Oligomerization of opioid receptors

被引:58
作者
Gomes, I [1 ]
Filipovska, J [1 ]
Jordan, BA [1 ]
Devi, LA [1 ]
机构
[1] NYU, Sch Med, Dept Pharmacol, MSB 408, New York, NY 10016 USA
关键词
immunoprecipitation; Western blotting; crosslinking; bioluminescence resonance energy transfer;
D O I
10.1016/S1046-2023(02)00094-4
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Opioid receptors belong to the family of G-protein-coupled receptors characterized by their seven transmembrane domains. The activation of these receptors by agonists such as morphine and endogenous opioid peptides leads to the activation of inhibitory G-proteins followed by a decrease in the levels of intracellular cAMP. Opioid receptor activation is also associated with the opening of K+ channels and the inhibition of Ca2+ channels. A number of investigations, prior to the development of opioid receptor CDNAs, suggested that opioid receptor types interacted with each other. Early pharmacological studies provided evidence for the probable interaction between opioid receptors. More recent studies using receptor selective antagonists, antisense oligonuelcotides, or animals lacking opioid receptors further suggested that interactions between opioid receptor types could modulate their activity. We examined opioid receptor interactions using biochemical, biophysical, and pharmacological techniques. We used differential epitope tagging and selective immunoisolation of receptor complexes to demonstrate homotypic and heterotypic interactions between opioid receptor types. We also used the proximity-based bioluminescence resonance energy transfer assay to explore opioid receptor-receptor interactions in living cells. In this article we describe the biochemical and biophysical methods involved in the detection of receptor dimers. We also address some of the concerns and suggest precautions to be taken in studies examining receptor-receptor interactions. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:358 / 365
页数:8
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