Homodimerization of human mu-opioid receptor overexpressed in Sf9 insect cells.
In this study, we demonstrate that human mu-opioid receptors do form SDS-resistant homodimers and examine the ability of human mu-opioid receptors to dimerize and the role of agonists in the dimerization. Increasing concentrations and longer exposure of agonists reduce the levels of dimmer with a corresponding increase in the levels of monomer. This effect is achieved with both peptide and alkaloid opioid agonists and it is antagonist reversible. These results suggest that human mu-opioid receptors are present as receptor oligomers and interconversion between dimeric and monomeric forms may be important for biological activity.
Li-Wei
Chen
C
Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, China.
Can
Gao
G
De-He
Zhou
Z
Qiang
Wei
W
Xue-Jun
Xu
X
Jie
Chen
C
Zhi-Qiang
Chi
C
D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D015153:Blotting, Western; D002460:Cell Line; D019281:Dimerization; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D005283:Fentanyl / Q000031:analogs & derivatives* / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D007313:Insecta; D008024:Ligands; D009294:Narcotics / Q000819:agonists; D010455:Peptides / Q000737:chemistry; D017450:Receptors, Opioid, mu / Q000737:chemistry* / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D013997:Time Factors
D008024:Ligands; D009294:Narcotics; D010455:Peptides; D017450:Receptors, Opioid, mu; D012967:Sodium Dodecyl Sulfate; C037016:F 7302; D019204:GTP-Binding Proteins; D005283:Fentanyl