Recent Advances in the Search for the μ-Opioidergic System

The Japanese Journal of Pharmacology

Hirokazu Mizoguchi¹  Ichiro Sora³  Minoru Narita²  Leon F. Tseng¹  Tsutomu Suzuki² 

[1] Department of Anesthesiology, Medical College of Wisconsin;Department of Toxicology, School of Pharmacy, Hoshi University;Department of Psychopharmacology, Tokyo Institute of Psychiatry

关键词: Endomorphin;    β-Endorphin;    G-Protein;    [35S]GTPγS binding;    μ-Opioid receptor;   

DOI  :  10.1254/jjp.89.229

学科分类：药理学

来源: Nihon Yakuri Gakkai Henshuubu / Japanese Pharmacological Society

【 摘 要 】

References(38)Cited-By(9)It is well documented that the μ-opioid receptor (MOP-R) is expressed by neurons in several central nervous system regions. Its occupancy with agonist drugs modulate a variety of physiological processes including pain, reward, stress, immune responses, neuroendocrine functions, and cardiovascular control. Based on the receptor binding assay, endomorphin-1 and endomorphin-2 have the highest specificity and affinity for the MOP-R of any endogenous substance so far described in the mammalian nervous system. In contrast, β-endorphin exhibits the strongest actions among endogenous opioid peptides mainly through the MOP-R; however, it also shows the distinct pharmacological actions. Recent cloning and expression studies have indicated that MOP-Rs are seven-transmembrane domain receptors whose actions are mediated through activation of heterotrimeric guanine nucleotide binding proteins (G-proteins). The activation of G-proteins by MOP-Rs can be measured by assessing agonist-induced stimulation of membrane binding of guanosine-5'-o-(3-[35S]thio)triphosphate ([35S]GTPγS). The subject of the present review is to focus on the differential mechanism underlying G-protein activation induced by these μ-opioid peptides using the [35S]GTPγS binding assay.

【 授权许可】

Unknown