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Vol. 55, Issue 1, 167-194, March 2003
Department of Biochemistry, Molecular Biology and Cell Biology,
Northwestern University, Evanston, Illinois (K.E.M.); Mayo Clinic and
Foundation, Department of Molecular Pharmacology and Experimental
Therapeutics, Rochester, Minnesota (L.J.M.); INSERM U 376, Montpellier,
France (D.B., S.D.); Department of Medicine II, Grosshadern, Klinikum
der Ludwig-Maximilians, University of Munich, Germany (B.G.); Institute
of Pharmacology and Toxicology, University of Lausanne, Lausanne,
Switzerland (B.T.); and Banting and Best Diabetes Centre, Toronto
General Hospital, University of Toronto, Toronto, Ontario, Canada
(D.J.D.)
Peptide hormones within the secretin-glucagon family are expressed in endocrine cells of the pancreas and gastrointestinal epithelium and in specialized neurons in the brain, and subserve multiple biological functions, including regulation of growth, nutrient intake, and transit within the gut, and digestion, energy absorption, and energy assimilation. Glucagon, glucagon-like peptide-1, glucagon-like peptide-2, glucose-dependent insulinotropic peptide, growth hormone-releasing hormone and secretin are structurally related peptides that exert their actions through unique members of a structurally related G protein-coupled receptor class 2 family. This review discusses advances in our understanding of how these peptides exert their biological activities, with a focus on the biological actions and structural features of the cognate receptors. The receptors have been named after their parent and only physiologically relevant ligand, in line with the recommendations of the International Union of Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC-IUPHAR).
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