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Comprehensive analysis of a dipeptide library to identify ghrelin release‐modulating peptides
Author(s) -
Nakato Junya,
Aoki Hayato,
Tokuyama Yuki,
Yamamoto Yuta,
Iwakura Hiroshi,
Matsumura Shigenobu,
Inoue Kazuo,
Ohinata Kousaku
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13522
Subject(s) - dipeptide , ghrelin , secretion , chemistry , in vivo , peptide , amino acid , in vitro , biochemistry , biology , receptor , microbiology and biotechnology
We performed a comprehensive analysis of ghrelin release‐modulating activity of a dipeptide library using MGN3‐1, a ghrelin‐producing cell line. We found that most dipeptides suppress ghrelin secretion, whereas the N‐terminal Ser‐containing dipeptides and a few others stimulate it. N‐terminal amino acid residues, but not C‐terminal residues, play a dominant role in the effects of dipeptides. Among dipeptides, Leu‐Ile (LI) and Ser‐Val (SV) most strongly suppress and stimulate ghrelin secretion, respectively. LI activates G i signaling and SV acts via the MAPK pathway. Orally administered LI and SV reduce and increase plasma ghrelin levels and food intake in mice, respectively. In conclusion, LI and SV, found based on the comprehensive screening of a dipeptide library, modulate ghrelin secretion in vitro and in vivo .