title: Structural requirements for biological activity of glucagon-like peptide-I.
abstract: Glucagon-like peptide-I (GLP-I) is encoded together with glucagon by the glucagon gene and is related in its structure to the glucagon-secretin family of peptides. Three of the predicted forms of the peptide, a 37-residue long GLP-I(1-37), a 31-residue GLP-I(7-37) and a 30-residue GLP-I(7-36)amide as well as three analogs des [Gly37, Arg36] GLP-I(7-37), des [Gly37, Arg36, Gly35] GLP-I(7-37) and des [His7] GLP-I(7-37) were synthesized by the stepwise solid phase method. These synthetic peptides were used to define the structural domains required for the binding of GLP-I to the pancreatic beta cell. The competitive binding experiments showed that both the amino and carboxyl terminal domains of the molecule contribute to GLP-I binding. In these experiments glucagon, another peptide that stimulates insulin secretion, was a weak full agonist of GLP-I binding. Results from these studies provide further characterization of the physiological role of this new peptide.
authors: Rockefeller University, New York, NY.
authors: S
authors: S
authors: Mojsov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001667:Binding, Competitive / Q000502:physiology; D002460:Cell Line; D005815:Genetic Code / Q000235:genetics; D004763:Glucagon-Like Peptides; D006801:Humans; D007328:Insulin / Q000378:metabolism; D000078790:Insulin Secretion; D008099:Liver / Q000502:physiology; D008969:Molecular Sequence Data; D010187:Pancreatic Hormones / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013329:Structure-Activity Relationship
chemical_list: D007328:Insulin; D010187:Pancreatic Hormones; D010455:Peptides; D004763:Glucagon-Like Peptides; C015236:glucagon-like-immunoreactivity