Identification and Application of Drosophila Novel Bioactive Peptides dRYamides
American Journal of Life Sciences
Volume 3, Issue 3-2, May 2015, Pages: 3-7
Received: Mar. 25, 2015; Accepted: Apr. 2, 2015; Published: May 6, 2015
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Authors
Takanori Ida, Department of Bioactive Peptides, Frontier Science Research Center University of Miyazaki, Miyazaki, Japan
Eri Iwamoto, Department of Bioactive Peptides, Frontier Science Research Center University of Miyazaki, Miyazaki, Japan
Takahiro Sato, Institute of Life Sciences, Kurume University, Fukuoka, Japan
Masayasu Kojima, Institute of Life Sciences, Kurume University, Fukuoka, Japan
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Abstract
The ligands of many orphan G protein-coupled receptors (GPCRs) remain to be identified, in both vertebrates and invertebrates, such as Drosophila melanogaster. Identification of their cognate ligands is critical for understanding the function and regulation of such GPCRs. Indeed, the discovery of bioactive peptides that bind GPCRs has enhanced our understanding of the mechanisms underlying many physiological processes. Here, we identified five endogenous ligands of the Drosophila orphan GPCRs, using functional assays and reverse pharmacological techniques. dRYamide-1 and -2 were found to be paired with the Drosophila neuropeptide Y (NPY)-like receptor (CG5811). Both dRYamide-1 and -2 contain a C-terminal RYamide. In vertebrates, RYamide motifs are found in NPY-family peptides. dRYamides were found to modulate feeding motivation in flies. These results suggest that deorphanizing the Drosophila orphan GPCRs might facilitate the elucidation of various physiological functions and identification of the ligands of orphan GPCRs in mammals.
Keywords
Novel Bioactive Peptide, Orphan GPCR, Drosophila
To cite this article
Takanori Ida, Eri Iwamoto, Takahiro Sato, Masayasu Kojima, Identification and Application of Drosophila Novel Bioactive Peptides dRYamides, American Journal of Life Sciences. Special Issue:Biology and Medicine of Peptide and Steroid Hormones. Vol. 3, No. 3-2, 2015, pp. 3-7. doi: 10.11648/j.ajls.s.2015030302.12
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