Parasympathetic denervation decreases muscarinic receptor binding in rat parotid.
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Biomedical subjects
Publications and source records attributed to D R Burt.
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The binding of [3H]haloperidol to rat striatal dopamine receptors increases after lesion (made by injection of 6-hydroxydopamine) of the nigrostriatal dopamine pathway in those rats which are behaviorally supersensitive, as reflected by apomorphine-induced contralateral rotations. The enhanced binding is associated with an increased number of receptor sites with no change in their affinity.
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Chronic treatment of rats with the neuroleptic drugs haloperidol, fluphenazine, and reserpine elicits a 20 to 25% increase in striatal dopamine receptor binding assayed with [3H]haloperidol. This increase in receptor sites may account for behavioral supersensitivity to dopamine receptor stimulants in such animals and for tardive dyskinesia in patients treated with these drugs.
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Tritiated haloperidol and tritiated dopamine label postsynaptic dopamine receptors in mammalian brain. Clinical potencies of butyrophenones, phenothiazines, and related drugs correlate closely with their ability to inhibit tritiated haloperidol binding. These binding methods provide a simple in vitro means for evaluating new drugs as potential antischizophrenic agents.
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Thyrotropin releasing hormone (TRH) binds to membranes of rat brain tissue via high- and low-affinity binding components. The high-affinity binding of TRH to brain membranes resembles binding to pituitary membranes in terms of its affinity and specificity for most peptides. In equilibrium studies, the affinity and specificity for most peptides. In equilibrium studies, the dissociation constant for high-affinity binding to brain membranes is about 50 dissociation constant for high-affinity binding to brain membranes is about 50nM, which is about the same as for aat pituitary membranes, while low-affinity binding to brain membranes has a dissociation constant of about 5 muM. Liver membranes display low-affinity binding for TRH with a dissociation constant similar to the low-affinity binding component of brain membranes. No high-affinity binding can be detected with liver membranes. Negligible saturable binding to TRH can be detected with membranes of any tissues examined other than liver, pituitary and brain...
Specific binding of [3H]dopamine to membranes from the corpus striatum of rat and calf brain appears to involve the postsynaptic dopamine receptor. Specific [3H]dopamine binding is saturable, wnd with half-maximal binding in calf membranes at 7 nM. Apomorphine is about twice as potent as dopamine in competing for binding sites, whereas (-)norepinephrine is 5% as potent as dopamine and isoproterenol is virtually inactive. The relative potencies of phenothiazines as inhibitors of specific dopamine binding correlates with their clinical potencies and actions on the dopamine-sensitive adenylate cyclase.
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