caa a22 4500 378849522 CHVBK 20180305123320.0 cr unu---uuuuu 161128e20030127xx s 000 0 eng 10.1515/BC.2003.012 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.012 Biochemical Characterization of β2-Adrenergic Receptor Dimers and Oligomers [Elektronische Daten] [A. Salahpour, H. Bonin, S. Bhalla, U. Petäjä-Repo, M. Bouvier] 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 β2-adrenergic receptor (β2AR) 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 β2AR 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 β2AR 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 and oligomers may be indicative of distinct biological roles in cells, additional studies will be required to further elucidate the biosynthesis and function of these receptor forms. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Salahpour A. aut Bonin H. aut Bhalla S. aut Petäjä-Repo U. aut Bouvier M. aut Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 117-123 1431-6730 384:1<117 2003 384 bchm https://doi.org/10.1515/BC.2003.012 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.012 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Salahpour A. aut NATIONALLICENCE 700 1- Bonin H. aut NATIONALLICENCE 700 1- Bhalla S. aut NATIONALLICENCE 700 1- Petäjä-Repo U. aut NATIONALLICENCE 700 1- Bouvier M. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/1(2003-01-27), 117-123 1431-6730 384:1<117 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter