Restriction of the in vitro formation of angiotensin II by leucinyl-arginyl-tryptophan, a novel peptide with potent angiotensin I-converting enzyme inhibitory activity

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 5, 2006, Pages 1277-1280

  Wu, Jianping ^a   Yuan, Lujiang ^a,b   Aluko, Rotimi E ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

^b SOUTHWEST UNIVERSITY   (China)

Author keywords

Angiotensin converting enzyme; Angiotensin II; Competitive inhibitor; Leucinyl arginyl tryptophan (LRW)

Indexed keywords

BIOCHEMISTRY; COMPUTER SIMULATION; ENZYME INHIBITION; ENZYME KINETICS;

ANGIOTENSIN CONVERTING ENZYME; ANGIOTENSIN II; COMPETITIVE INHIBITOR; LEUCINYL-ARGINYL-TRYPTOPHAN (LRW);

ENZYMES;

DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; LEUCINYL ARGINYL TRYPTOPHAN; LEUCINYL-ARGINYL-TRYPTOPHAN; OLIGOPEPTIDE;

ARTICLE; DRUG EFFECT; HUMAN;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; HUMANS; OLIGOPEPTIDES; PEPTIDYL-DIPEPTIDASE A;

EID: 33646787492     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70.1277     Document Type: Article

References (19)

1. Zaman, M. A., Oparil, S., and Calhoun, D. A., Drugs targeting the renin-angiotensin-aldosterone system. Nat. Rev. Drug Discov., 1, 621-626 (2002).
2. Skeggs, L. T., Kahn, J. R., and Shumway, N. P., The preparation and function of the hypertensin-converting enzyme. J. Exp. Med., 103, 295-299 (1956).
3. Urata, H., Kinoshita, A., Misono, K., Bumpus, F. M., and Hussain, A., Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart. J. Biol. Chem., 265, 22348-22357 (1990).
4. Wu, J., Aluko, R. E., and Nakai, S., Structural requirements of angiotensin-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides. J. Agric. Food Chem., 54, 732-738 (2006).
5. Cushman, D. W., and Cheung, H. S., Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol., 20, 1637-1648 (1971).
6. Lineweaver, H., and Burk, D., The determination of enzyme dissociation constants. J. Am. Chem. Soc., 56, 658-666 (1934).
7. Fruitier-Arnaudin, I., Cohen, M., Bordenave, S., Sannier, F., and Piot, J. M., Comparative effects of angiotensin IV and two hemorphins on angiotensin-converting enzyme activity. Peptides, 23, 1465-1470 (2002).
8. Fujita, H., Yokoyama, K., and Yoshikawa, M., Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food protein. J. Food Sci., 65, 564-569 (2000).
9. Miyoshi, S., Ishikawa, H., Kaneko, T., Fukui, F., Tanaka, H., and Maruyama, S., Structures and activity of angiotensin-converting enzyme inhibitors in α-zein hydrolysate. Agric. Biol. Chem., 55, 1313-1318 (1991).
10. Yang, Y., Marczak, E. D., Yokoo, M., Usui, H., Kawamura, Y., and Yoshikawa, M., Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach rubisco. J. Agric. Food Chem., 51, 4897-4902 (2003).
11. 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. Peptide Sci., 5, 289-297 (1999).
12. Kohama, Y., Oka, H., Kayamori, Y., Tsujikawa, K., Mimura, T., Nagase, Y., and Satake, M., Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from tuna muscle. Agric. Biol. Chem., 55, 2169-2170 (1991).
13. Kohama, Y., Oka, H., Matsumoto, S., Teramoto, T., Okaba, M., Mimura, T., Nagase, Y., Chiba, Y., and Fujita, T., Induction of angiotensin-converting enzyme inhibitory activity by acid-limited proteolysis of glyceraldehyde 3-phosphate dehydrogenase. Biochem. Biophys. Res. Commun., 161, 456-460 (1989).
14. FitzGerald, R. J., Murray, B. A., and Walsh, D. J., Hypotensive peptides from milk proteins. J. Nutr., 134, 980S-988S (2004).
15. Cheung, H. S., and Cushman, D. W., Inhibition of homogeneous angiotensin I-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops Jararaca. Biochim. Biophys. Acta, 293, 451-463 (1973).
16. Pihlanto-Leppälä, A., Rokka, T., and Korhonen, H., Angiotensin I-converting enzyme inhibitory peptides derived from bovine milk proteins. Int. Dairy J., 8, 325-331 (1998).
17. 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, 4033-4039 (1971).
18. Meng, Q. C., Balcells, E., Dell'italia, L., Durand, J., and Oparil, S., Sensitive method for quantitation of angiotensin-converting enzyme (ACE) activity in tissue. Biochem. Pharmacol., 50, 1445-1450 (1995).
19. Kohama, Y., Oka, H., Matsumoto, S., Nakagawa, T., Miyamoto, T., Teramoto, T., Mimura, T., Nagase, Y., Satake, M., Takane, T., and Fujita, T., Biological properties of angiotensin-converting enzyme inhibitor derived from tuna muscle. J. Pharmacobiodyn., 12, 566-571 (1989).