Premium
The Muscarinic Receptor Adenylate Cyclase Complex of Rat Striatum: Desensitization Following Chronic Inhibition of Acetylcholinesterase Activity
Author(s) -
Olianas Maria C.,
Onali Pierluigi,
Schwartz Joan P.,
Neff N. H.,
Costa E.
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb02806.x
Subject(s) - muscarinic acetylcholine receptor , cyclase , striatum , adenylate kinase , muscarinic acetylcholine receptor m5 , desensitization (medicine) , chemistry , acetylcholinesterase , muscarinic acetylcholine receptor m4 , muscarinic acetylcholine receptor m1 , endocrinology , medicine , pharmacology , receptor , neuroscience , muscarinic acetylcholine receptor m3 , biology , biochemistry , enzyme , dopamine
Chronic inhibition of acetylcholinesterase activity by treatment with diisopropylfluorophosphate (DFP) decreased the capacity of acetylcholine (ACh) acting at a muscarinic receptor to inhibit basal adenylate cyclase activity in homogenates from rat striatum. There was also a loss of the capacity of ACh to inhibit the activation of adenylate cyclase by dopamine. The desensitization of the muscarinic receptor adenylate cyclase complex was associated with a marked attenuation of the capacity of ACh to stimulate a high‐affinity GTPase activity present in striatal membranes. The EC 50 value of ACh for inhibiting adenylate cyclase and for stimulating GTPase activity increased following treatment with DFP, while the Hill coefficient for both responses was unaltered.