» Articles » PMID: 20003394

Ghrelin-like Peptide with Fatty Acid Modification and O-glycosylation in the Red Stingray, Dasyatis Akajei

Overview
Journal BMC Biochem
Publisher Biomed Central
Specialty Biochemistry
Date 2009 Dec 17
PMID 20003394
Citations 1
Authors
Affiliations
Soon will be listed here.
Abstract

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 (GRLN-LP) 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 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.

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

Citing Articles

Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2009-2010.

Harvey D Mass Spectrom Rev. 2014; 34(3):268-422.

PMID: 24863367 PMC: 7168572. DOI: 10.1002/mas.21411.

References
1.
Hosoda H, Kojima M, Kangawa K . Biological, physiological, and pharmacological aspects of ghrelin. J Pharmacol Sci. 2006; 100(5):398-410. DOI: 10.1254/jphs.crj06002x. View

2.
Yeung C, Chan C, Woo N, Cheng C . Seabream ghrelin: cDNA cloning, genomic organization and promoter studies. J Endocrinol. 2006; 189(2):365-79. DOI: 10.1677/joe.1.06593. View

3.
Bousfield G, Butnev V, Gotschall R, BAKER V, MOORE W . Structural features of mammalian gonadotropins. Mol Cell Endocrinol. 1996; 125(1-2):3-19. DOI: 10.1016/s0303-7207(96)03945-7. View

4.
Kaiya H, Miyazato M, Kangawa K, Peter R, Unniappan S . Ghrelin: a multifunctional hormone in non-mammalian vertebrates. Comp Biochem Physiol A Mol Integr Physiol. 2008; 149(2):109-28. DOI: 10.1016/j.cbpa.2007.12.004. View

5.
Riley L, Fox B, Kaiya H, Hirano T, Grau E . Long-term treatment of ghrelin stimulates feeding, fat deposition, and alters the GH/IGF-I axis in the tilapia, Oreochromis mossambicus. Gen Comp Endocrinol. 2005; 142(1-2):234-40. DOI: 10.1016/j.ygcen.2005.01.009. View