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• W1693202216 startingPage "161" @default.
• W1693202216 abstract "This chapter discusses the biochemical changes that occur during the desensitization of striatal dopamine receptor. The experimental data indicate that prolonged occupancy of dopamine recognition sites confers subsensitivity to various dopamine-mediated mechanisms, which include radioligand recognition sites and the regulatory subunit of adenylate cyclase. In addition, data demonstrate that the desensitization of dopamine receptors is associated with an increased phosphorylation mediated by a cyclic adenosine monophosphate (cAMP)-dependent protein kinase of proteins located at postsynaptic membranes. The data suggest that in caudate nucleus, the dopamine-sensitive adenylate cyclase is a part of a multimolecular receptor complex consisting of various proteins with highly specific functions. The activity of adenylate cyclase is regulated by a tissue-specific distribution of D-1 or D-2 recognition sites coupled to the catalytic subunit of the enzyme by Ns or Ni subunits, respectively. The experimental data also indicate that during the desensitization of dopamine-sensitive adenylate cyclase, intracellular signals are amplified leading to an increase in the phosphorylation of specific proteins located in striatal membranes." @default.
• W1693202216 created "2016-06-24" @default.
• W1693202216 creator A5046368205 @default.
• W1693202216 creator A5090548570 @default.
• W1693202216 date "1986-01-01" @default.
• W1693202216 modified "2023-10-18" @default.
• W1693202216 title "Chapter 14 Molecular mechanisms involved in the desensitization of dopamine receptors in slices of corpus striatum" @default.
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• W1693202216 doi "https://doi.org/10.1016/s0079-6123(08)61057-2" @default.
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