Isolation, localization, and characterization of gastrointestinal peptides.
Increasing numbers of peptides have been found in the gastrointestinal tract. Some of these are localized primarily in endocrine cells in the gastrointestinal epithelium (e.g., gastrin, secretin) or pancreatic islets (e.g., insulin, glucagon), and function chiefly as circulating hormones. Other peptides, e.g., VIP, are principally neuropeptides present mainly in nerve cells, nerve fibres and nerve terminals; they function mainly as neurotransmitters or neuromodulators. The isolation of gut peptides has usually depended on the use of characteristic bioassays. More recently, some peptides have been isolated on the basis of unique terminal amino-acid composition. Certain chemical structures are associated with typical biological actions, and several "families" of related peptides are recognized.
D001483:Base Sequence; D001681:Biological Assay; D055598:Chemical Phenomena; D002621:Chemistry; D004702:Endocrine Glands / Q000032:analysis; D005768:Gastrointestinal Hormones / Q000032:analysis*; D006801:Humans; D009474:Neurons / Q000032:analysis; D018377:Neurotransmitter Agents / Q000032:analysis; D012333:RNA, Messenger; D011863:Radioimmunoassay; D011956:Receptors, Cell Surface / Q000378:metabolism; D014018:Tissue Distribution
D005768:Gastrointestinal Hormones; D018377:Neurotransmitter Agents; D012333:RNA, Messenger; D011956:Receptors, Cell Surface