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.
Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, China.
Chen
C
Li-Wei
Gao
G
Can
Zhou
Z
De-He
Wei
W
Qiang
Xu
X
Xue-Jun
Chen
C
Jie
Chi
C
Zhi-Qiang
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