A continuous fluorescence resonance energy transfer angiotensin I-converting enzyme assay

Nature Protocols

Volumn 1, Issue 4, 2006, Pages 1971-1976

  Carmona, Adriana K ^a   Schwager, Sylva L ^b   Juliano, Maria A ^a   Juliano, Luiz ^a   Sturrock, Edward D ^b  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSITY OF CAPE TOWN   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENOL; AMINOBENZOIC ACID; DIPEPTIDYL CARBOXYPEPTIDASE; TISSUE EXTRACT;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BODY FLUID; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; METHODOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; QUANTITATIVE ANALYSIS;

ANIMALS; FLUORESCENCE RESONANCE ENERGY TRANSFER; PEPTIDYL-DIPEPTIDASE A; RABBITS;

EID: 34248672821     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.306     Document Type: Article

References (26)

1. Skeggs, S.L.T., Jr., Kahn, J.R. & Shumway, N.P. The preparation and function of the hypertensin-converting enzyme. J. Exp. Med. 103 295-299 (1956).
2. Yang, H.Y.T., Erdös, E.G. & Levin, Y. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochem Biophis Acta 214, 374-376 (1970).
3. Dorer, F.E., Kahn, J.R., Lentz, K.E., Levine, M. & Skeggs, L.T. Hydrolysis of bradykinin by angiotensin-converting enzyme. Circ. Res. XXXIV, 824-827 (1974).
4. Rousseau, A., Michaud, A., Chauvet, M.-T., Lenfant, M. & Corvol, P. The homoregulatory peptide N-acetyl-Ser-Asp-Pro is a natural and specific substrate of N-terminal active site of angiotensin converting enzyme. J. Biol. Chem. 270, 3656-3661 (1995).
5. Jaspard, E., Wei, L. & Alhenc-Gelas, F. Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kinase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268, 9496-9503 (1993).
6. Soubrier, F. et al. Two putative active centers in human angiotensin I-converting enzyme. Proc. Natl. Acad. Sci. USA. 85 9386-9390 (1988).
7. Bernstein, K.E., Martin, B.M., Edwards, A.S. & Bernstein, E.A. Mouse angiotensin converting enzyme is a protein composed of two homologous domains. J. Biol. Chem. 264, 11945-11951 (1989).
8. Lattion, A.-L., Soubrier, F., Allegrini, J., Hubert, C., Corvol, P. & Alhenc-Gelas, F. The testicular transcript of angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 252, 99-104 (1989).
9. Ehlers, M.R.W., Fox, E.A., Strydom, D.J. & Riordan, J.F. Molecular cloning of human testicular angiotensin-converting enzyme: The testis isoenzyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. USA 86 7741-7745 (1989).
10. Wei, L. et al. Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes. J. Biol. Chem. 266, 5540-5546 (1991).
11. Beldent, V., Michaud, A., Wei, L., Chauvet, M.T. & Corvol, P. Proteolytic release of human angiotensin-converting enzyme. J. Biol. Chem. 268, 26428-26434 (1993).
12. Wei, L., Alhenc-Gelas, F., Corvol, P. & Clauser, E. The two homologous domains of angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266, 9002-9008 (1991).
13. Deddish, P.A., Jackman, H.L., Skidgel, R.A. & Erdos, E.G. Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme. Biochem. Pharmacol. 53, 1459-1463 (1997).
14. Wei, L., Clauser, E., Alhenc-Gelas, F. & Corvol, P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267, 13398-13405 (1992).
15. Foster, T. Intermolecular energy migration and fluorescence. Ann. Phys. 2, 55-75 (1948).
16. Sapsford, K.E., Berti, L. & Medintz, I.L. Materials for fluorescence resonance energy transfer analysis: Beyond traditional donor-acceptor combinations. Angew. Chem. Int. Ed. Engl. 45, 4562-4589 (2006).
17. Carmel, A. & Yaron, A. An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrate of angiotensin-I-converting enzyme and of bacterial dipeptidyl carboxypeptidase. Eur. J. Biochem. 87, 265-273 (1978).
18. Araujo, M.C. et al. Internally quenched fluorogenic substrates for angiotensin I-converting enzyme. J. Hypertens. 17, 665-672 (1999).
19. Araujo, M.C. et al. Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39, 8519-8525 (2000).
20. Chagas, J.R., Juliano, L. & Prado, E.S. Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal. Biochem. 192, 419-425 (1991).
21. Dive, V. et al. 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. USA 96, 4330-4335 (1999).
22. Bersanetti, P.A. et al. Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates. Biochemistry 43, 15729-15736 (2004).
23. Alves, M.F. et al. A continuous fluorescent assay for the determination of plasma and tissue angiotensin I-converting enzyme activity. Braz. J. Med. Biol. Res. 38, 861-868 (2005).
24. Bradford, M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
25. Eloyd, J.B.F. Standards in Fluorescence Spectroscopy (Chapman & Hall, London, 1981).
26. Liu, Y. et al. Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction. Anal. Biochem. 267, 331-335 (1999).