Endopeptidases 3.4.24.15 and 24.16 in endothelial cells: Potential role in vasoactive peptide metabolism

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 284, Issue 6 53-6, 2003, Pages

  Norman, M Ursula ^a   Reeve, Shane B ^a   Dive, Vincent ^b   Smith, A Ian ^a   Lew, Rebecca A ^a  

^a BAKER IDI HEART AND DIABETES INSTITUTE   (Australia)

^b CEA SACLAY   (France)

Author keywords

Bradykinin; Endothelium; Inhibitor; Peptidase

Indexed keywords

7 METHOXYCOUMARIN 4 ACETYLPROLYLLEUCYLGLYCYL DEXTRO LYSINE (2,4 DINITROPHENYL); BRADYKININ; COUMARIN DERIVATIVE; NEUROLYSIN; NEUROTENSIN; THIMET OLIGOPEPTIDASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CARDIOVASCULAR FUNCTION; CELL CULTURE; CELL MEMBRANE; CELL TRANSFORMATION; CYTOSOL; ENDOTHELIUM CELL; HUMAN; HUMAN CELL; HYPOTENSION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM;

EID: 0037686695     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.01116.2002     Document Type: Article

References (32)

1. Authier F, Posner BI, and Bergeron JJM. Insulin-degrading enzyme. Clin Invest Med 19: 149-160, 1996.
2. Barnes K, Shimada K, Takahashi M, Tanzawa K, and Turner AJ. Metallopeptidase inhibitors induce an up-regulation of endothelin-converting enzyme levels and its redistribution from the plasma membrane to an intracellular compartment. J Cell Sci 109: 919-928, 1996.
3. Chu TG and Orlowski M. Active site directed N-carboxy-methyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. Biochemistry 23: 3598-3603, 1984.
4. Crack PJ, Wu TJ, Cummins PM, Ferro ES, Tullai JW, Glucksman MJ, and Roberts JL. The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane. Brain Res 835: 113-124, 1999.
5. Dendorfer A, Wolfrum S, Schafer U, Stewart JM, Inamura N, and Dominiak P. Potentiation of the vascular response to kinins by inhibition of myocardial kininases. Hypertension 35: 32-37, 2000.
6. Edgell CJS, McDonald CC, and Graham JB. Permanent cell line expressing factor VIII related antigen established by hybridization. Proc Natl Acad Sci USA 80: 3734-3737, 1983.
7. Ferro ES, Tambourgi DV, Gobersztejn F, Gomes MD, Sucupira M, Armelin MCS, Kipnis TL, and Camargo ACM. Secretion of a neuropeptide-metabolizing enzyme similar to endopeptidase 22.19 by glioma C6 cells. Biochem Biophys Res Commun 191: 275-281, 1993.
8. Ferro ES, Tullai JW, Glucksman MJ, and Roberts JL. Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15). DNA Cell Biol 18: 781-789, 1999.
9. Fontenele-Neto JD, Massarelli EE, Garrido PAG, Beaudet A, and Ferro ES. Comparative fine structural distribution of endopeptidase 24.15 (EC342415) and 2416 (EC3.4.24.16) in rat brain. J Comp Neurol 438: 399-410, 2001.
10. Glucksman MJ and Roberts JL. Strategies for characterizing, cloning, and expressing soluble endopeptidases. In: Peptidases and Neuropeptide Processing, edited by Smith AI. San Diego, CA: Academic, 1995, p. 296-316.
11. Goldsmith JC, McCormick JJ, and Yen A. Endothelial cell cycle kinetics. Changes in culture and correlation with endothelial properties. Lab Invest 51: 643-647, 1984.
12. Hoang MV and Turner AJ. Novel activity of endothelin-converting enzyme: hydrolysis of bradykinin. Biochem J 327: 23-26, 1997.
13. Jiracek J, Yiotakis A, Vincent B, Lecoq A, Nicolaou A, Checler F, and Dive V. Development of highly potent and selective phosphinic peptide inhibitors of zinc endopeptidase 24.15 using combinatorial chemistry. J Biol Chem 270: 21701-21706, 1995.
14. Johnson AR. Human pulmonary endothelial cells in culture. Activities of cells from arteries and cells from veins. J Clin Invest 65: 841-850, 1980.
15. Lew RA, Hey NJ, Tetaz TJ, Glucksman MJ, Roberts JL, and Smith AI. Substrate specificity differences between recombinant rat testes endopeptidase EC 3.4.24.15 and the native brain enzyme. Biochem Biophys Res Commun 209: 788-795, 1995.
16. Lew RA, Tetaz T, and Smith AI. Characterization of a membrane-associated EC 3.4.24.15-like endopeptidase expressed by endothelial cells of the ovine median eminence. J Neuroendocrinol 6: 225-232, 1994.
17. Linz W, Wiemer G, Gohlke P, Unger T, and Scholkens BA. Contribution of kinins to the cardiovascular actions of angiotensin-converting enzyme inhibitors. Pharmacol Rev 47: 25-49, 1995.
18. Llorens-Cortes C, Huang H, Vicart P, Gasc JM, Paulin D, and Corvol P. Identification and characterization of neutral endopeptidase in endothelial cells from venous or arterial origins. J Biol Chem 267: 14012-14018, 1992.
19. Lowry OH, Rosebrough NJ, Farr AL, and Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 193: 265-275, 1951.
20. Norman MU, Smith AI, and Lew RA. Role of calcium in the release of the bradykinin-degrading peptidase EC 3.4.24.16 from endothelial cells. Lett Peptide Sci 6: 349-352, 1999.
21. Rioli V, Kato A, Portaro FC, Cury GK, te Kaat K, Vincent B, Checler F, Camargo AC, Glucksman MJ, Roberts JL, Hirose S, and Ferro ES. Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family: comparison with the related recombinant endopeptidase 3.4.24.15. Biochem Biophys Res Commun 250: 5-11, 1998.
22. Schriefer JA, Broudy EP, and Hassen AH. Endopeptidase inhibitors decrease myocardial ischemia/reperfusion injury in an in vivo rabbit model. J Pharmacol Exp Ther 278: 1034-1039, 1996.
23. Schriefer JA, Broudy EP, and Hassen AH. Inhibitors of bradykinin-inactivating enzymes decrease myocardial ischemia/reperfusion injury following 3 and 7 days of reperfusion. J Pharmacol Exp Ther 298: 970-975, 2001.
24. Shrimpton CN, Abbenante G, Lew RA, and Smith AI. Development and characterisation of novel potent and stable inhibitors of endopeptidase EC 3.4.24.15. Biochem J 345: 351-356, 2000.
25. Skidgel RA. Bradykinin-degrading enzymes: structure, function, distribution, and potential roles in cardiovascular pharmacology. J Cardiovasc Pharmacol 20, Suppl 9: S4-S9, 1992.
26. Smith AI, Lew RA, Shrimpton CN, Evans RG, and Abbenante G. A novel stable inhibitor of endopeptidases EC 3.4.24.15 and 3.4.24.16 potentiates bradykinin-induced hypotension. Hypertension 35: 626-630, 2000.
27. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, and Klenk DC. Measurement of protein using bicinchoninic acid. Anal Biochem 150: 76-85, 1985.
28. Vincent B, Beaudet A, Dauch P, Vincent JP, and Checler F. Distinct properties of neuronal and astrocytic endopeptidase 3.4.24.16: a study on differentiation, subcellular distribution, and secretion processes. J Neurosci 16: 5049-5059, 1996.
29. Vincent B, Dauch P, Vincent JP, and Checler F. Stably transfected human cells overexpressing rat brain endopeptidase 3.4.24.16: biochemical characterization of the activity and expression of soluble and membrane-associated counterparts. J Neurochem 68: 837-845, 1997.
30. Vincent B, Jiracek J, Noble F, Loog M, Roques B, Dive V, Vincent JP, and Checler F. Effect of a novel selective and potent phosphinic peptide inhibitor of endopeptidase 3.4.24.16 on neurotensin-induced analgesia and neuronal inactivation. Br J Pharmacol 121: 705-710, 1997.
31. Woulfe J, Checler F, and Beaudet A. Light and electron microscopic localization of the neutral metalloendopeptidase EC 3.4.24.16 in the mesencephalon of the rat. Eur J Neurosci 4: 1309-1319, 1992.
32. Yang Z, Arnet U, von Segesser L, Siebenmann R, Turina M, and Luscher TF. Different effects of angiotensin-converting enzyme inhibition in human arteries and veins. J Cardiovasc Pharmacol 22, Suppl 5: S17-S22, 1993.