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Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei

Hiroyuki Kaiya3*, Shiho Kodama1, Koutaro Ishiguro2, Kouhei Matsuda2, Minoru Uchiyama2, Mikiya Miyazato3 and Kenji Kangawa3

Author Affiliations

1 Biochemical research laboratories, ASUBIO PHARMA CO, LTD, 1-1-1, Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618-8513, Japan

2 Department of Biology, Faculty of Science, Toyama University, Toyama 930-8555, Japan

3 Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan

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BMC Biochemistry 2009, 10:30  doi:10.1186/1471-2091-10-30

Published: 14 December 2009



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 (GRLN-LP) in a cartilaginous fish, the red stingray, Dasyatis akajei.


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 O-glycosylated 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.


This study reveals the structural diversity of GRLN and GRLN-LP in vertebrates.