PHOSPHORYLATED MU-OPIOID RECEPTOR PURIFIED FROM RAT BRAINS LACKS FUNCTIONAL COUPLING WITH GI1, A GTP-BINDING PROTEIN IN RECONSTITUTED LIPID VESICLES

被引：47

作者：

HARADA, H

UEDA, H

KATADA, T

UI, M

SATOH, M

机构：

[1] KYOTO UNIV,FAC PHARMACEUT SCI,DEPT PHARMACOL,KYOTO 606,JAPAN

[2] UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,TOKYO 113,JAPAN

[3] TOKYO INST TECHNOL,DEPT LIFE SCI,YOKOHAMA,KANAGAWA 227,JAPAN

来源：

NEUROSCIENCE LETTERS | 1990年 / 113卷 / 01期

关键词：

Opioid receptor; Phosphorylation; Reconstitution; Signal transduction;

D O I：

10.1016/0304-3940(90)90492-R

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The effects of phosphorylation of a μ-opioid receptor on signal transduction to G-protein were studied. The μ-opioid receptor purified from rat whole brains was reconstituted with purified Gi1 in phosphatidylcholine vesicles. DAGO, a μ-opioid agonist at 1 μM-1 mM increased GTPase activity by 10-110% of control, in a concentration-dependent manner. When the μ-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). © 1990.

引用

页码：47 / 49

页数：3

共 5 条

[1] PHOSPHORYLATION OF MU-OPIOID RECEPTORS - A PUTATIVE MECHANISM OF SELECTIVE UNCOUPLING OF RECEPTOR-GI INTERACTION, MEASURED WITH LOW-KM GTPASE AND NUCLEOTIDE-SENSITIVE AGONIST BINDING [J].