Metalloprotease-mediated cleavage secretion of pulmonary ACE by vascular endothelial and kidney epithelial cells

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 271, Issue 2 40-2, 1996, Pages

  Ramchandran, Ramaswamy ^c   Kasturi, Sriram ^a   Douglas, Janice G ^c   Sen, Indira ^b  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

^c NONE

Author keywords

angiotensin converting enzyme secretase; compound 3; metalloprotease inhibitor

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; ISOENZYME; METALLOPROTEINASE INHIBITOR;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME RELEASE; KIDNEY EPITHELIUM; LUNG; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; VASCULAR ENDOTHELIUM;

EID: 33750723853     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1996.271.2.h744     Document Type: Article

References (29)

1. Beldent, V., A. Michaud, L. Wei, M.-T. Chauvet, and P. Corvol. Proteolytic release of human angiotensin-converting enzyme. J. Biol. Chem. 268: 26428-26434, 1993.
2. Bordier, C. Phase separation of integral membrane proteins in Triton X-114. J. Biol. Chem. 256: 1604-1607, 1981.
3. Caldwell, P. R. B., B. C. Seegal, K. C. Hsu, M. Das, and R. L. Soffer. Angiotensin-converting enzyme: vascular endothelial localization. Science Wash. DC 191: 1050-1051, 1976.
4. Crowe, P. D., B. N. Walter, K. M. Mohler, C. Otten-Evans, R. A. Black, and C. F. Ware. Ametalloprotease inhibitor blocks shedding of the 80-KD TNF receptor and TNF processing in T lymphocytes J. Exp. Med. 181: 1205-1210, 1995.
5. Cushman, D. W., and M. A. Ondetti. Inhibitors of angiotensin-converting enzyme. Prog. Med. Chem. 17: 41-104, 1980.
6. Deddish, P. A., J. Wang, B. Michel, P. W. Morris, N. O. Davidson, R. A. Skidgel, and E. G. Erdös. Naturally occurring active N-domain of human angiotensin I-converting enzyme. Proc. Natl. Acad. Sci. USA 91: 7807-7811, 1994.
7. Defendini, R., E. A. Zimmerman, J. A. Weare, F. Alhenc-Gelas, and E. G. Erdös. Angiotensin-converting enzyme in epithelial and neuroepithelial cells. Neuroendocrinology 37: 32-40, 1983.
8. Ehlers, M. R. W., P. Y.-N. Chen, and J. F. Riordan. Spontaneous solubilization of membrane-bound human testis angiotensin-converting enzyme in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA 88: 1009-1013, 1991.
9. Ehlers, M. R. W., P. Y.-N. Chen, and J. F. Riordon. Purification and characterization of a recombinant human testis angiotensin-converting enzyme expressed in Chinese hamster ovary cells. Protein Expr. Purif. 2:1-9, 1991.
10. El-Dorry, H. A., H. G. Bull, K, Iwata, N. A. Thornberry, E. H. Cordes, and R. L. Soffer. Molecular and catalytic properties of rabbit testicular dipeptidyl carboxypeptidase. J. Biol. Chem. 257: 14128-14133, 1982.
11. Erdös, E. G., and R. A. Skidgel. The unusual substrate specificity and the distribution of human angiotensin-coaverting enzyme. Hypertension Dallas 8 Suppl. I: I-34-I-37, 1986.
12. Erdös, E. G., and H. Y. Yang. An enzyme in microsomal fraction of kidney that inactivates bradykinin. Life Sci. 6: 569-574, 1967.
13. Hooper, N. M. Angiotensin-converting enzyme: implications from molecular biology for its physiological functions. Int. J. Biochem. 23: 641-647, 1991.
14. Hooper, N. M., J. Keen, J. C. Pappin, and A. J. Turner. Pig kidney angiotensin-converting enzyme. Biochem. J. 246: 85-93, 1987.
15. Howard, T. E., S.-Y. Shai, K. G. Langford, B. M. Martin, and K. E. Bernstein. Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene. Mol. Cell. Biol. 8: 4294-4302, 1990.
16. Hubert, C., A.-M. Houot, P. Corvol, and E. Soubrier. Structure of the angiotensin I-converting enzyme gene: two alternate promoters correspond to evolutionary steps of a duplicated gene. J. Biol. Chem. 266: 15377-15383, 1991.
17. Kasturi, S., A. M. Jabbar, G. C. Sen, and I. Sen. Role of glycosylation in the biosynthesis and activity of rabbit testicular angiotensin-converting enzyme. Biochemistry 33: 6228-6234, 1994.
18. Koop, D. R., R M. Laethem, A. L. Goldner, and J. G. Douglas. Cytochrome P450 expression and metabolism in isolated rabbit renal epithelium. Methods Enzymol. 206: 364-368, 1991.
19. Kumar, R. S., T. J. Thekkumkara, and G. C. Sen. The mRNAs encoding the two angiotensin-converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites. J. Biol. Chem. 266: 3854-3862, 1991.
20. Mohler, K. M., P. R. Sleath, J. N. Fitzner, D. P. Cerretti, M. Alderson, S. Kerwar, D. S. Torrance, C. Otten-Evans, T. Greenstreet, K. Weerawarna, S. R. Kronheim, M. Petersen, M. Gerhart, C. J. Kozolsky, C. J. March, and R. A. Black. Protection against a lethal dose of endotoxin by an inhibitor of tumor necrosis factor processing. Nature Lond. 370: 218-220, 1994.
21. Oppong, S. Y., and N. M. Hooper. Characterization of a secretase activity which releases angiotensin-converting enzyme from the membrane. Biochem. J. 292: 597-603, 1993.
22. Ramchandran, R. and I. Sen. Cleavage-processing of angiotensin-converting enzyme by a membrane-associated metalloprotease. Biochemistry 34: 12645-12652, 1995.
23. Ramchandran, R., G. C. Sen, K. Misono, and I. Sen. Regulated cleavage-secretion of the membrane-bound angiotensin-converting enzyme. J. Biol. Chem. 269: 2125-2130, 1994.
24. Sen, I., S. Kasturi, A. M. Jabbar, and G. C. Sen. Mutation in two specific residues of testicular angiotensin-converting enzyme change its catalytic properties. J. Biol. Chem. 268: 25748-25754, 1993.
25. Sen, I., H. Samanta, W. Livingston III, and G. C. Sen. Establishment of transfected cell lines producing testicular angiotensin-converting enzyme. J. Biol. Chem. 266: 21985-21990, 1991.
26. Skeggs, L. T. D., Jr., J. R. Kahn, and N. P. Shumway. Preparation and function of hypertensin converting enzyme. J. Exp. Med. 103: 295-299, 1956.
27. Thekkumkara, T. J., W. Livingston III, R. S. Kumar, and G. C. Sen. Use of alternative polyadenylation site, for tissue-specific transcription of two angiotensin-converting enzyme mRNAs. Nucleic Acids Res. 20: 683-687, 1992.
28. Wei, L., F. Alhenc-Gelas, P. Corvol, and E. Clauser. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266: 9002-9008, 1991.
29. 2 and cyclic adenosine monophosphate production in rabbit tubular epithelial cells. J. Clin. Invest. 81: 710-719, 1988.