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Nitric oxide regulates adenylyl cyclase activity in rat striatal membranes
Author(s) -
Hudson Tracie Y.,
Corbett John A.,
Howlett Allyn C.,
Klein Claudette
Publication year - 2001
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 - 10.1046/j.1471-4159.2001.00331.x
Subject(s) - adenylyl cyclase , forskolin , adcy10 , adcy9 , adcy6 , medicine , gs alpha subunit , endocrinology , nitric oxide , adcy3 , agonist , camp dependent pathway , chemistry , gene isoform , stimulation , biology , biochemistry , receptor , gene
The regulation of adenylyl cyclase activity by nitric oxide (NO) was studied in rat (Sprague–Dawley) striatal membranes. Three chemically distinct NO donors attenuated forskolin‐stimulated activity but did not alter basal activity. Maximum inhibition resulted in a 50% decrease in forskolin‐stimulated activity, consistent with the presence of multiple isoforms of adenylyl cyclase and our previous findings that only the forskolin‐stimulated activity of the type‐5 and ‐6 isoform family of enzymes is inhibited by NO. To monitor primarily the type‐5 isoform, we examined the ability of NO donors to attenuate D 1 ‐agonist‐stimulated adenylyl cyclase activity. Under those conditions, complete inhibition was observed. The data indicate that NO attenuates neuromodulator‐stimulated cAMP signaling in the striatum.