Isolation and characterization of a novel bradykinin potentiating peptide (BPP) from the skin secretion of Phyllomedusa hypochondrialis

Peptides

Volumn 28, Issue 3, 2007, Pages 515-523

  Conceição, Katia ^a   Konno, Katsuhiro ^a   de Melo, Robson Lopes ^a   Antoniazzi, Marta M ^a   Jared, Carlos ^a   Sciani, Juliana M ^a   Conceição, Isaltino M ^a   Prezoto, Benedito C ^a   de Camargo, Antônio Carlos Martins ^a   Pimenta, Daniel C ^a  

^a INSTITUTO BUTANTAN   (Brazil)

Author keywords

Bradykinin; Bradykinin potentiating peptide; De novo sequencing; Mass spectrometry; Natural peptides; Phyllomedusa hypochondrialis; Secretion

Indexed keywords

BRADYKININ; CAPTOPRIL; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE; PYROGLUTAMYLARGINYLTRYPTOPHYLPROLYLHISTIDYLLEUCYL GLUTAMYLISOLEUCYLPROLYLPROLINE; PYROGLUTAMYLASPARAGINYLTRYPTOPHYLPROLYLARGINYLPROLYL GLUTAMINYLISOLEUCYLPROLYLPROLINE; PYROGLUTAMYLASPARAGINYLTRYPTOPHYLPROLYLHISTIDYLPROLYL GLUTAMINYLISOLEUCYLPROLYLPROLINE; PYROGLUTAMYLGLYCYLLEUCYLPROLYLPROLYLARGINYLPROLYLISOLEUCYLPROLYLPROLINE; PYROGLUTAMYLPHENYLALANYLARGINYLPROLYLSERYLTYROSYL GLUTAMINYLISOLEUCYLPROLYLPROLINE; PYROGLUTAMYLSERYLTRYPTOPHYLPROLYLGLYCYLPROLYL ASPARAGINYLISOLEUCYLPROLYLPROLINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPETITIVE INHIBITION; CONTROLLED STUDY; DRUG POTENTIATION; ENZYME INHIBITION; FEMALE; FROG; MALE; NONHUMAN; PHYLLOMEDUSA HYPOCHONDRIALIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ISOLATION; PROTEIN MOTIF; RAT; SKIN SECRETION;

AMINO ACID SEQUENCE; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; ANURA; BLOOD PRESSURE; BRADYKININ; DRUG SYNERGISM; FEMALE; GUINEA PIGS; ILEUM; MALE; OLIGOPEPTIDES; RATS; RATS, WISTAR; SKIN;

ANURA; BOTHROPS JARARACA; HYLIDAE; PHYLLOMEDUSA HYPOCHONDRIALIS;

EID: 33846849342     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.10.002     Document Type: Article

References (54)

1. Araujo M.C., Melo R.L., Cesari M.H., Juliano M.A., Juliano L., and Carmona A.K. Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39 (2000) 8519-8525
2. Atherton, and Sheppard. Solid phase peptide synthesis-a practical approach (1989), IRL Press, Oxford p. 75-160
3. Bamberg U., Elg P., and Stewagen P. Tryptic and plasmatic peptide fragments increasing the effect of bradykinin on isolated smooth muscle. Scand J Clin Lab Invest 24 (1960) 21-35
4. Brand G.D., Krause F.C., Silva L.P., Leite J.R., Melo J.A., Prates M.V., et al. Bradykinin-related peptides from Phyllomedusa hypochondrialis. Peptides 27 (2006) 2137-2146
5. Calixto J.B., Cabrini D.A., Ferreira J., and Campos M.M. Kinins in pain and inflammation. Pain 87 (2000) 1-5
6. Chen T., Zhou M., Gagliardo R., Walker B., and Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypochondrialis. Peptides 27 (2006) 2129-2136
7. Clarke B.T. The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol Rev Camb Philos Soc 72 (1997) 365-379
8. Conceição K., Konno K., Richardson M., Antoniazzi M.M., Jared C., Daffre S., et al. Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis. Peptides 27 (2006) 3092-3099
9. Conlon J.M. Bradykinin and its receptors in non-mammalian vertebrates. Regul Pept 79 (1999) 71-81
10. Conlon J.M., Jouenne T., Cosette P., Cosquer D., Vaudry H., Taylor C.K., et al. Bradykinin-related peptides and tryptophyllins in the skin secretions of the most primitive extant frog, Ascaphus truei. Gen Comp Endocrinol 143 (2005) 193-199
11. Couture R., Harrisson M., Vianna R.M., and Cloutier F. Kinin receptors in pain and inflammation. Eur J Pharmacol 429 (2001) 161-176
12. Cyr M., Lepage Y., Blais Jr. C., Gervais N., Cugno M., Rouleau J.L., et al. Bradykinin and des-Arg(9)-bradykinin metabolic pathways and kinetics of activation of human plasma. Am J Physiol Heart Circ Physiol 281 (2001) H275-H283
13. Daudin FM. Histoire naturelle des rainettes, des grenouilles et des crapauds. 1802 Imprimerie de Bertrandet; libraire Leurault, Paris. p. 108. (ex Easteal 1986).
14. Erspamer V., Erspamer G.F., and Cei J.M. Active peptides in the skins of two hundred and thirty American amphibian species. Comp Biochem Physiol C 85 (1986) 125-137
15. Erspamer V. Bioactive secretions of the integument. In: Heatwole H., and Barthalmus G.T. (Eds). The integument, amphibian biology vol. 1 (1994), Surrey Beatty & Sons, Chipping Norton 179-350
16. Ferreira L.A.F., Möllring T., Lebrun F.L.A.S., Raida M., Znottka R., and Habermehl G.G. Structure and effects of a kinin potentiating fraction F (AppF) isolated from Agkistrodon piscivorus piscivorus venom. Toxicon 33 (1995) 1313-1319
17. Ferreira L.A., Galle A., Raida M., Schraderr M., Lebrun I., and Habermehl G. Isolation: analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom. J Protein Chem 17 (1998) 285-289
18. Ferreira S.H. A bradykinin-potentiating factor (Bpf) present in the venom of Bothrops jararaca. Br J Pharmacol 24 (1965) 163-169
19. Ferreira S.H., and e Silva M.R. Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom. Experientia 21 (1965) 347-349
20. Ferreira S.H., Bartelt D.C., and Greene L.J. Isolation of bradykinin potentiating peptides from Bothrops jararaca venom. Biochemistry 9 (1970) 2583-2593
21. Giles A.R. Guidelines for the use of animals in biochemical research. Thromb Haemost 58 (1987) 1078-1084
22. Hayashi M.A., Murbach A.F., Ianzer D., Portaro F.C., Prezoto B.C., Fernandes B.L., et al. The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J Neurochem 85 (2003) 969-977
23. Henriques O.B., de Deus R.B., and Santos R.A. Bradykinin potentiating peptides isolated from alpha-casein tryptic hydrolysate. Biochem Pharmacol 36 (1987) 182-184
24. Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y., Camargo A.C., et al. Bradykinin-potentiating peptides and C-type natriuretic peptides from snake venom. Immunopharmacology 44 (1999) 129-135
25. Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stocklin R., de Camargo A.C.M., et al. Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography. Peptides 25 (2004) 1085-1092
26. Ianzer D., Konno K., Xavier C.H., Stö cklin R., Santos R.A.S., Camargo A.C.M., et al. Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo. Peptides 27 (2006) 2957-2966
27. Kato H., and Suzuki T. Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii. Isolation of five bradykinin potentiators and the amino acid sequences of two of them potentiators B and C. Biochemistry 10 (1971) 972-980
28. Kato H., and Suzuki T. Structure of bradykinin-potentiating peptide containing tryptophan from the venom of Agkistrodon halys blomhoffii. Experientia 26 (1970) 1025
29. Konno K., Palma M.S., Hitara I.Y., Juliano M.A., Juliano L., and Yasuhara T. Identification of bradykinins in solitary wasp venoms. Toxicon 40 (2002) 309-312
30. Kreil G. Antimicrobial peptides from amphibian skin: an overview. Ciba Found Symp 186 (1994) 77-90
31. Lebrun I., Lebrun F.L., Henriques O.B., Carmona A.K., Juliano L., and Camargo A.C. Isolation and characterization of a new bradykinin potentiating octapeptide from gamma-casein. Can J Physiol Pharmacol 73 (1995) 85-91
32. Li L., Bjourson A.J., He J., Cai G., Rao P., and Shaw C. Bradykinins and their cDNA from piebald odorous frog, Odorrana schmackeri, skin. Peptides 24 (2003) 863-872
33. Linz W., Wiemer G., Gohlke P., Unger T., and Scholkens B.A. Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors. Pharmacol Rev 47 (1995) 25-49
34. Matsui T., Li C.H., and Osajima Y. Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. J Pept Sci 5 (1999) 289-297
35. Moreau M.E., Garbacki N., Molinaro G., Brown N.J., Marceau F., and Adam A. The kallikrein-kinin system: current and future pharmacological targets. J Pharmacol Sci 99 (2005) 6-38
36. Murayama N., Hayashi M.A., Ohi H., Ferreira L.A., Hermann V.V., Saito H., et al. Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide. Proc Natl Acad Sci USA 94 (1997) 1189-1193
37. Ondetti M.A., Williams N.J., Sabo E.F., Pluscec J., Weaver E.R., and Kocy O. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry 10 (1971) 4033-4039
38. Ondetti M.A., and Cushman D.W. Enzymes of the renin-angiotensin system and their inhibitors. Annu Rev Biochem 1 (1982) 283-308
39. Piot J.M., Zhao Q., Guillochon D., Ricart G., and Thomas D. Isolation and characterization of a bradykinin-potentiating peptide from a bovine peptic hemoglobin hydrolysate. FEBS Lett 299 (1992) 75-79
40. Rabito S.F., Biia A., and Segovia R. Plasma kininogen content of toads. Comp Biochem Physiol 41 (1972) 281-284
41. Rittschof D., and Cohen J.H. Crustacean peptide and peptide-like pheromones and kairomones. Peptides (2004) 251503-251516
42. e Silva M.R., Beralolo W.T., and Rosenfeld G. Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am J Physiol 156 (1949) 261-273
43. Seki T., Miwa I., Nakajima T., and Erdos E.G. Kallikrein-kinin system in non-mammalian blood. Am J Physiol 224 (1973) 1425-1430
44. Shimuta S.I., Sabia E.B., Paiva A.C.M., and Paiva T.B. Effect of stretching on the sensitivity of the guinea pig ileum to bradykinin and on its modification by bradykinin potentiating peptides. Eur J Pharmacol 70 (1981) 551-558
45. Sosnina N.A.A., Golubenco Z., Akhunov A.A., Kugaevskaya E.V., Eliseeva Y.E., and Orekhovich V.N. Bradykinin-potentiating peptides from the spider Latrodectus tredecimguttatus-inhibitors of carboxycathepsin and of a preparation of karakurt venom kininase. Dokl Akad Nauk SSSR 315 (1990) 281-284
46. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 (1994) 4673-4680
47. Torfs P., Nieto J., Veelaert D., Boon D., van de Water G., Waelkens E., et al. The kinin peptide family in invertebrates. Ann NY Acad Sci 897 (1999) 361-373
48. Westermeier R., and Naven T. Proteomics in practice (2002), Wiley-VCH, Germany
49. Wilkinson G.N. Statistical estimations in enzyme kinetics. Biochem J 80 (1961) 324-332
50. Witkop B., and Brossi A. Natural toxins and drug development. In: Krogsgaard-Larsen P., Christensen S.B., and Kofod H. (Eds). Proceedings of the Alfred Benzon Symposium on natural products and drug development, vol. 20 (1984), Munksgaard, Copenhagen 283-300
51. Yamafuji K., Taniguchi Y., and Sakamoto E. The thiol enzyme from rat spleen that produces bradykinin potentiating peptide from rat plasma. Immunopharmacology 32 1-3 (1996) 157-159
52. Yang H.Y.T., Erdös E.G., and Levin Y. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim Biophys Acta 214 (1970) 374-376
53. Zeng X.C., Li W.X., Peng F., and Zhu Z.H. Cloning and characterization of a novel cDNA sequence encoding the precursor of a novel venom peptide (BmKbpp) related to a bradykinin-potentiating peptide from Chinese scorpion Buthus martensii. Karsch IUBMB life 49 (2000) 207-210
54. Zhao Q., Garreau I., Sannier F., and Piot J.M. Opioid peptides derived from hemoglobin: hemorphins. Biopolymers 43 (1997) 75-98