Agonist-Induced Subsensitivity of Adenylate Cyclase Coupled with a Dopamine Receptor in Slices from Rat Corpus Striatum

Incubation, for 30 min, of striatal slices with 10 μ M dopamine, 10 μ M apomorphine, or 10 μ M SKF 38393 decreases dopamine-stimulated adenylate cyclase activity by 50-60%. This loss in dopamine-stimulated enzyme activity appears to be mediated by a persistent occupancy of recognition sites of the D...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1982-07, Vol.79 (14), p.4456-4460
Main Authors: Memo, Maurizio, Lovenberg, Walter, Hanbauer, Ingeborg
Format: Article
Language:English
Subjects:
Adenylyl Cyclases - metabolism
Agonists
Animals
Apomorphine - pharmacology
Bicarbonates
Calcium-Binding Proteins - metabolism
Calmodulin - metabolism
Cell Membrane - metabolism
Cholera
Cholera Toxin - pharmacology
Corpus striatum
Corpus Striatum - enzymology
Corpus Striatum - metabolism
dopamine
Dopamine - pharmacology
Dopamine receptors
Dose-Response Relationship, Drug
Enzyme Activation - drug effects
Enzyme linked immunosorbent assay
Fluorides - pharmacology
Homogenization
In Vitro Techniques
Inurement
Male
Rats
Receptors
Receptors, Dopamine - drug effects
Receptors, Dopamine - metabolism
Toxins
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Summary:Incubation, for 30 min, of striatal slices with 10 μ M dopamine, 10 μ M apomorphine, or 10 μ M SKF 38393 decreases dopamine-stimulated adenylate cyclase activity by 50-60%. This loss in dopamine-stimulated enzyme activity appears to be mediated by a persistent occupancy of recognition sites of the D-1 receptor because: (i) at 10 μ M SKF 38393, a selective D-1 receptor agonist, facilitates desensitization and LY 141865, a selective D-2 receptor agonist, fails to elicit desensitization of dopamine-dependent adenylate cyclase; and (ii) preincubation with dopamine in the presence of 1 μ M haloperidol but not 1 μ M sulpiride curtails the desensitization of dopamine-dependent adenylate cyclase. In dopamine-desensitized striatal slices the Kdfor N-propylnorapomorphine binding is increased but the content of membrane-bound calmodulin and the activation of adenylate cyclase by NaF and cholera toxin are decreased significantly. In striatal slices incubated with dopamine for prolonged time periods the coupling of the GTP-binding protein with adenylate cyclase and dopamine recognition sites may be impaired and the content of membrane-bound calmodulin is decreased.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.14.4456