Hudson T Y, Corbett J A, Howlett A C, Klein C
Edward A. Doisy Department of Biochemistry and Molecular Biology, Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, St Louis, Missouri 63104, USA.
J Neurochem. 2001 Jun;77(5):1279-84. doi: 10.1046/j.1471-4159.2001.00331.x.
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.
在大鼠（斯普拉格-道利）纹状体膜中研究了一氧化氮（NO）对腺苷酸环化酶活性的调节作用。三种化学性质不同的NO供体减弱了福斯可林刺激的活性，但未改变基础活性。最大抑制导致福斯可林刺激的活性降低50%，这与腺苷酸环化酶存在多种同工型以及我们之前的发现一致，即只有5型和6型同工型酶家族的福斯可林刺激活性受到NO的抑制。为了主要监测5型同工型，我们检测了NO供体减弱D(1)激动剂刺激的腺苷酸环化酶活性的能力。在这些条件下，观察到完全抑制。数据表明，NO减弱了纹状体中神经调质刺激的cAMP信号传导。
