Biotechnology of beta-adrenergic receptors.
The emergence of Biotechnology has provided pharmacologists with a variety of methods for investigating the structure, the function, and the regulation of membrane-bound receptors with a precision that was not imagined even five years ago. These new tools have been developed and used to analyze the known catecholamine beta 1- and beta 2-adrenergic receptors and to discover and study a new subtype, the beta 3 receptor. We review here the salient features of each of these three receptors, compare their structural and functional properties, and propose models to explain their differential regulation in time and space. A whole family of proteins has now been found to share with the beta-adrenergic receptors their most prominent features, including seven transmembrane domains and coupling with GTP-binding "G" proteins. We therefore propose that the biotechnology-based procedures developed for the beta-adrenergic receptors will be well applicable to the other members of this "R7G" family of receptors.
Strosberg
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AD
Laboratoire d'Immuno-Pharmacologie Moléculaire, CNRS UPR 0415, Paris, France.
D000262:Adenylyl Cyclases / Q000235:genetics / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000276:immunology; D000918:Antibody Specificity; D001665:Binding Sites; D003001:Cloning, Molecular / Q000379:methods; D000242:Cyclic AMP / Q000502:physiology; D019204:GTP-Binding Proteins / Q000235:genetics / Q000502:physiology; D005796:Genes; D006031:Glycosylation; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011943:Receptors, Adrenergic, beta / Q000187:drug effects / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D015290:Second Messenger Systems; D014714:Vertebrates / Q000378:metabolism
D000888:Antibodies, Anti-Idiotypic; D010446:Peptide Fragments; D011943:Receptors, Adrenergic, beta; D011993:Recombinant Fusion Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases