Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: An oxidative mechanism for regulation of serine proteinases by myeloperoxidase

Journal of Biological Chemistry

Volumn 280, Issue 32, 2005, Pages 29311-29321

  Shao, Baohai ^a   Belaaouaj, Abderrazzaq ^b   Verlinde, Christophe L M J ^a   Fu, Xiaoyun ^a   Heinecke, Jay W ^a,c  

^a UNIVERSITY OF WASHINGTON   (United States)

^b WASHINGTON UNIVERSITY   (United States)

^c Division of Metabolism Endocrinology and Nutrition   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; HYDROGEN PEROXIDE; OXIDATION; PROTEINS; TISSUE;

HYPOCHLOROUS ACID (HOCL); METHIONINE SULFOXIDE; PROTEOLYTIC CLEAVAGE; TISSUE PROTEINS;

AMINO ACIDS;

ASPARTIC ACID; BENZYLSULFONYL FLUORIDE; CATHEPSIN G; HYPOCHLOROUS ACID; METHIONINE SULFOXIDE; MYELOPEROXIDASE; SERINE PROTEINASE; SULFIDE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CYTOKINE RELEASE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MECHANISM; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; INFLAMMATION; NEUTROPHIL; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; TANDEM MASS SPECTROMETRY; TISSUE INJURY;

ANIMALS; CATALYTIC DOMAIN; CATHEPSINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; INFLAMMATION; MASS SPECTROMETRY; METHIONINE; MICE; MODELS, CHEMICAL; MODELS, MOLECULAR; NEUTROPHILS; OXIDANTS; OXYGEN; PEPTIDES; PEROXIDASE; PROTEIN BINDING; SERINE ENDOPEPTIDASES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TIME FACTORS;

EID: 23844495082     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M504040200     Document Type: Article

References (52)

1. Klebanoff, S. J. (1980) Ann. Intern. Med. 93, 480-489
2. Travis, J. (1988) Am. J. Med 84, 37-42
3. Belaaouaj, A., McCarthy, R., Baumann, M., Gao, Z., Ley, T. J., Abraham, S. N., and Shapiro, S. D. (1998) Nat. Med. 4, 615-618
4. Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., and Segal, A. W. (2002) Nature 416, 291-297
5. Weiss, S. J. (1989) N. Engl. J. Med. 320, 365-376
6. Travis, J., and Salvensen, G. S. (1983) Annu. Rev. Biochem. 52, 655-709
7. Campbell, E. J., Campbell, M. A., Boukedes, S. S., and Owen, C. A. (1999) J. Clin. Invest. 104, 337-344
8. Turkington, P. T. (1992) Thromb. Res. 67, 147-155
9. Molino, M., Blanchard, N., Belmonte, E., Tarver, A. P., Abrams, C., Hoxie, J. A., Cerletti C., and Brass, L. F. (1995) J. Biol. Chem. 270, 11168-11175
10. Adkison, A. M., Raptis, S. Z., Kelley, D. G., and Pham, C. T. (2002) J. Clin. Invest. 109, 363-371
11. Hof, P., Mayr, I., Huber, R., Korzus, E., Potempa, J., Travis, J., Powers, J. C., and Bode, W. (1996) EMBO J. 15, 5481-5491
12. Czapinska, H., and Otlewski, J. (1999) Eur. J. Biochem. 260, 571-595
13. Schechter, I., and Berger, A. (1968) Biochem. Biophys. Res. Commun. 32, 898-902
14. Maison, C. M., Villiers, C. L., and Colomb, M. G. (1991) J. Immunol. 147, 921-926
15. Tanaka, T., Minematsu, Y., Reilly, C. F., Travis, J., and Powers, J. C. (1985) Biochemistry 24, 2040-2047
16. Bank, U., Kupper, B., Reinhold, D., Hoffmann, T., and Ansorge, S. (1999) FEBS Lett. 461, 235-240
17. Babior, B. M., Kipnes R. S., and Curnutte, J. T. (1973) J. Clin. Invest. 52, 741-744
18. Klebanoff, S. J. (1975) Semin. Hematol. 12, 117-142
19. Harrison, J. E., and J. Schultz, J. (1976) J. Biol. Chem. 251, 1371-1374
20. Hampton, M. B., Kettle, A. J., and Winterbourn, C. C. (1998) Blood 92, 3007-3017
21. Gaut, J. P., Yeh, G. C., Tran, H. D., Byun, J., Henderson, J. P., Richter, G. M., Brennan, M. L., Lusis, A. J., Belaaouaj, A., Hotchkiss, R. S., and Heinecke, J. W. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 11961-11966
22. Aratani, Y., Koyama, H., Nyui, S., Suzuki, K., Kura, F., and Maeda, N. (1999) Infect. Immun. 67, 1828-1836
23. Heinecke, J. W. (1999) J. Lab. Clin. Med. 133, 321-325
24. Hazen, S. L., and Heinecke, J. W. (1997) J. Clin. Invest. 99, 2075-2081
25. Heller, J. I., Crowley, J. R., Hazen, S. L., Salvay, D. M., Wagner, P., Pennathur, S., and Heinecke, J. W. (2000) J. Biol. Chem. 275, 9957-9962
26. Henderson, J. P., Byun, J., Takeshita, J., and Heinecke, J. W. (2003) J. Biol. Chem. 278, 23522-23528
27. Leeuwenburgh, C., Rasmussen, J. E., Hsu, F. F., Mueller, D. M., Pennathur, S., and Heinecke, J. W. (1997) J. Biol. Chem. 272, 3520-3526
28. Owen, C. A., Campbell, M. A., Sannes, P. L., Boukedes, S. S., and Campbell, E. J. (1995) J. Cell Biol. 131, 775-789
29. Voetman, A. A., Weening, R. S., Hamers, M. N., Meerhof, L. J., Bot, A. A., and Roos, D. (1981) J. Clin. Invest. 67, 1541-1549
30. Kobayashi, M., Tanaka, T., and Usui, T. (1982) J. Lab. Clin. Med. 100, 896-907
31. Clark, R. A., and Borregaard, N. (1985) Blood 65, 375-381
32. Morris, J. C. (1966) J. Phys. Chem. 70, 3798-3805
33. Nelson, D. P., and Kiesow, L. A. (1972) Anal. Biochem. 49, 474-478
34. Heinecke, J. W., Li, W., Francis, G. A., and Goldstein, J. A. (1993) J. Clin. Invest. 91, 2866-2872
35. Heinecke, J. W., Baker, L., Rosen, H., and Chait, A. (1986) J. Clin. Invest. 77, 757-761
36. DelMar, E. G., Largman, C., Brodrick, J. W., and Geokas, M. C. (1979) Anal. Biochem. 99, 316-320
37. MacIvor, D. M., Shapiro, S. D., Pham, C. T., Belaaouaj, A., Abraham, S. N., and Ley, T. J. (1999) Blood 94, 4282-4293
38. Brennan, M. L., Anderson, M. M., Shih, D. M., Qu, X. D., Wang, X. P., Mehta, A. C., Lim, L. L., Shi, W. B., Hazen, S. L., Jacob, J. S., Crowley, J. R., Heinecke, J. W., and Lusis, A. J. (2001) J. Clin. Invest. 107, 419-430
39. Fu, X., Kassim, S. Y., Parks, W. C., and Heinecke, J. W. (2001) J. Biol. Chem. 276, 41279-41287
40. Fu, X., Kao, J. L., Bergt, C., Kassim, S. Y., Huq, N. P., d'Avignon, A., Parks, W. C., Mecham, R. P., and Heinecke, J. W. (2004) J. Biol. Chem. 279, 6209-6212
41. Fu, X., Kassim, S. Y., Parks, W. C., and Heinecke, J. W. (2003) J. Biol. Chem. 278, 28403-28409
42. Pattison, D. I., and Davies M. J. (2001) Chem. Res. Toxicol. 14, 1453-1464
43. Winterbourn, C. C., and Metodiewa, D. (1999) Free Radic. Biol. Med. 27, 322-328
44. Winterbourn, C. C. (1985) Biochim. Biophys. Acta 840, 204-210
45. Hawkins, C. L., and Davies, M. J. (1998) Biochem. J. 332, 617-625
46. Hazell, L. J., van den Berg, J. J., and Stocker, R. (1994) Biochem. J. 302, 297-304
47. Hazen S. L., Hsu, F. F., Crowley, J. R., Mueller, D. M., and Heinecke, J. W. (1996) J. Clin. Invest. 98, 1283-1289
48. Gaut, J. P., Byun, J., Tran, H. D., Lauber, W. M., Carroll, J. A., Hotchkiss, R. S., Belaaouaj, A., and Heinecke, J. W. (2002) J. Clin. Invest. 109, 1311-1319
49. Bott, R., Ultsch, M., Kossiakoff, A., Graycar, T., Katz, B., and Power, S. (1988) J. Biol. Chem. 263, 7895-7906
50. DePaz, R. A., Barnett, C. C., Dale, D. A., Carpenter, J. F., Gaertner, A. L., and Randolph, T. W. (2000) Arch. Biochem. Biophys. 384, 123-132
51. Hirche, T. O., Gaut, J. P., Heinecke, J. W., and Belaaouaj, A. (2005) J. Immunol. 174, 1557-1565
52. Vivekananthan, D. P., Penn, M. S., Sapp, S. K., Hsu, A., and Topol, E. J. (2003) Lancet 361, 2017-2023