Cloning and expression of an isoform of the rat μ opioid receptor (rMOR1B) which differs in agonist induced desensitization from rMOR1

FEBS Letters

Zimprich, Alexander²  Höllt, Volker¹  Simon, Tatiana² 

[1] Department of Pharmacology and Toxicology, Otto von Guericke-University, Leipzigerstrasse 44, 39120 Magdeburg, Germany;Department of Physiology, University of Munich, Munich, Germany

关键词: Opioid receptor;    Alternative splicing;    Desensitization;    Cloning;    G protein-coupled receptor;   

DOI  :  10.1016/0014-5793(95)00028-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel rat μ opioid receptor (rMOR1B) has been isolated. It shows identity to the recently published sequence of rMOR1 [Chen, et al., Mol. Pharmacol., 44 (1993) 8–12] up to amino acid 386 and differs only in length and amino acid composition at the very carboxy-terminal tail. Both μ opioid receptor isoforms, when stably expressed in CHO-K1 cells, show similar affinities to opioid compounds and are equally effective in the inhibition of forskolin-induced cAMP formation. Reverse transcription polymerase chain reaction (RT-PCR) revealed that rMOR1B displays a similar distribution as rMOR1 in various rat brain areas. Studies measuring the inhibition of adenylate cyclase in cells that had been pre-exposed to the μ opioid agonist DAMGO indicated that rMOR1B is much more resistant to agonist-induced desensitization than rMOR1.

【 授权许可】

Unknown