从大鼠脑中纯化的磷酸化μ-阿片受体在重组脂质小泡中缺乏与GTP结合蛋白Gi1的功能性偶联。
Phosphorylated mu-opioid receptor purified from rat brains lacks functional coupling with Gi1, a GTP-binding protein in reconstituted lipid vesicles.
作者信息
Harada H, Ueda H, Katada T, Ui M, Satoh M
机构信息
Department of Pharmacology, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
出版信息
Neurosci Lett. 1990 May 18;113(1):47-9. doi: 10.1016/0304-3940(90)90492-r.
The effects of phosphorylation of a mu-opioid receptor on signal transduction to G-protein were studied. The mu-opioid receptor purified from rat whole brains was reconstituted with purified Gi1 in phosphatidylcholine vesicles. DAGO, a mu-opioid agonist at 1 microM-1 mM increased GTPase activity by 10-110% of control, in a concentration-dependent manner. When the mu-opioid receptor was phosphorylated by cyclic AMP-dependent protein kinase prior to reconstitution with Gi1, the DAGO-stimulation was markedly reduced (20% increase at 1 mM DAGO).
研究了μ-阿片受体磷酸化对G蛋白信号转导的影响。从大鼠全脑中纯化的μ-阿片受体与纯化的Gi1在磷脂酰胆碱囊泡中重构。μ-阿片激动剂DAGO在1μM - 1 mM浓度下可使GTP酶活性比对照增加10 - 110%，呈浓度依赖性。在用Gi1重构之前，当μ-阿片受体被环磷酸腺苷依赖性蛋白激酶磷酸化时，DAGO刺激作用明显降低（1 mM DAGO时增加20%）。
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