Proceedings of the National Academy of Sciences · 1972 · 287 citations · 27 references
Life SciencesBiochemistryPharmacologyCell SignalingNeuropharmacologySignal TransductionCyclic Nucleotide SignalingRetinal NeurobiologyRetinal NeuroscienceAdenylate Cyclase RegulationAdenylate Cyclase SignalingAdenylyl Cyclase RegulationAdenylyl Cyclase SignalingCyclic Adenosine Monophosphate PathwayCyclic Adenosine Monophosphate SignalingRetinal PharmacologyRetinal Physiology
A catecholamine-sensitive adenylate cyclase system is present in homogenates of both calf and rat retinas. Dopamine is a more potent activator of the bovine enzyme than is norepinephrine or epinephrine. Cyclic AMP concentrations in intact bovine retina are increased by dopamine, as well as by other catecholamines, and by depolarizing agents. Studies with adrenergic blocking agents suggest that the stimulation of retinal adenylate cyclase by catecholamines cannot be clearly defined in terms of the characteristics of alpha or beta adrenergic receptors. Bovine retina also contains a protein kinase that is stimulated 20-fold by cyclic AMP. It is proposed that dopamine is the major activator of a retinal adenylate cyclase, and that this activation is related to its role as a neurotransmitter.
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Cyclic Nucleotide-dependent Protein Kinases
Eishichi Miyamoto, J.F. Kuo, Paul Greengard · Journal of Biological Chemistry · 1969 · 550 citations · Full text