@article{844012b0b44c11df825b000ea68e967b,
title = "Oxyntomodulin differentially affects glucagon-like peptide-1 receptor beta-arrestin recruitment and signaling through Galpha(s)",
abstract = "The glucagon-like peptide (GLP)-1 receptor is a promising target for the treatment of type 2 diabetes and obesity, and there is great interest in characterizing the pharmacology of the GLP-1 receptor and its ligands. In the present report, we have applied bioluminescence resonance energy transfer assays to measure agonist-induced recruitment of betaarrestins and G-protein-coupled receptor kinase (GRK) 2 to the GLP-1 receptor in addition to traditional measurements of second messenger generation. The peptide hormone oxyntomodulin is described in the literature as a full agonist on the glucagon and GLP-1 receptors. Surprisingly, despite being full agonists in GLP-1 receptor-mediated cAMP accumulation, oxyntomodulin and glucagon were observed to be partial agonists in recruiting betaarrestins and GRK2 to the GLP-1 receptor. We suggest that oxyntomodulin and glucagon are biased ligands on the GLP-1 receptor.",
author = "Rasmus Jorgensen and Valentina Kubale and Milka Vrecl and Schwartz, {Thue W} and Elling, {Christian E}",
note = "Keywords: Animals; Arrestins; COS Cells; Cercopithecus aethiops; Cyclic AMP; G-Protein-Coupled Receptor Kinase 2; G-Protein-Coupled Receptor Kinase 5; GTP-Binding Protein alpha Subunits, Gs; Glucagon; Glucagon-Like Peptide 1; Humans; Luminescent Measurements; Oxyntomodulin; Protein-Serine-Threonine Kinases; Receptors, Glucagon; Signal Transduction; beta-Adrenergic Receptor Kinases",
year = "2007",
doi = "10.1124/jpet.107.120006",
language = "English",
volume = "322",
pages = "148--54",
journal = "Journal of Pharmacology and Experimental Therapeutics",
issn = "0022-3565",
publisher = "American Society for Pharmacology and Experimental Therapeutics",
number = "1",
}
