Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism

Biochemical Journal

Volumn 383, Issue 1, 2004, Pages 45-51

  Rice, Gillian I ^a,b   Thomas, Daniel A ^a   Grant, Peter J ^b   Turner, Anthony J ^a   Hooper, Nigel M ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b LEEDS GENERAL INFIRMARY   (United Kingdom)

Author keywords

Active site titration; Angiotensin converting enzyme; Cardiovascular disease; Neprilysin; Renin angiotensin system; Vasopeptidase

Indexed keywords

BIODEGRADATION; BLOOD; ELECTROLYTES; ENZYME KINETICS; HEMODYNAMICS; POLYPEPTIDES; PRESSURE EFFECTS;

ANGIOTENSIN PEPTIDES; BLOOD PRESSURE; ELECTROLYTE HOMOEOSTASIS;

ENZYMES;

ALDOSTERONE; ANGIOTENSIN; ANGIOTENSIN CONVERTING ENZYME 2; ANGIOTENSIN[1-7]; ANGIOTENSIN[1-9]; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; MEMBRANE METALLOENDOPEPTIDASE; PEPTIDE; RENIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BLOOD PRESSURE; CARDIOVASCULAR DISEASE; CHO CELL; COMPETITIVE INHIBITION; CONTROLLED STUDY; DRUG EFFECT; ELECTROLYTE BALANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SPECIFICITY; FLUID BALANCE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN METABOLISM; RENIN ANGIOTENSIN ALDOSTERONE SYSTEM; VASOCONSTRICTION; VASODILATATION;

ANGIOTENSIN I; ANGIOTENSIN II; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANGIOTENSINS; ANIMALS; BINDING SITES; CARBOXYPEPTIDASES; CHO CELLS; CRICETINAE; CRICETULUS; HUMANS; HYDROLYSIS; KINETICS; NEPRILYSIN; PEPTIDE FRAGMENTS; PEPTIDYL-DIPEPTIDASE A; SUBSTRATE SPECIFICITY;

ANIMALIA; FELIS CATUS;

EID: 6344246036     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040634     Document Type: Article

References (51)

1. Soubrier, F., Hubert, C., Testut, P., Nadaud, S., Alhenc-Gelas, F. and Corvol, P. (1993) Molecular biology of the angiotensin I converting enzyme: I. biochemistry and structure of the gene. J. Hypertens. 11, 471-476
2. Rice, G. I., Foy, C. A. and Grant, P. J. (1999) Angiotensin converting enzyme and angiotensin II type 1-receptor gene polymorphisms and risk of ischaemic heart disease. Cardiovasc. Res. 41, 746-753
3. Dzau, V. J. (1994) Cell biology and genetics of angiotensin in cardiovascular disease. J. Hypertens. 12, S3-S10
4. Brown, N. J. and Vaughan, D. E. (1996) The renin-angiotensin and fibrinolytic systems: co-conspirators in the pathogenesis of ischemic cardiovascular disease. Trends Cardiovasc. Med. 6, 239-243
5. Fluharty, S. J., Reagan, L. P. and Yee, D. K. (1995) The angiotensin type 1 and type 2 receptor families: siblings or cousins? In Tissue Renin-Angiotensin Systems (Mukhopadhyay, A. K. and Raizada, M. K., eds.), pp. 193-211, Plenum Press, New York
6. Carretero, O. A. and Oparil, S. (2000) Essential hypertension. Part II: treatment. Circulation 101, 446-453
7. Fonarow, G. C. (2000) Heart failure: recent advances in prevention and treatment. Rev. Cardiovasc. Med. 1, 25-33
8. Tipnis, S. R., Hooper, N. M., Hyde, R., Karran, E., Christie, G. and Turner, A. J. (2000) A human homolog of angiotensin-converting enzyme: cloning and functional expression as a captopril-insensitive carboxypeptidase. J. Biol. Chem. 275, 33238-33243
9. Donoghue, M., Hsieh, F., Baronas, E., Godbout, K., Gosselin, M., Stagliano, N., Donovan, M., Woolf, B., Robinson, K., Jeyaseelan, R. et al. (2000) A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ. Res. 87, e1-e9
10. Vickers, C., Hales, P., Kaushik, V., Dick, L., Gavin, J., Tang, J., Godbout, K., Parsons, T., Baronas, E., Hsieh, F. et al. (2002) Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. J. Biol. Chem. 277, 14838-14843
11. Deddish, P. A., Marcic, B., Jackman, H. L., Wang, H.-Z., Skidgel, R. A. and Erdös, E. G. (1998) N-domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: angiotensin-(1-7) and keto-ACE. Hypertension 31, 912-917
12. Ferrario, C. M., Chappell, M. C., Tallant, E. A., Brosnihan, K. B. and Diz, D. I. (1997) Counterregulatory actions of angiotensin-(1-7). Hypertension 30, 535-541
13. Turner, A. J. and Hooper, N. M. (2002) The angiotensin-converting enzyme gene family: genomics and pharmacology. Trends Pharmacol. Sci. 23, 177-183
14. Mattei, M.-G., Hubert, C., Alhenc-Gelas, F., Roeckel, N., Corvol, P. and Soubrier, F. (1989) Angiotensin-l converting enzyme gene is on chromosome 17. Cytogenet. Cell Genet. 51, 1041
15. Hubert, C., Houot, A.-M., Corvol, P. and Soubrier, F. (1991) Structure of the angiotensin I-converting enzyme gene: two alternative promoters correspond to evolutionary steps of a duplicated gene. J. Biol. Chem. 266, 15377-15383
16. Soubrier, F., Alhenc-Gelas, F., Hubert, C., Allegrini, J., John, M., Tregear, G. and Corvol, P. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc. Natl. Acad. Sci. U.S.A. 85, 9386-9390
17. Wei, L., Alhenc-Gelas, R., Corvol, P. and Clauser, E. (1991) The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266, 9002-9008
18. Campbell, D. J. (2003) Vasopeptidase inhibition: a double-edged sword? Hypertension 41, 383-389
19. Turner, A. J., Isaac, R. E. and Coates, D. (2001) The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. BioEssays 23, 261-269
20. Erdös, E. G. and Skidgel, R. A. (1989) Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3, 145-151
21. Hooper, N. M., Hryszko, J., Oppong, S. Y. and Turner, A. J. (1992) Inhibition by converting enzyme inhibitors of pig kidney aminopeptidase P. Hypertension 19, 281-285
22. Wei, L, Alhenc-Gelas, F., Soubrier, F., Michaud, A., Corvol, P. and Clauser, E. (1991) Expression and characterization of recombinant human angiotensin I-converting enzyme: evidence for a C-terminal transmembrane anchor and for a processing of the secreted recombinant and plasma enzymes. J. Biol. Chem. 266, 5540-5546
23. Hooper, N. M., Keen, J., Pappin, D. J. C. and Turner, A. J. (1987) Pig kidney angiotensin converting enzyme: purification and characterization of amphipathic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane. Biochem. J. 247, 85-93
24. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J. and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85
25. Dive, V., Cotton, J., Yiotakis, A., Michaud, A., Vassiliou, S., Jiracek, J., Vazeux, G., Chauvet, M.-T., Cuniasse, P. and Corvol, P. (1999) 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, 4330-4335
26. Mumford, R. A., Strauss, A. W., Powers, J. C., Pierzchala, P. A., Nishino, N. and Zimmerman, M. (1980) A zinc metalloendopeptidase associated with dog pancreatic membranes. J. Biol. Chem. 255, 2227-2230
27. α-[(S)-1- carboxy-3-phenylpropyl]L-lysyl-L-proline. J. Biol. Chem. 260, 2952-2962
28. Rose, C., Voisin, S., Gros, C., Schwartz, J.-C. and Ouimet, T. (2002) Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin. Biochem. J. 363, 697-705
29. Williams, J. W. and Morrison, J. F. (1979) The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63, 437-467
30. Woodman, Z. L., Oppong, S. Y., Cook, S., Hooper, N. M., Schwager, S. L. U., Brandt, W. F., Ehlers, M. R. W. and Sturrock, E. D. (2000) Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites. Biochem. J. 347, 711-718
31. Bull, H. G., Thornberry, N. A. and Cordes, E. H. (1985) Purification of angiotensin-converting enzyme from rabbit lung and human plasma by affinity chromatography. J. Biol. Chem. 260, 2963-2972
32. Cotton, J., Hayashi, M. A. F., Cuniasse, P., Vazeux, G., Ianzer, D., De Camargo, A. C. M. and Dive, V. (2002) Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides. Biochemistry 41, 6065-6071
33. Bunning, P., Budek, W., Escher, R. and Schonherr, E. (1986) Characteristics of angiotensin converting enzyme and its role in the metabolism of angiotensin I by endothelium. J. Cardiovasc. Pharmacol. 8, S52-S57
34. 1098 is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity. J. Biol. Chem. 276, 33518-33525
35. Nakagomi, K., Yamada, R., Ebisu, H., Sadakane, Y., Akizawa, T. and Tanimura, T. (2000) Isolation of acein-2, a novel angiotensin-1-converling enzyme inhibitory peptide derived from a tryptic hydrolysate of human plasma. FEBS Lett. 467, 235-238
36. Gafford, J. T., Skidgel, R. A., Erdös, E. G. and Hersh, L. B. (1983) Human kidney "enkephalinase", a neutral metalloendopeptidase that cleaves active peptides. Biochemistry 22, 3265-3271
37. Guy, J. L., Jackson, R. M., Acharya, K. R., Sturrock, E. D., Hooper, N. M. and Turner, A. J. (2003) Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence. Biochemistry 42, 13185-13192
38. Binevski, P. V., Sizova, E. A., Pozdnev, V. F. and Kost, O. A. (2003) Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme. FEBS Lett. 550, 84-88
39. Georgiadis, D., Beau, F., Czarny, B., Cotton, J., Yiotakis, A. and Dive, V. (2003) Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin. Circ. Res. 93, 148-154
40. Marcic, B., Deddish, P. A., Jackman, H. L., Erdös, E. G. and Tan, F. (2000) Effects of the N-terminal sequence of ACE on the properties of its C-domain. Hypertension 36, 116-121
41. Lawrence, A. C., Evin, G., Kladis, A. and Campbell, D. J. (1990) An alternative strategy for the radioimmunoassay of angiotensin peptides using amino-terminal-directed antisera: measurement of eight angiotensin peptides in human plasma. J. Hypertens. 8, 715-724
42. Erdös, E. G., Jackman, H. L., Brovkovych, V., Tan, F. and Deddish, P. A. (2002) Products of angiotensin I hydrolysis by human cardiac enzymes potentiate bradykinin. J. Mol. Cell. Cardiol. 34, 1569-1576
43. Sibinga, N. E. S. and Ware, J. A. (2000) A pair of ACEs, for openers? Circ. Res. 87, 523-525
44. Bernstein, K. E. (2002) Two ACEs and a heart. Nature (London) 417, 799-802
45. Oudit, G. Y., Crackower, M. A., Backx, P. H. and Penninger, J. M. (2003) The role of ACE2 in cardiovascular physiology. Trends Cardiovasc. Med. 13, 93-101
46. Yagil, Y. and Yagil, C. (2003) Hypothesis: ACE2 modulates blood pressure in the mammalian organism. Hypertension 41, 871-873
47. Jackman, H. L., Massad, M. G., Sekosan, M., Tan, F., Brovkovych, V., Marcic, B. M. and Erdös, E. G. (2002) Angiotensin 1-9 and 1-7 release in human heart: role of cathepsin A. Hypertension 39, 976-981
48. Kokkonen, J. O., Saarinen, J. and Kovanen, P. T. (1997) Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid: inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin-converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity. Circulation 95, 1455-1463
49. Crackower, M. A., Sarao, R., Oudit, G. Y., Yagil, C., Kozieradzki, I.,Scanga, S. E., Oliveira-dos-Santos, A. J., Costa, J. D., Zhang, L, Pei, Y. et al. (2002) Angiotensin-converting enzyme 2 is an essential regulator of heart function. Nature (London) 417, 822-528
50. Zisman, L. S., Keller, R. S., Weaver, B., Lin, Q., Speth, R., Bristow, M. R. and Canver, C. C. (2003) Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme homologue ACE2. Circulation 108, 1707-1712
51. Zisman, L. S., Meixell, G. E., Bristow, M. R. and Canver, C. C. (2003) Angiotensin-(1-7) formation in the intact human heart: in vivo dependence on angiotensin II as substrate. Circulation 108, 1679-1681