Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specific structural motifs control protein oxidation

Journal of Biological Chemistry

Volumn 279, Issue 8, 2004, Pages 6209-6212

  Fu, Xiaoyun ^a   Kao, Jeff L F ^b   Bergt, Constanze ^a   Kassim, Sean Y ^a   Huq, Nabiha P ^a   D'Avignon, André ^b   Parks, William C ^b,c   Mecham, Robert P ^c   Heinecke, Jay W ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b WASHINGTON UNIVERSITY   (United States)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CROSSLINKING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION; PROTEINS; TISSUE;

ENZYME ACTIVITY; OXIDANTS; PATHOLOGICAL DESTRUCTION;

BIOCHEMISTRY;

GLYCINE; HYPOCHLOROUS ACID; MATRILYSIN; MATRIX METALLOPROTEINASE; MYELOPEROXIDASE; TRYPTOPHAN;

ARTICLE; CATALYSIS; CHLORINATION; CROSS LINKING; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STRUCTURE; EXTRACELLULAR MATRIX; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PHAGOCYTOSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN STRUCTURE; TUMOR GROWTH;

AMINO ACID MOTIFS; CATALYTIC DOMAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROSS-LINKING REAGENTS; DEUTERIUM; GLYCINE; HYDROGEN; HYPOCHLOROUS ACID; INFLAMMATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; MATRIX METALLOPROTEINASE 7; MODELS, CHEMICAL; MODELS, MOLECULAR; OXYGEN; PEPTIDE LIBRARY; PEPTIDES; PHAGOCYTES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TEMPERATURE; TRYPTOPHAN; ULTRAVIOLET RAYS;

EID: 1342346608     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.C300506200     Document Type: Article

References (29)

1. Woessner, J. F., and Nagase, H. (2000) Matrix metalloproteinases and TIMPs, Oxford University Press, New York
2. Chang, C., and Werb, Z. (2001) Trends Cell Biol. 11, S37-S43
3. Libby, P. (2001) Circulation 104, 365-372
4. Shapiro, S. D. (2002) Biochem. Soc. Trans. 30, 98-102
5. Weiss, S. J., Peppin, G., Ortiz, X., Ragsdale, C., and Test, S. T. (1985) Science 227, 747-749
6. Peppin, G. J., and Weiss, S. J. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 4322-4326
7. Fu, X., Kassim, S. Y., Parks, W. C., and Heinecke, J. W. (2001) J. Biol. Chem. 276, 41279-41287
8. Michaelis, J., Vissers, M. C., and Winterbourn, C. C. (1992) Arch. Biochem. Biophys. 292, 555-562
9. Rajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., and Galis, Z. S. (1996) J. Clin. Invest. 98, 2572-2579
10. Harrison, J. E., and Schultz, J. (1976) J. Biol. Chem. 251, 1371-1374
11. Klebanoff, S. J., and Clark, R. A. (1978) The Neutrophil: Functional and Clinical Disorders, North-Holland Pub. Co., New York
12. Hurst, J. K., and Barrette, W. C., Jr. (1989) Crit. Rev. Biochem. Mol. Biol. 24, 271-328
13. Gu, Z., Kaul, M., Yan, B., Kridel, S. J., Cui, J., Strongin, A., Smith, J. W., Liddington, R. C., and Lipton, S. A. (2002) Science 297, 1186-1190
14. Fu, X., Kassim, S. Y., Parks, W. C., and Heinecke, J. W. (2003) J. Biol. Chem. 20, 28403-28409
15. Razmiafshari, M., Kao, J., d'Avignon, A., and Zawia, N. H. (2001) Toxicol. Appl. Pharmacol. 172, 1-10
16. Fu, X., Mueller, D. M., and Heinecke, J. W. (2002) Biochemistry 41, 1293-1301
17. Winterbourn, C. C., Vissers, M. C., and Kettle, A. J. (2000) Curr. Opin. Hematol. 7, 53-58
18. Katritzky, A. R., and Rees, C. W. (1984) Comprehensive Heterocyclic Chemistry: The Structure, Reactions, Synthesis, and Uses of Heterocyclic Compounds, Vol. 4, p. 214, Oxford University Press, New York
19. De Rosa, M., and Alonso, T. (1978) J. Org. Chem. 43, 2639-2643
20. Sanders, J. K. M., and Hunter, B. K. (1993) Modern NMR Spectroscopy: A Guide for Chemists, 2nd Ed., Oxford University Press, New York
21. Zhang, H., Andrekopoulos, C., Joseph, J., Chandran, K., Karoui, H., Crow, J. P., and Kalyanaraman, B. (2003) J. Biol. Chem. 278, 24078-24089
22. Hazen, S. L., and Heinecke, J. W. (1997) J. Clin. Invest. 99, 2075-2081
23. Henderson, J. P., Byun, J., Takeshita, J., and Heinecke, J. W. (2003) J. Biol. Chem. 278, 23522-23528
24. Vissers, M. C., and Winterbourn, C. C. (1991) Arch. Biochem. Biophys. 285, 53-59
25. Carr, A. C., Tijerina, T., and Frei, B. (2000) Biochem. J. 346, 491-499
26. Kettle, A. J., and Candaeis, L. P. (2000) Redox. Rep. 5, 179-184
27. Kang, D. K., Jeong, J., Drake, S. K., Wehr, N. B., Rouault, T. A., and Levine, R. L. (2003) J. Biol. Chem. 278, 14857-14864
28. Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K., and Barford, D. (2003) Nature 423, 769-773
29. van Montfort, R. L., Congreve, M., Tisi, D., Carr, R., and Jhoti, H. (2003) Nature 423, 773-777