Angiotensin-converting enzyme (ACE) inhibitors have different selectivity for bradykinin binding sites of human somatic ACE

European Journal of Pharmacology

Volumn 577, Issue 1-3, 2007, Pages 1-6

  Ceconi, Claudio ^a,b   Francolini, Gloria ^b   Olivares, Adriana ^b   Comini, Laura ^b   Bachetti, Tiziana ^b   Ferrari, Roberto ^a  

^a UNIVERSITY OF FERRARA   (Italy)

^b IRCCS   (Italy)

Author keywords

ACE; ACE inhibitor; Angiotensin I; Binding affinity; Bradykinin; Cardiovascular disease; HUVEC; Perindopril; Perindoprilat; Selectivity

Indexed keywords

ANGIOTENSIN I; ANGIOTENSIN II; BRADYKININ; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENALAPRILAT; IODINE 125; N (1 CARBOXY 3 PHENYLPROPYL)LYSYLPROLINE 4 HYDROXYBENZAMIDINE; PERINDOPRILAT; QUINAPRILAT; RAMIPRILAT; TRANDOLAPRILAT;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DRUG BINDING; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; ISOTOPE LABELING; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; BINDING SITES; BINDING, COMPETITIVE; BRADYKININ; CELLS, CULTURED; ENDOTHELIUM; HUMANS; PEPTIDYL-DIPEPTIDASE A; RECEPTORS, BRADYKININ;

EID: 35448931632     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejphar.2007.07.061     Document Type: Article

References (30)

1. Bertrand M.E. Provision of cardiovascular protection by ACE inhibitors: a review of recent trials. Curr. Med. Res. Opin. 20 (2004) 1559-1569
2. Braunwald E., Domanski M.J., Fowler S.E., Geller N.L., Gersh B.J., Hsia J., Pfeffer M.A., Rice M.M., Rosenberg Y.D., and Rouleau J.L. Angiotensin-converting-enzyme inhibition in stable coronary artery disease. N. Engl. J. Med. 351 (2004) 2058-2068
3. Brown N.J., and Vaughan D.E. Angiotensin-converting enzyme inhibitors. Circulation 97 (1998) 1411-1420
4. Bull H.G., Thornberry N.A., Cordes M.H., Patchett A.A., and Cordes E.H. Inhibition of rabbit lung angiotensin-converting enzyme by N alpha-[(S)-1-carboxy-3-phenylpropyl]l-alanyl-l-proline and N alpha-[(S)-1-carboxy-3-phenylpropyl]l-lysyl-l-proline. J. Biol. Chem. 260 (1985) 2952-2962
5. Ceconi C., Fox K.M., Remme W.J., Simoons M.L., Bertrand M., Parrinello G., Kluft C., Blann A., Cokkinos D., and Ferrari R. ACE inhibition with perindopril and endothelial dysfunction. Results of a substudy of the EUROPA study: PERTINENT. Cardiovasc. Res. 73 (2007) 237-246
6. Dive V., Cotton J., Yiotakis A., Michaud A., Vassiliou S., Jiracek J., Vazeux G., Chauvet M.T., Cuniasse P., and Corvol P. RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 4330-4335
7. Dzau V.J., Bernstein K., Celermajer D., Cohen J., Dahlof B., Deanfield J., Diez J., Drexler H., Ferrari R., Van Gilst W., Hansson L., Hornig B., Husain A., Johnston C., Lazar H., Lonn E., Luscher T., Mancini J., Mimran A., Pepine C., Rabelink T., Remme W., Ruilope L., Ruzicka M., Schunkert H., Swedberg K., Unger T., Vaughan D., and Weber M. Pathophysiologic and therapeutic importance of tissue ACE: a consensus report. Cardiovasc. Drugs Ther. 16 (2002) 149-160
8. Erdos E.G. The ACE and I: how ACE inhibitors came to be. FASEB J. 20 (2006) 1034-1038
9. ESC. Management of stable angina pectoris. Recommendations of the Task Force of the European Society of Cardiology. Eur. Heart J. 27 (2006) 1341-1381
10. Ferrari R. Angiotensin-converting enzyme inhibition in cardiovascular disease: evidence with perindopril. Expert. Rev. Cardiovasc. Ther. 3 (2005) 15-29
11. Fox K.M. Efficacy of perindopril in reduction of cardiovascular events among patients with stable coronary artery disease: randomised, double-blind, placebo-controlled, multicentre trial (the EUROPA study). Lancet 362 (2003) 782-788
12. Fyhrquist F., Tikkanen I., Gronhagen-Riska C., Hortling L., and Hichens M. Inhibitor binding assay for angiotensin-converting enzyme. Clin. Chem. 30 (1984) 696-700
13. Georgiadis D., Beau F., Czarny B., Cotton J., Yiotakis A., and Dive V. Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: insights from selective inhibitors. Circ. Res. 93 (2003) 148-154
14. Jaffe E.A., Nachman R.L., Becker C.G., and Minick C.R. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Invest. 52 (1973) 2745-2756
15. Jaspard E., Wei L., and Alhenc-Gelas F. Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268 (1993) 9496-9503
16. Krebs L.T., Hanesworth J.M., Sardinia M.F., Speth R.C., Wright J.W., and Harding J.W. A novel angiotensin analog with subnanomolar affinity for angiotensin-converting enzyme. J. Pharmacol. Exp. Ther. 293 (2000) 260-267
17. Moncada S., and Higgs A. The l-arginine-nitric oxide pathway. N. Engl. J. Med. 329 (1993) 2002-2012
18. Moncada S., Palmer R.M., and Higgs E.A. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43 (1991) 109-142
19. 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
20. Patchett A.A., Harris E., Tristram E.W., Wyvratt M.J., Wu M.T., Taub D., Peterson E.R., Ikeler T.J., ten Broeke J., Payne L.G., Ondeyka D.L., Thorsett E.D., Greenlee W.J., Lohr N.S., Hoffsommer R.D., Joshua H., Ruyle W.V., Rothrock J.W., Aster S.D., Maycock A.L., Robinson F.M., Hirschmann R., Sweet C.S., Ulm E.H., Gross D.M., Vassil T.C., and Stone C.A. A new class of angiotensin-converting enzyme inhibitors. Nature 288 (1980) 280-283
21. Pfeffer M.A., and Frohlich E.D. Improvements in clinical outcomes with the use of angiotensin-converting enzyme inhibitors: cross-fertilization between clinical and basic investigation. Am. J. Physiol. Heart Circ. Physiol. 291 (2006) H2021-H2025
22. Pitt B., O'Neill B., Feldman R., Ferrari R., Schwartz L., Mudra H., Bass T., Pepine C., Texter M., Haber H., Uprichard A., Cashin-Hemphill L., and Lees R.S. The QUinapril Ischemic Event Trial (QUIET): evaluation of chronic ACE inhibitor therapy in patients with ischemic heart disease and preserved left ventricular function. Am. J. Cardiol. 87 (2001) 1058-1063
23. Saijonmaa O., and Fyhrquist F. Upregulation of angiotensin converting enzyme by atrial natriuretic peptide and cyclic GMP in human endothelial cells. Cardiovasc. Res. 40 (1998) 206-210
24. Saijonmaa O., Nyman T., and Fyhrquist F. Downregulation of angiotensin-converting enzyme by tumor necrosis factor-alpha and interleukin-1beta in cultured human endothelial cells. J. Vasc. Res. 38 (2001) 370-378
25. Soubrier F., Alhenc-Gelas F., Hubert C., Allegrini J., John M., Tregear G., and Corvol P. Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9386-9390
26. Tumanan-Mendozaa B.A., Dansb A.L., Lucienne Villacinc L., Mendozad V.L., Rellama-Blacke S., Bartolomef M., Ragualf J., Flor B., and Josephine Valdezg J. Dechallenge and rechallenge method showed different incidences of cough among four ACE-Is. J. Clin. Epidemiol. 60 (2007) 547-553
27. Wei L., Alhenc-Gelas F., Corvol P., and Clauser E. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266 (1991) 9002-9008
28. Wei L., Clauser E., Alhenc-Gelas F., and Corvol P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267 (1992) 13398-13405
29. Yusuf S., Sleight P., Pogue J., Bosch J., Davies R., and Dagenais G. Effects of an angiotensin-converting-enzyme inhibitor, ramipril, on cardiovascular events in high-risk patients. The Heart Outcomes Prevention Evaluation Study Investigators. N. Engl. J. Med. 342 (2000) 145-153
30. Zisman L.S. Inhibiting tissue angiotensin-converting enzyme: a pound of flesh without the blood?. Circulation 98 (1998) 2788-2790