Author: Hosoda, H.; Kojima, M.; Matsuo, H.; Kangawa, K.
Description: Ghrelin, a novel peptide purified from stomach, is the endogenous ligand for the growth hormone secretagogue receptor and has potent growth hormone-releasing activity. The Ser3 residue of ghrelin is modified by n-octanoic acid, a modification necessary for hormonal activity. We established two ghrelin-specific radioimmunoassays; one recognizes the octanoyl-modified portion and another the C-terminal portion of ghrelin. Using these radioimmunoassay systems, we found that two major molecular forms exist-ghrelin and des-n-octanoyl ghrelin. While ghrelin activates growth-hormone secretagogue (GHS) receptor-expressing cells, the nonmodified des-n-octanyl form of ghrelin, designated as des-acyl ghrelin, does not. In addition to these findings, our radioimmunoassay systems also revealed high concentrations of ghrelin in the stomach and small intestine.
Subject headings: Amino Acid Sequence; Animals; Duodenum; Gastric Mucosa; Ghrelin; Immunoglobulins; Male; Molecular Sequence Data; Peptide Hormones; Peptides; Radioimmunoassay; Rats; Rats; Sprague-Dawley; Tissue Distribution
Publication year: 2000
Journal or book title: Biochemical and Biophysical Research Communications
Volume: 279
Issue: 3
Pages: 909-913
Find the full text: https://www.sciencedirect.com/science/article/abs/pii/S0006291X00940397
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Serial number: 3403