About this Biochemistry, Genetics and Molecular Biology article
Biochemical Characterization of β2-Adrenergic Receptor Dimers and Oligomers by A. Salahpour; H. Bonin; S. Bhalla; U. Petäjä-Repo; M. Bouvier is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
G Protein-coupled receptor dimerization/oligomerization has been well established during the last several years. Studies have demonstrated the existence of dimers/digomers both in vitro and in living cells. However, a thorough characterization of the biochemical nature of receptor dimers and oligomers as well as their occurrence at the cell surface has not been properly addressed. In this study, we show that both  2 -adrenergic receptor ( 2 AR) dimers and oligomers exist at the plasma membrane and that the detection of such species, following receptor solubilization and resolution by denaturing polyacrylamide gel electrophoresis (SDS-PAGE), does not result from the formation of spurious disulfide bonds during cell lysis. Moreover, our results indicate that the biochemical nature of  2 AR dimers is different from that of the oligomers. Although both complexes are partially resistant to SDS denaturation, disulfide bonding is absolutely required for the stability of  2 AR oligomers but not dimers in SDS-PAGE. Indeed, dimeric species can be detected even in the presence of high concentrations of reducing and alkylating agents. Although the different biochemical nature of the dimers
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- Author
- A. Salahpour; H. Bonin; S. Bhalla; U. Petäjä-Repo; M. Bouvier
- Publisher
- Walter de Gruyter GmbH
- Published
- 2003
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)