Biochemical and Pharmacological Aspects of Two Bradykinin-Potentiating Peptides Obtained from Tryptic Hydrolysis of Casein

Journal of Protein Chemistry

Volumn 22, Issue 7-8, 2003, Pages 601-606

  Perpetuo, Elen A ^a   Juliano, Luis ^b   Lebrun, Iva ^a  

^a INSTITUTO BUTANTAN   (Brazil)

^b FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Angiotensin converting enzyme; Bradykinin; Casein; Potentiating peptides

Indexed keywords

BRADYKININ; CASEIN; DIPEPTIDYL CARBOXYPEPTIDASE; GLUTAMYLMETHIONYLPROLYLPHENYLALANYLPROLYLLYSINE; OPIATE PEPTIDE; THIMET OLIGOPEPTIDASE; TYROSYLPROLYLVALYLGLUTAMYLPROLYLPHENYLALANYLTHREONYLGLUTAMIC ACID; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; DRUG MECHANISM; DRUG POTENTIATION; DRUG PROTEIN BINDING; ENZYME INHIBITION; FEMALE; GUINEA PIG; ILEUM; IN VITRO STUDY; MALE; NONHUMAN; PEPTIDE ANALYSIS; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN ISOLATION; PROTEIN MOTIF; RAT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; BLOOD PRESSURE; BRADYKININ; CASEINS; FEMALE; GUINEA PIGS; HYDROLYSIS; ILEUM; METALLOENDOPEPTIDASES; OLIGOPEPTIDES; PAIN; RATS; TRYPSIN; UTERUS;

ANIMALIA; CAVIA PORCELLUS; SERPENTES; SUS SCROFA;

EID: 0347362479     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOPC.0000008724.98339.ff     Document Type: Article

References (30)

1. Bendhack, L. M., Lindsey, C. J., and Paiva, A. C. M. (1986). Converting enzyme inhibitors decrease kininase but not converting activity in the rat mesenteric vascular bed. Hypertension 8(suppl I): 90-94.
2. Chagas, J. R., Juliano, L., and Prado, E. S. (1991). Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal Biochem. 192: 419-425.
3. Chang, K. J., Killian, A., Hazum, E., and Cuatrecasas, J. P. (1981). Morphiceptin: a potent and specific agonist for morphine receptors. Science 212: 75-77.
4. Erdos, E. G., and Skidgel, R. A. (1989). Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3(2): 144-151.
5. Ferreira, S. H., and Rocha e Silva, M. (1965). Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom. Experientia 15;21(6): 347-349.
6. Ferreira, L. A. F., Henriques, O. B., Lebrun, I., Batista, M. B. C., Prezoto, B. C., Andreoni, A. S. S., et al. (1992). A new bradykinin-potentiating peptide (peptide P) isolated from the venom of Bothropsjararacussu. Toxicon 30: 33-40.
7. Henriques, O. B., Ferreira, L. A. F., Flash, H. M., and Oliveira, E. B. (1983). Bradykinin potentiator from a casein peptone preparation. Adv. Med. & Biol. 156A: 621-623.
8. Henriques, O. B., Deus, R. B., and Santos, R. A. S. (1987). Bradykinin-potentiating peptides isolated from alpha-casein tryptic hydrolysate. Biochem. Pharmacol. 36: 182-184.
9. Jacob, J. J., and Ramabadran, K. (1978). Enhacement of a nociceptive reaction by opioid antagonist in mice. Braz. J. Pharmacol. 64(1): 91-98.
10. Kest, B., Orlowski, M., Molineaux, C. J., and Bodnar, R. J. (1991). Antinoceptive properties of inhibitors of endopeptidase 24.15. Int. J. Neurosci. 56(14): 141-149.
11. Kim, K. S., Kumar, S., Simmons, W. H., and Brown, N. J. (2000). Inhibition of aminopeptidase P potentiates wheal response to BK in angiotensin converting enzyme inhibitor treated humans. J. Pharmacol. Exp. Ther. 292(1): 295-298.
12. Kubota, E., Dean, R. G., Balding, L. C., and Burrel, L. M. (2002). Inhibition of peptidases in the control of blood pressure. Essays Biochem. 38: 129-139.
13. Lebrun, I. (1988). Estudo dos efeitos e metabolização de peptídeos no útero isolado de rata. Dissertação de Mestrado, Faculdade de Medicina de Ribeirão Preto da Universidade de São Paulo.
14. Lebrun, I., Camargo, A. C. M., and Corrêa, F. M. A. (1988). Pharmacological effects and metabolism of neurotensin and bradykinin in the isolated rat uterus. European of Pharmacology 148: 231-237.
15. Lebrun, I., Lebrun, F. L. A. S., Henriques, O. B., Carmona, A. K., Juliano, L., and Camargo, A. C. M. (1995). Isolation and characterization of a new bradykinin potentiating octapeptide from γ-casein. Can. J. Physiol. Pharmacol. 73: 85-91.
16. Maruyama, S., Nakagomi, K., Tomizuka, N., and Suzuki, H. (1982). A peptide inhibitor of angiotensin I-converting enzyme in the tryptic hydrolysate of casein. Agric. Biol. Chem. 46: 1393-1395.
17. Maruyama, S., Nakagomi, K., Tomizuka, N., and Suzuki, H. (1985). Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agric. Biol. Chem. 49: 1405-1409.
18. Meisel, H. (1998). Overview on milk protein-derived peptides. Int. Dairy Journal 8: 363-373.
19. Miyoshi, S., Ishikawa, H., Kaneko, T., Fukui, F., Tanaka, H., and Maruyama, S. (1991). Activity of angiotensin-converting enzyme inhibitors in a alfa-zein hydrolysate. Agric. Biol. Chem. 55: 1313-1318.
20. Paik, S. H., Camarao, G. C., Bauer, J. A., Leite, P. E., Oliveira, E. S., Camargo, A. C., et al. (1994). Effects of morphine withdrawal syndrome on endo-oligopeptidase (EC 3.4.22.19) activity. Eur. J. Pharmacol. 253(1-2): 101-106.
21. Pierotti, A., Dong, K., Glucksman, M. J., Orlowski, M., and Roberts, J. L. (1990). Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry 29(45): 10323-10329.
22. Rioli, V., Gozzo, F. C., Heimann, A. S., Linardi, A., Krieger, J. E., Shida, C. S., et al. (2003). Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. J. Biol. Chem. 278(10): 8547-8555.
23. Rodrigues, M. S., Schaffel, R., and Assreuy, J. (1992). Comparative study on the mechanism of bradykinin potentiation induced by bradykinin-potentiating peptide 9a, enalaprilat and kinin potentiating peptide. Eur. J. Pharmacol. 216: 357-362.
24. Seppo, L., Jauhiainem, T., Poudda, T., and Korpella, R. (2003). A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects. Am. J. Clin. Nutr. 77: 326-330.
25. Stewart, J. M. (1975). Synthesis and properties of new bradykinin potentiating peptides. J. Med. Chem. 18(2): 130-133.
26. Teschemacher, H., and Brantl, V. (1994). Milk protein derived atypical opioid peptides and related compounds with opioid antagonist activity. In: Brantl, V., and Teschemacher, H. (eds.), β-Casomorphins and Related Peptides: Recent Developments. VCH, Weinhein, pp. 3-17.
27. Van Eick, A. J. (1967). A change in the response of the mouse in the "hot plate" analgesia-test, owing to a central action of atropine and related compounds. Acta Physiol. Pharmacol. Neerl. 14(4): 499-500.
28. Vickers, C., Hales, P., Kaushik, V., Dick, L., Gavin, J., Tang, J., et al. (2002). Hydrolysis of biological peptides by human angiotensin converting enzyme related carboxypeptidase. J. Biol. Chem. 277(17): 14838-14843.
29. Ward, P. E., Chow, A., and Drapeau, G. (1991). Metabolism of bradykinin agonists and antagonists by plasma aminopeptidase P. Biochem. Pharmacol. 42: 721-727.
30. Yong, T., Gao, P. X., Koizumi, S., Conlon, J. M., Rennard, S. I., Mayhan, W. G., and Rubinstein, I. (1992). Role of peptidases in bradykinin induced increase in vascular permeability in vivo. Circ. Res. 70: 952-959.