Journal
BMC BIOCHEMISTRY
Volume 10, Issue -, Pages -Publisher
BMC
DOI: 10.1186/1471-2091-10-30
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Funding
- MEXT of Japan
- National Institute of Biomedical Innovation (NIBIO) of Japan
- Takeda Scientific Foundation of Japan
- Suntory institute for bioorganic research (SUNBOR GRANT) of Japan
- Grants-in-Aid for Scientific Research [21591189, 21370025] Funding Source: KAKEN
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Background: Ghrelin (GRLN) is now known to be an appetite-stimulating and growth hormone (GH)-releasing peptide that is predominantly synthesized and secreted from the stomachs of various vertebrate species from fish to mammals. Here, we report a GRLN-like peptide (GRLNLP) in a cartilaginous fish, the red stingray, Dasyatis akajei. Results: The purified peptide contains 16 amino acids (GVSFHPQPRS10TSKPSA), and the serine residue at position 3 is modified by n-octanoic acid. The modification is the characteristic of GRLN. The six N-terminal amino acid residues (GVSFHP) were identical to another elasmobranch shark GRLN-LP that was recently identified although it had low identity with other GRLN peptides. Therefore, we designated this peptide stingray GRLN-LP. Uniquely, stingray GRLN-LP was Oglycosylated with mucin-type glycan chains [N-acetyl hexosamine (HexNAc) 3 hexose(Hex) 2] at threonine at position 11 (Thr-11) or both serine at position 10 (Ser-10) and Thr-11. Removal of the glycan structure by O-glycanase made the in vitro activity of stingray GRLN-LP decreased when it was evaluated by the increase in intracellular Ca2+ concentrations using a rat GHS-R1a-expressing cell line, suggesting that the glycan structure plays an important role for maintaining the activity of stingray GRLN-LP. Conclusions: This study reveals the structural diversity of GRLN and GRLN-LP in vertebrates.
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