Ghrelin is a growth-hormone-releasing acylated peptide from stomach

Masayasu Kojima (), Hiroshi Hosoda, Yukari Date, Masamitsu Nakazato, Hisayuki Matsuo and Kenji Kangawa
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Masayasu Kojima: National Cardiovascular Center Research Institute, Fujishirodai, Suita
Hiroshi Hosoda: National Cardiovascular Center Research Institute, Fujishirodai, Suita
Yukari Date: National Cardiovascular Center Research Institute, Fujishirodai, Suita
Masamitsu Nakazato: Miyazaki Medical College
Hisayuki Matsuo: National Cardiovascular Center Research Institute, Fujishirodai, Suita
Kenji Kangawa: National Cardiovascular Center Research Institute, Fujishirodai, Suita

Nature, 1999, vol. 402, issue 6762, 656-660

Abstract: Abstract Small synthetic molecules called growth-hormone secretagogues (GHSs)1,2,3 stimulate the release of growth hormone (GH) from the pituitary4,5. They act through GHS-R, a G-protein-coupled receptor for which the ligand is unknown. Recent cloning of GHS-R6,7 strongly suggests that an endogenous ligand for the receptor does exist and that there is a mechanism for regulating GH release that is distinct from its regulation by hypothalamic growth-hormone-releasing hormone (GHRH)4,5. We now report the purification and identification in rat stomach of an endogenous ligand specific for GHS-R. The purified ligand is a peptide of 28 amino acids, in which the serine 3 residue is n-octanoylated. The acylated peptide specifically releases GH both in vivo and in vitro, and O-n-octanoylation at serine 3 is essential for the activity. We designate the GH-releasing peptide ‘ghrelin’ (ghre is the Proto-Indo-European root of the word ‘grow’). Human ghrelin is homologous to rat ghrelin apart from two amino acids. The occurrence of ghrelin in both rat and human indicates that GH release from the pituitary may be regulated not only by hypothalamic GHRH, but also by ghrelin.

Date: 1999
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DOI: 10.1038/45230

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