The Contribution of Arginine Residues within the P6-P1 Region of α1-Antitrypsin to Its Reaction with Furin

Journal of Biological Chemistry

Volumn 276, Issue 42, 2001, Pages 38971-38979

  Dufour, Erick K ^b   Denault, Jean Bernard ^b   Bissonnette, Lyne ^b   Hopkins, Paul C R ^a   Lavigne, Pierre ^b   Leduc, Richard ^b  

^a GLADSTONE INSTITUTE OF CARDIOVASCULAR DISEASE   (United States)

^b UNIVERSITY OF SHERBROOKE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYMES; MUTAGENESIS; STOICHIOMETRY;

PROTEOLYSIS;

BIOCHEMISTRY;

ALPHA 1 ANTITRYPSIN; ARGININE; ARGINYLGLUTAMYLARGINYLISOLEUCYLARGINYLARGININE; FURIN; LEUCYLGLUTAMYLALANYLISOLEUCYLPROLYLMETHIONINE; PEPTIDE DERIVATIVE; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; DODECYL SULFATE SODIUM; LEUCINE; RECOMBINANT PROTEIN; SUBTILISIN;

AMINO ACID SEQUENCE; ARTICLE; CELL STRAIN; CELL STRAIN 293; CHEMICAL PARAMETERS; CONTROLLED STUDY; EMBRYO; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STOICHIOMETRY; WILD TYPE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; IMMUNOBLOTTING; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TIME;

EQUUS ASINUS;

ALPHA 1-ANTITRYPSIN; AMINO ACID SEQUENCE; ARGININE; BINDING SITES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FURIN; IMMUNOBLOTTING; KINETICS; LEUCINE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM DODECYL SULFATE; SUBTILISINS; TIME FACTORS;

EID: 0035914296     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102959200     Document Type: Article

References (48)

1. Bergeron, F., Leduc, R., and Day, R. (2000) J. Mol. Endocrinol. 24, 1-22
2. Steiner, D. F. (1998) Curr. Opin. Chem. Biol. 2, 31-39
3. Molloy, S. S., Anderson, E. D., Jean, F., and Thomas, G. (1999) Trends Cell Biol. 9, 28-35
4. Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., and Thomas, G. (1992) J. Biol. Chem. 267, 16396-16402
5. Watanabe, T., Nakagawa, T., Ikemizu, J., Nagahama, M., Murakami, K., and Nakayama, K. (1992) J. Biol. Chem. 267, 8270-8274
6. Angliker, H., (1995) J. Med. Chem. 38, 4014-4018
7. Lazure, C., Gauthier, D., Jean, F., Boudreault, A., Seidah, N. G., Bennett, H. P., and Hendy, G. N. (1998) J. Biol. Chem. 273, 8572-8580
8. Boudreault, A., Gauthier, D., and Lazure, C. (1998) J. Biol. Chem. 273, 31574-31580
9. Cameron, A., Appel, J., Houghten, R. A., and Lindberg, I. (2000) J. Biol. Chem. 275, 36741-36749
10. Komiyama, T., and Fuller, R. S. (2000) Biochemistry. 39, 15156-15165
11. Dahlen, J. R., Jean, F., Thomas, G., Foster, D. C., and Kisiel, W. (1998) J. Biol. Chem. 273, 1851-1854
12. Anderson, E. D., Thomas, L., Hayflick, J. S., and Thomas, G. (1993) J. Biol. Chem. 268, 24887-24891
13. Dufour, E. K., Denault, J.-B., Hopkins, P. C. R., and Leduc, R. (1998) FEBS Lett. 426, 41-46
14. Jean, F., Stella, K., Thomas, T., Liu, G., Xiang, Y., Reason, A. J., and Thomas G. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 7293-7298
15. Engh, R. A., Huber, R., Bode, W., and Schulze, A. J. (1995) Trends Biotechnol. 13, 503-510
16. O'Malley, K. M., and Cooperman, B. S. (2001) J. Biol. Chem. 276, 6631-6639
17. Huntington, J. A., Read, R. J., and Carrell, R. W. (2000) Nature 407, 923-926
18. Cooperman, B. S., Stavridi, E., Nickbarg, E., Rescorla, E., Schechter, N. M., and Rubin, H. (1993) J. Biol. Chem. 268, 23616-23625
19. Nash, P., McFadden, G., and Whitty, A. (2000) FEBS Lett. 475, 1-6
20. Courtney, M., Buchwalder, A., Tessier, L.-H., Jaye, M., Benavente, A., Balland, A., Kohli, V., Lathe, R., Tolstoshev, P., and Lecocq, J.-P. (1984) Proc. Natl. Acad. Sci. U. S. A. 81, 669-673
21. Kwon, K.-S., Lee, S., and Myeong-Hee, Y. (1995) Biochim. Biophys. Acta 1247, 179-184
22. Denault, J. B., Lazure, C., Day, R., and Leduc, R. (1995) Protein Express. Purif. 19, 113-124
23. Knight, G. (1995) Methods Enzymol. 248, 85-101
24. Morrison, J. F., and Walsh, C. T. (1988) Adv. Enzymol. 61, 201-301
25. Longstaff, C., and Gaffney, P. J. (1991) Biochemistry. 30, 979-986
26. Takahashi, S., Hatsuzawa, K., Watanabe, T., Murakami, K., and Nakayama, K. (1994) J. Biochem. (Tokyo) 116, 47-52
27. Waley, S. G. (1985) Biochem. J. 227, 843-849
28. Tian, W.-X., and Tsou, C.-L. (1982) Biochemistry 21, 1028-1032
29. Wilczynska, M., Fa, M., Ohlsson, P. I., and Ny, T. (1995) J. Biol. Chem. 270, 29652-29655
30. Luo, Y., Zhou, Y., and Cooperman, B. S. (1999) J. Biol. Chem. 274, 17733-17741
31. Van de Ven, W. J. M., Creemers, J. W. M., and Roebroek, A. J. M. (1991) Enzyme 45, 257-270
32. Misumi, Y, Oda, K, Fujiwara, T, Takami, N, Tashiro, K, and Ikehara, Y. (1991) J. Biol. Chem. 266, 16954-16959
33. Drews, R., Paleyanda, R. K., Lee, T. K., Chang, R. R., Rehemtulla, A., Kaufman, R. J., Drohan, W. N., and Lubon, H. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 10462-10466
34. Hendy, G. N., Bennett, H. P., Gibbs, B. F., Lazure, C., Day, R., and Seidah, N. G. (1995) J. Biol. Chem. 270, 9517-9525
35. Siezen, R. J., Creemers, J. W. M., and Van de Ven, W. J. M. (1994) Eur. J. Biochem. 222, 255-266
36. Jean, F., Boudreault, A., Bazak, A., Seidah, N. G., and Lazure C. (1995) J. Biol. Chem. 270, 19225-19231
37. Krysan, D. J., Rockwell, N. C., and Fuller, R. S. (1999) J. Biol. Chem. 274, 23229-23234
38. Owen, M. C., George, P. M., Lane, D. A., and Boswell, D. R. (1991) FEBS Lett. 280, 216-220
39. Sherman, P. M., Lawrence, D. A., Yang, A. Y., Vandenberg, E. T., Paielli, D., Olsen, S. T., Shore, J. D., and Ginsberg, D. (1992) J. Biol. Chem. 267, 7588-7595
40. Djie, M. Z., Le Bonniec, B. F., Hopkins, P. C. R., Hipler, K., and Stone, S. R. (1996) Biochemistry 35, 11461-11469
41. Chaillan-Huntington, C. E., Gettins, P. G. W., Huntington, J. A., and Patston, P. A (1997) Biochemistry. 36, 9562-9570
42. Gettins, P. G. W., Patston, P. A., and Olson, S. T. (1996) Serpins: Structure, Function and Biology, R. G. Landes, Austin, TX
43. Miller, S. Janin, J. Lesk, A. M., and Chothia C. (1987) J. Mol. Biol. 196, 641-656
44. Horovitz, A. (1996) Fold Des. 1, R121-R126
45. Warshel, A., and Åqvist, J. (1991) Annu. Rev. Biophys Biophys. Chem. 20, 267-298
46. Schechter, I., and Berger, A. (1967) Biochem. Biophys. Res. Commun. 27, 157-162
47. Johnson, D., and Travis J. (1978) J. Biol. Chem. 253, 7142-7144
48. Wise, R. J., Barr, P. J., Wong, P. A., Kiefer, M. C., Brake, A. J., and Kaufman, R. J. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 9378-9382