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Adenosine 3',5'-cyclic monophosphate phosphodiesterase in guinea-pig lung—Properties and effect of adrenergic drugs.
Biochem Pharmacol 1973; 22(8):959-969
The hydrolysis of adenosine-3',5'-cyclic-monophosphate (60924) (cAMP) by adenosine-3',5'-monophosphate-phosphodiesterase (PDE) was studied in whole homogenates and cell fractions of guinea-pig lung. cAMP has been implicated as a controlling agent in a number of processes which govern lung function. Increases in cAMP have been associated with tracheal smooth muscle relaxation and decreases with the immunological release of histamine (51456) from human lung. The physiological responses of these systems and the intracellular cAMP levels respond to stimulation with isoproterenol, epinephrine, norepinephrine (51412), and methoxamine (390283) via both alpha and beta receptors. This report describes the results of experiments which demonstrated that guinea-pig lung contains two forms of phosphodiesterase with different affinities for cAMP and that predominately the low affinity form is affected by adrenergic drugs.
NIOSH-Publication; NIOSH-Grant; Pulmonary-system-disorders; Catecholamines; Sympathetic-nervous-system; Enzyme-activity; Cytology; Histamine; Endocrinology; Sympathomimetics; Biochemistry; Pulmonary-system; Pharmacology
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