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• W2409931094 abstract "It is well documented that the mu-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, beta-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]GTPgammaS). The subject of the present review is to focus on the differential mechanism underlying G-protein activation induced by these mu-opioid peptides using the [35S]GTPgammaS binding assay." @default.
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• W2409931094 date "2002-01-01" @default.
• W2409931094 modified "2023-10-10" @default.
• W2409931094 title "Recent Advances in the Search for the μ-Opioidergic System: Differential Mechanism of G-Protein Activation Induced by Endogenous μ-Opioid Peptides, Endomorphin and β-Endorphin" @default.
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• W2409931094 doi "https://doi.org/10.1254/jjp.89.229" @default.
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