of a lipid phase separation occurring at 28 degrees C in the outer half of the bilayer to around 22 degrees C. The increase in bilayer fluidity relieves a physical constraint on the membrane-bound adenylate cyclase, activating the enzyme. 9. The various inhibition phenomena are discussed in detail, together with the suggestion that the interaction between the uncoupled catalytic unit of adenylate cyclase and the lipids of the bilayer is altered on its physical coupling to the glucagon receptor.
138 citations
Journal Article•
TL;DR: Forskolin represents a potentially useful class of antiglaucoma agents differing in molecular mechanism of action from previously used drugs.
Abstract: Forskolin is a diterpene derivative of the plant Coleus forskohlii that stimulates adenylate cyclase activity without interacting with cell surface receptors. Forskolin lowers the intraocular pressure of rabbits, monkeys, and humans. In rabbits, net aqueous humor inflow decreases, outflow facility remains unchanged, and ciliary blood flow increases. Tolerance to the intraocular pressure lowering effect did not occur in rabbits after topical doses given every 6 hr for 15 days. In vitro forskolin activates adenylate cyclase of crude particulate homogenates prepared from cultured human ciliary epithelia or from dissected ciliary epithelial processes of rabbit or human eyes. This activation is not blocked by timolol. The stimulation of adenylate cyclase by isoproterenol in vitro is potentiated in the presence of forskolin. Forskolin represents a potentially useful class of antiglaucoma agents differing in molecular mechanism of action from previously used drugs.
138 citations