Sensitive substrates for neprilysin (neutral endopeptidase) and thermolysin that are highly resistant to serine proteases

FEBS Letters

Volumn 380, Issue 1-2, 1996, Pages 79-82

  Spungin Bialik, Anya ^a   Ben Meir, Daniella ^a   Fudim, Ella ^a   Carmeli, Shmuel ^a   Blumberg, Shmaryahu ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

CALLA CD 10; Neprilysin; Neutral endopeptidase; Serine protease; Substrate selectivity; Thermolysin

Indexed keywords

CHYMOTRYPSIN; MEMBRANE METALLOENDOPEPTIDASE; SERINE PROTEINASE; SUBTILISIN; THERMOLYSIN; TRIPEPTIDE DERIVATIVE;

ARTICLE; CONTROLLED STUDY; ENZYME KINETICS; ENZYME SPECIFICITY; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

CALLA; FELIS CATUS;

EID: 0030066879     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(96)00008-7     Document Type: Article

References (28)

1. Kerr, M.A. and Kenny, A.J. (1974) Biochem. J. 137, 477-488.
2. Gee, N.S., Bowes, M.A., Buck, P. and Kenny, A.J. (1985) Biochem. J. 228, 119-126.
3. Ronco, P., Pollard, H., Galceran, M., Delauche, M., Schwartz, J.C. and Verroust, P. (1988) Lab. Invest. 58, 210-217.
4. Matthews, B.W., Colman, P.M., Jansonius, J.N., Titani, K., Walsh, K.A. and Neurath, H. (1972) Nature New Biol. 238, 41-43.
5. Blumberg, S., Vogel, Z. and Altstein, M. (1981) Life Sci. 28, 301-306.
6. Pozsgay, M., Michaud, C., Liebman, M. and Orlowski, M. (1986) Biochemistry 25, 1292-1299.
7. Erdös, E.G. and Skidgel, R.A. (1989) FASEB J. 4, 145-151.
8. Roques, B.P., Noble, F., Dauge, V., Fournie-Zaluski, M.-C. and Beaumunt, A. (1993) Pharmacol. Rev. 45, 87-146.
9. Letarte, M., Vera, S., Tran, R., Addis, J.B.L., Onizuka, R.J., Quackenbush, E.J., Jongeneel, C.V. and McInnes, R.R. (1988) J. Exp. Med. 168, 1247-1253.
10. Shipp, M.A., Vijayaraghavan, J., Schmidt, E.V., Masteller, E.L., D'Adamio, L., Hersh, L.B. and Reinherz, E.L. (1989) Proc. Natl. Acad. Sci. USA 86, 297-301.
11. Malfroy, B., Kuang, W.J., Seeburg, P.H., Mason, A.J. and Schofield, P.R. (1988) FEBS Lett. 229, 206-210.
12. Mumford, R.A., Pierzchala, P.A., Strauss, A.W. and Zimmerman, M. (1981) Proc. Natl. Acad. Sci. USA 78, 6623-6627.
13. Hersh, L.B. and Morihara, K. (1986) J. Biol. Chem. 261, 6433-6437.
14. Indig, F.E., Ben-Meir, D., Spungin, A. and Blumberg, S. (1989) FEBS Lett. 255, 237-240.
15. Blumberg, S. and Katchalski-Katzir, E. (1979) Biochemistry 18, 2126-2133.
16. Martin, G.E. and Zektzer, A.S. (1988) Two Dimensional NMR Methods for Establishing Molecular Connectivity, VCH Publ. Inc., New York and Weinheim, pp. 1-490.
17. Latt, S.A., Holmquist, B. and Vallee, B.L. (1969) Biochem. Biophys. Res. Commun. 37, 333-339.
18. 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 Klcnk, D.C. (1985) Anal. Biochem. 150, 76-85.
19. Spungin, A. and Blumberg, S. (1989) Eur. J. Biochem. 183, 471-477.
20. Prescott, J.M. and Wilkes, S.H. (1976) Methods Enzymol. 45, 530-543.
21. Schechter, I. and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157-162.
22. Kasafirek, E., Fric, P. and Malis, F. (1976) Eur. J. Biochem. 69, 1-13.
23. Stambolieva, N.A., Ivanova, I.P. and Yomtova, V.M. (1992) Arch. Biochem. Biophys. 294, 703-706.
24. Segal, D.M., Powers, J.C., Cohen, G.H., Davies, D.R. and Wilcox, P.E. (1971) Biochemistry 10, 3728-3738.
25. Robertus, J.D., Alden, R.A., Birktoft, J.J., Kraut, J., Powers, J.C. and Wilcox, P.E. (1972) Biochemistry 11, 2439-2449.
26. Bode, W., Papamokos, E. and Musil, D. (1987) Eur. J. Biochem. 166, 673-692.
27. Kester, W.R. and Matthews, B.W. (1977) Biochemistry 16, 2506-2516.
28. Matthews, B.W. (1988) Acc. Chem. Res. 21, 333-340.