Skin secretion of the toad Bombina variegata contains multiple insulin-releasing peptides including bombesin and entirely novel insulinotropic structures

Biological Chemistry

Volumn 385, Issue 3-4, 2004, Pages 315-321

  Marenah, Lamin ^a   Flatt, Peter R ^a   Orr, David F ^a   McClean, Steven ^a   Shaw, Chris ^a   Abdel Wahab, Yasser H A ^a  

^a UNIVERSITY OF ULSTER   (United Kingdom)

Author keywords

Bombina variegata; Insulin secretion; Peptides

Indexed keywords

ANTIDIABETIC AGENT; BOMBESIN; CYCLIC AMP; GLUCOSE; INSULIN; PEPTIDE; PYROGLUTAMIC ACID;

ADOLESCENT; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; DATA BASE; ELECTROSTIMULATION; INCUBATION TIME; INSULIN RELEASE; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN ISOLATION; PURIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE HOMOLOGY; SKIN SECRETION; SKIN SURFACE; STATISTICAL ANALYSIS; TOAD;

AMINO ACID SEQUENCE; AMPHIBIAN VENOMS; ANIMALS; ANURA; BOMBESIN; ELECTRIC STIMULATION; GASTRIC INHIBITORY POLYPEPTIDE; MOLECULAR SEQUENCE DATA; SKIN;

ANURA; BOMBINA; BOMBINA BOMBINA; BOMBINA VARIEGATA; MAMMALIA;

EID: 2542494931     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.027     Document Type: Article

References (48)

1. Abdel-Wahab, Y. H., O'Harte, F. P. M., Mooney, M. H., Conlon, J. M. and Flatt, P. R. (1999). N-terminal glycation of cholecystokinin-8 abolishes its insulinotropic action on clonal pancreatic B-cells. Biochim. Biophys. Acta 1452, 60-67.
2. Anastasi, A., Erspamer, V. and Bucci, M. (1971). Isolation and structure of bombesin and alytesin, 2 analogous active peptides from the skin of the European amphibians Bombina and Alytes. Experientia 27, 166-167.
3. Bachmayer, H., Michl, H. and Roos, B. (1967). Animal Toxins (Oxford, UK: Pergamon Press), pp. 395-399.
4. Balboni, F., Bernabei, P. A., Barberio, C., Sanna, A., Rossi Ferrini, P. and Delfino, G. (1992). Cutaneous venom of Bombina variegata pachypus (Amphibia, Anura): effects on the growth of the human HL 60 cell line. Cell Biol. Int. Rep. 16, 329-338.
5. Barthalmus, G. T. (1994). Amphibian Biology (Surrey, UK: Beatty and Sons), pp. 382-410.
6. Bevins, C. L. and Zasloff, M. (1990). Peptides from frog skin. Annu. Rev. Biochem. 59, 395-414.
7. Brown, J. C. and Otte, S. C. (1978). Gastrointestinal hormones and the control of insulin secretion. Diabetes 27, 782-787.
8. Creutzfeldt, W. (1979). The incretin concept today. Diabetologia 16, 75-85.
9. Creutzfeldt, W., Feurle, G. and Ketterer, H. (1970). Effect of gastrointestinal hormones on insulin and glucagon secretion. N. Engl. J. Med. 282, 1139-1141.
10. Daly, J. W. (1995). The chemistry of poisons in amphibian skin. Proc. Natl. Acad. Sci. USA 92, 9-13.
11. de Jong, A. J., Klamer, M., Jansen, J. B. and Lamers, C. B. (1987). Effect of atropine and somatostatin on bombesin-stimulated plasma gastrin, cholecystokinin and pancreatic polypeptide in man. Regul. Pept. 17, 285-293.
12. Dockray, G. J., Vaillant, C. and Walsh, J. H. (1979). The neuronal origin of bombesin-like immunoreactivity in the rat gastrointestinal tract. Neuroscience 4, 1561-1568.
13. Duclohier, H., Molle, G. and Spach, G. (1989). Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56, 1017-1021.
14. Erspamer, V. (1980). Gastrointestinal Hormones (New York, USA: Raven Press), pp. 343-361.
15. Erspamer, V. (1994). Amphibian Biology (Surrey, UK: Beatty and Sons), pp. 178-350.
16. Erspamer, V. and Melchiorri, P. (1980). Active polypeptides from amphibian skin to gastrointestinal tract and brain of mammals. Trends Pharmacol. Sci. 1, 391-395.
17. Erspamer, V., Melchiorri, P., Falconieri Erspamer, G., Montecucchi, P. C. and de Castiglione, R. (1985). Phyllomedusa skin: a huge factory and store-house of a variety of active peptides. Peptides 6 (Suppl. 3), 7-12.
18. Erspamer, V., Falconieri Erspamer, G. and Cei, J. M. (1986). Active peptides in the skins of two hundred and thirty American amphibian species. Comp. Biochem. Physiol. C Comp. Pharmacol. 85, 125-137.
19. Flatt, P. R. and Bailey, C. J. (1981). Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetologia 20, 573-577.
20. Ford, L. S. and Cannatella, D. C. (1993). The major clades of frogs. Herpetol. Monogr. 7, 94-117.
21. Gromada, J., Holst, J. J. and Rorsman, P. (1998). Cellular regulation of islet hormone secretion by the incretin hormone glucagon-like peptide 1. Pflüger's Arch. Eur. J. Physiol. 435, 583-594.
22. Hunt, S. M., Chrzanowska, C., Barnnett, C. R., Brand, H. N. and Fawell, J. K. (1987). A comparison of in vitro cytotoxicity assays and their application to water samples. Altern. Lab. Anim. 15, 20-29.
23. Inoue, K., McKay, D., Yajima, H. and Rayford, P. L. (1983). Effect of synthetic porcine gastrin-releasing peptide on plasma levels of immunoreactive cholecystokinin pancreatic polypeptide and gastrin in dogs. Peptides 4, 153-157.
24. Ipp, E. and Unger, R. H. (1979). Bombesin stimulates the release of insulin and glucagon, but not pancreatic somatostatin, from the isolated perfused dog pancreas. Endocr. Res. Commun. 6, 37-42.
25. Kaneto, A., Kaneko, T., Nakaya, S., Kajinuma, H. and Kosaka, K. (1978). Effect of bombesin infused intrapancreatically on glucagon and insulin secretion. Metabolism 27, 549-553.
26. Ladenheim, E. E., Moore, K. A., Salorio, C. F., Mantey, S. A., Taylor, J. E., Coy, D. H., Jensen, R. T. and Moran, T. H. (1997). Characterization of bombesin binding sites in the rat stomach. Eur. J. Pharmacol. 319, 245-251.
27. Mastromei, G., Barberio, C., Pistolesi, S. and Delfino, G. (1991). A bactericidal protein in Bombina variegata pachypus skin venom. Toxicon 29, 321-328.
28. McClenaghan, N. H., Barnett, C. R., Ah-Sing, E., Abdel-Wahab, Y. H., O'Harte, F. P. M., Yoon, T. W., Swanston-Flatt, S. K. and Flatt, P. R. (1996). Characterization of a novel glucose-responsive insulin-secreting cell line, BRIN-BD11, produced by electrofusion. Diabetes 45, 1132-1140.
29. McDonald, T. J., Jornvall, H., Nilsson, G., Vagne, M., Ghatei, M., Bloom, S. R. and Mutt, V. (1979). Characterization of a gastrin releasing peptide from porcine non-antral gastric tissue. Biochem. Biophys. Res. Commun. 90, 227-233.
30. McDonald, T. J., Ghatei, M. A., Bloom, S. R., Track, N. S., Radziuk, J., Dupre, J. and Mutt, V. (1981). A qualitative comparison of canine plasma gastroenteropancreatic hormone response to bombesin and the porcine gastrin-releasing peptide (GRP). Regul. Pept. 2, 293-304.
31. Montecucchi, P. C. (1985). Isolation and primary structure determination of amphibian skin tryptophyllins. Peptides 6 (Suppl. 3), 187-195.
32. Moore, K. S., Bevins, C. L., Brasseur, M. M., Tomassini, N., Turner, K., Eck, H. and Zasloff, M. (1991). Antimicrobial peptides in the stomach of Xenopus laevis. J. Biol. Chem. 266, 19851-19857.
33. Mor, A. and Nicolas, P. (1994). Isolation and structure of novel defensive peptides from frog skin. Eur. J. Biochem. 219, 145-154.
34. Mor, A., Hani, K. and Nicolas, P. (1994). The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269, 31635-31641.
35. Moran, T. H., Moody, T. W., Hostetler, A. M., Robinson, P. H., Goldrich, M. and McHugh, P. R. (1988). Distribution of bombesin binding sites in the rat gastrointestinal tract. Peptides 9, 643-649.
36. Neuwirth, M., Daly, J. W., Myers, C. W. and Tice, L. W. (1979). Morphology of the granular secretory glands in skin of poison-dart frogs (Dendrobatidae). Tissue Cell 11, 755-771.
37. O'Harte, F. P., Gray, A. M. and Flatt, P. R. (1998a). Gastric inhibitory polypeptide and effects of glycation on glucose transport and metabolism in isolated mouse abdominal muscle. J. Endocrinol. 156, 237-243.
38. O'Harte, F. P. M., Abdel-Wahab, Y. H., Conlon, J. M. and Flatt, P. R. (1998b). Glycation of glucagon-like peptide-1(7-36)amide: characterization and impaired action on rat insulin secreting cells. Diabetologia 41, 1187-1193.
39. Richter, K., Egger, R. and Kreil, G. (1990). Molecular cloning of a cDNA encoding the bombesin precursor in skin of Bombina variegata. FEBS Lett. 262, 353-355.
40. Scarpignato, C. and Bertaccini, G. (1981). Bombesin delays gastric emptying in the rat. Digestion 21, 104-106.
41. Scarpignato, C., Micali, B., Vitulo, F., Zimbaro, G. and Bertaccini, G. (1981). The effect of bombesin on gastric emptying of solids in man. Peptides 2 (Suppl. 2), 199-203.
42. Seaquist, E. R., Neal, A. R., Shoger, K. D., Walseth, T. F. and Robertson, R. P. (1992). G-proteins and hormonal inhibition of insulin secretion from HIT-T15 cells and isolated rat islets. Diabetes 41, 1390-1399.
43. Simmaco, M., Barra, D., Chiarini, F., Noviello, L., Melchiorri, P., Kreil, G. and Richter, K. (1991). A family of bombinin-related peptides from the skin of Bombina variegata. Eur. J. Biochem. 199, 217-222.
44. Tyler, M. J., Stone, D. J. and Bowie, J. H. (1992). A novel method for the release and collection of dermal, glandular secretions from the skin of frogs. J. Pharmacol. Toxicol. Methods 28, 199-200.
45. Varga, G., Liehr, R. M., Scarpignato, C. and Coy, D. H. (1995). Distinct receptors mediate gastrin-releasing peptide and neuromedin beta-induced delay of gastric of liquids in rats. Eur. J. Pharmacol. 286, 109-112.
46. Williams, R. W., Starman, R., Taylor, K. M., Gable, K., Beeler, T., Zasloff, M. and Covell, D. (1990). Raman spectroscopy of synthetic antimicrobial frog peptides magainin 2a and PGLa. Biochemistry 29, 4490-4496.
47. Wolf, B. A., Easom, R. A., Hughes, J. H., McDaniel, M. L. and Turk, J. (1989). Secretagogue-induced diacylglycerol accumulation in isolated pancreatic islets. Mass spectrometric characterization of the fatty acyl content indicates multiple mechanisms of generation. Biochemistry 28, 4291-4301.
48. Yamatani, T., Chiba, T., Kadowaki, S., Hishikawa, R., Yamaguchi, A., Inui, T., Fujita, T. and Kawazu, S. (1988). Dual action of protein kinase C activation in the regulation of insulin release by muscarinic agonist from rat insulinoma cell line (RINr). Endocrinology 122, 2826-2832.