|
|
|
|
|
|
A Novel Insulinotropic Peptide from the Skin Secretions of Amolops loloensis Frog |
Guo-Xiang Mo1, Xue-Wei Bai1, Zong-Jie Li1, Xiu-Wen Yan1, Xiao-Qing He2, Ming-Qiang Rong2 |
1. School of Biological Sciences, Nanjing Agriculture University, Nanjing 210095, Jiangshu, China; 2. Kunming Institue of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China |
|
|
Abstract Various kinds of biologically active peptides have previously been isolated from the skin secretions of Amolops loloensis frog, such as antimicrobial peptides, bradykinin-like peptides and algesic peptides. A novel insulinotropic peptide named amolopin was identified in A. loloensis frog's skin secretion. Its primary structure sequence was determined by Edman degradation as: FLPIVGKSLSGLSGKL-NH2. BLAST search indicates that the amino acid sequence of amolopin is quite different from other known insulin secretagogues, including mastoparan, exendins and a-latrotoxin, nor does it like incretins(e.g. glucagons like peptide-1 and glucose-dependent insulinotropic ploypeptide) either. However, amolopin shows certain structural similarity with amphibian antimicrobial temporins and vespid chemotactic peptides isolated from Vespa magnifica. Amolopin can stimulate insulin release in INS-1 cells in a dose-dependent manner. Primary investigation on its action mechanisms reveals that amolopin does not increase the influx of Ca2+. In conclusion, a novel 16-amino acid peptide with insulin-releasing activity is initially discovered from the skin secretion of A. loloensis frog. Further work is necessary to evaluate its potential as novel anti-diabetic candidate.
|
Keywords
Insulinotropic peptide
Amolops loloensis
Skin secretion
Insulin-releasing
Frog
|
Fund:This work was supported by National Natural Science Foundation(31200590), Jiangsu Province(BK2012365, BE2012748) and Yunan Province(2013FB072). |
Issue Date: 11 February 2018
|
|
|
1. M. Simmaco, G. Mignogna, D. Barra, Biopolymers 47, 435-450 (1998) 2. J. Li, X. Xu, C. Xu, W. Zhou, K. Zhang, H. Yu, Y. Zhang, Y. Zheng, H.H. Rees, R. Lai, D. Yang, J. Wu, Mol. Cell. Proteomics 6, 882-894 (2007) 3. J.P. Raufman, Regul. Pept. 61, 1-18 (1996) 4. T.A. Nogueira, F. Ferreira, H.M. Toyama, F.L. Stoppiglia, S. Marangoni, A. Boschero, M.E. Carneiro, Toxicon 45, 243-248 (2005) 5. N. Yokokawa, M. Komatsu, T. Takeda, T. Aizawa, T. Yamada, Biochem. Biophys. Res. Commun. 158, 712-716 (1989) 6. A. Rohou, J. Nield, Y.A. Ushkaryov, Toxicon 49, 531-549 (2007) 7. C.A. Ashton, M.A. Rahman, E.K. Volynski, C. Manser, V.E. Orlova, H. Matsushita, A.B. Davletov, V.M. Heel, V.E. Grishin, A.Y. Ushkaryov, Biochimie 82, 453-468 (2000) 8. D.I. Israel, Nucleic Acids Res. 21, 2627-2631 (1993) 9. P.M. Jones, F.M. Mann, S.J. Persaud, C.P. Wheeler-Jones, Mol. Cell. Endocrinol. 94, 97-103 (1993) 10. H.R. Amin, H. Chen, R. Veluthakal, B.R. Silver, J. Li, A. Kowluru, Endocrinology 144, 4508-4518 (2003) 11. M. Simmaco, G. Mignogna, S. Canofeni, R. Miele, M.L. Mangoni, D. Barra, Eur. J. Biochem. 242, 788-792 (1996) 12. Y.H. Abdel-Wahab, L. Marenah, D.F. Orr, C. Shaw, P.R. Flatt, Biol. Chem. 386, 58-581 (2005) 13. L. Marenah, P.R. Flatt, D.F. Orr, S. McClean, C. Shaw, Y.H. Abdel-Wahab, J. Endocrinol. 181, 347-354 (2004) 14. L. Marenah, P.R. Flatt, D.F. Orr, C. Shaw, Y.H. Abdel-Wahab, Peptides 26, 2117-2123 (2005) 15. L. Marenah, P.R. Flatt, D.F. Orr, C. Shaw, Y.H. Abdel-Wahab, J. Endocrinol. 188, 1-9 (2006) 16. Y.H. Abdel-Wahab, L. Marenah, P.R. Flatt, J.M. Conlon, Protein Pept. Lett. 14, 702-707 (2007) 17. J. Liang, Y. Han, J. Li, X. Xu, H.H. Rees, R. Lai, Peptides 27, 2683-2687 (2006) 18. Y. Lu, J. Li, H. Yu, X. Xu, J. Liang, Y. Tian, D. Ma, G. Lin, G. Huang, R. Lai, Peptides 27, 3085-3091 (2006) 19. H. Yu, X. Wang, J. Liu, R. Lai, J. Pept. Sci. 13, 798-802 (2007) 20. M. Asfari, D. Janjic, P. Meda, G. Li, A.P. Halban, B.C. Wollheim, Endocrinology 130, 167-178 (1992) 21. E. Santini, P. Fallahi, M.S. Ferrari, A. Masoni, A. Antonelli, E. Ferranini, Diabetes 53, 79-83 (2004) 22. K.J. Mitchell, T. Tsuboi, G.A. Rutter, Diabetes 53, 393-400 (2004) 23. J. Fauconnier, D.C. Andersson, S.J. Zhang, J.T. Lanner, R. Wibom, A. Katz, J.D. Bruton, H. Westerblad, Diabetes 56, 1136-1142 (2007) 24. X. Hu, M. Jiang, J. Zhang, A. Zhang, F. Lin, M. Tan, New Phytol. 173, 27-38 (2007) 25. H. Feng, Y. Lv, M. Wang, J, Li. Zool. Res. 30, 165-170 (2009) 26. X. Xu, J. Li, Q. Lu, H. Yang, Y. Zhang, R. Lai, Toxicon 47, 249-253 (2006) 27. A. Dubois, Bull. Mens. Soc. Linn. Lyon. 61, 305-352 (1992) 28. C. Liu, Fieldiana Zool. Mem. 2, 1-400 (1950) 29. N. Morikawa, K. Hagiwara, T. Nakajima, Biochem. Biophys. Res. Commun. 189, 184-190 (1992) 30. M.L. Mangoni, J.M. Saugar, M. Dellisanti, D. Barra, M. Simmaco, L. Rivas, J. Biol. Chem. 280, 984-990 (2005) 31. M. Zhou, L. Wang, D.E. Owens, T. Chen, B. Walker, C. Shaw, Peptides 28, 1605-1610 (2007) 32. E.H. Hohmeier, B.C. Newgard, Mol. Cell. Endocrinol. 228, 121-128 (2004) |
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|