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- W1981124744 abstract "The effect of potassium depolarization on dopamine D1 receptor activity in bovine retina was investigated. Preincubation of bovine retinas in buffer containing high KC1 (56 mM) as compared to a low KC1 control buffer resulted in a significant decrease in dopamine-stimulated adenylate cyclase with no change in basal or GTP-stimulated adenylate cyclase activity. The apparentVmax for dopamine was decreased from102 ± 15 pmol/min/mg protein in retinas preincubated in high KC1 to71 ± 11 pmol/min/mg protein in control retinas (n = 5). The apparentKa for dopamine stimulation of the enzyme did not change. The potassium-induced desentization could be blocked by preincubation with the dopamine antagonistcis-flupenthixol suggesting that the desentization was caused by the release of dopamine. The rapid desentization was not accompanied by a change in D1 receptor density as assessed by binding of [3H]SCH23390 nor in agonist binding as assessed by competition of the selective D1 agonist, SKF38393, for [3H]SCH23390 binding. The potassium-induced desentization was mimicked by preincubation of retinas in control medium containing isobutylmethylxanthine or dibutyryl cyclic AMP. Incubation of retinas in 56 mM KC1 also fed to a decrease in activation of adenylate cyclase by vasoactive intestinal polypeptide. These results strongly suggest that potassium depolarization leads to a very rapid heterologous desentization of adenylate cyclase in bovine retinas." @default.
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- W1981124744 date "1990-06-01" @default.
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- W1981124744 title "Desensitization of the dopaminergic system in bovine retina following incubation with high potassium" @default.
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- W1981124744 doi "https://doi.org/10.1016/0006-8993(90)91555-u" @default.
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