Receptor for Motilin Identified in the Human Gastrointestinal System

• Published in: Science (American Association for the Advancement of Science) 1999-06, Vol.284 (5423), p.2184-2188
• Main Authors: Feighner, Scott D., Tan, Carina P., McKee, Karen Kulju, Palyha, Oksana C., Hreniuk, Donna L., Pong, Sheng-Shung, Austin, Christopher P., Figueroa, David, MacNeil, Douglas, Cascieri, Margaret A., Nargund, Ravi, Bakshi, Raman, Abramovitz, Mark, Stocco, Rino, Kargman, Stacia, O'Neill, Gary, Lex H. T. Van Der Ploeg, Evans, Jilly, Patchett, Arthur A., Smith, Roy G., Howard, Andrew D.
• Format: Article
• Language: English
• Subjects: Alternative Splicing; Amino Acid Sequence; Amino acids; Anatomy; Base Sequence; Binding Sites; Biological and medical sciences; Calcium - metabolism; Cell Line; Cell lines; Cell membranes; Chromosome Mapping; Chromosomes, Human, Pair 13; Cloning, Molecular; Colon - metabolism; Digestive system; Erythromycin - metabolism; Fundamental and applied biological sciences. Psychology; Gastric Mucosa - metabolism; Gastrointestinal motility; Gastrointestinal system; Gastrointestinal tract; Genes. Genome; Genomics; GTP-Binding Proteins - metabolism; Hormones; Humans; In Situ Hybridization; Intestine, Small - metabolism; Ligands; Messenger RNA; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Molecular Structure; Motilin - analogs & derivatives; Motilin - metabolism; Motility; Nucleotides; Observation; Peptides; Proteins; Receptors; Receptors, Gastrointestinal Hormone - chemistry; Receptors, Gastrointestinal Hormone - genetics; Receptors, Gastrointestinal Hormone - metabolism; Receptors, Neuropeptide - chemistry; Receptors, Neuropeptide - genetics; Receptors, Neuropeptide - metabolism; Scientific Concepts; Thyroid Gland - metabolism; Transfection
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.284.5423.2184

Motilin is a 22-amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract of humans and other species. It affects gastric motility by stimulating interdigestive antrum and duodenal contractions. A heterotrimeric guanosine triphosphate-binding protein (G protein)-coupled receptor for motilin was isolated from human stomach, and its amino acid sequence was found to be 52 percent identical to the human receptor for growth hormone secretagogues. The macrolide antibiotic erythromycin also interacted with the cloned motilin receptor, providing a molecular basis for its effects on the human GI tract. The motilin receptor is expressed in enteric neurons of the human duodenum and colon. Development of motilin receptor agonists and antagonists may be useful in the treatment of multiple disorders of GI motility.