Progelatinase B forms from human neutrophils. Complex formation of monomer/lipocalin with TIMP-1

Biological Chemistry

Volumn 377, Issue 7-8, 1996, Pages 529-533

  Kolkenbrock, Hansjörg ^a   Hecker Kia, Adelheid ^a   Orgel, Dagmar ^a   Kinawi, Abdelwahab ^b   Ulbrich, Norbert ^a  

^a DEUTSCHES RHEUMA FORSCHUNGSZENTRUM   (Germany)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Lipocalin complex; Progelatinase B; TIMP 1

Indexed keywords

ENZYME PRECURSOR; GELATINASE; LIPOCALIN; TISSUE INHIBITOR OF METALLOPROTEINASE; TRYPSIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; CARBOHYDRATE ANALYSIS; CHROMATOGRAPHY; COMPLEX FORMATION; CONTROLLED STUDY; EXTRACELLULAR SPACE; HUMAN; HUMAN CELL; NEUTROPHIL; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION;

EID: 0029808125     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm3.1996.377.7-8.529     Document Type: Article

References (26)

1. Birkedal-Hansen, H., Werb, Z., Welgus, H., and Van Wart, H., eds. (1992). Matrix Metalloproteinases and Inhibitors. (Stuttgart, Jena, New York: Gustav Fischer Verlag).
2. Engelbrecht, S., Pieper, E., Macartney, H., Rautenberg, W., Wenzel, H., and Tscheche, H. (1982). Separation of the human leukocyte enzymes alanine aminopeptidase, cathepsin G, collagenase, elastase, and myeloperoxidase. Hoppe Seyler's Z. Physiol. Chem. 363, 305-315.
3. Fridman, R., Bird, R., Hoyhtya, M., Oelkuct, M., Komarek, D., Liang, C. M., Berman, M. L., Liotta, L. A., Stetler-Stevenson, W. G., and Fuerst, T. R. (1993). Expression of human recombinant 72 kDa gelatinase and tissue inhibitor of metalloproteinase-2 (TIMP-2): Characterization of complex and free enzyme. Biochem. J. 289, 411-416
4. Goldberg, G. J., Marmer, B. L., Grant, J. A., Eisen, A. Z., Wilhelm, S. M., and He, C. (1989). Human 72 kDa type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designed TIMP-2. Proc. Natl. Acad. Sci. USA 86, 8207-8211.
5. Goldberg, G. J., Strongin, A., Collier, I. E., Genrich, L T., and Marmer, B. L. (1992). Interaction of 92 kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitional collagenase and activation of the the proenzyme with stromelysin. J. Biol. Chem. 267, 4583-4591.
6. Green, N. M., and Work, E. (1953). Pancreatic trypsin inhibitor. 2. reaction with trypsin. Biochem. J. 54, 347-352.
7. He, C., Wilhelm, S. M., Pentland, A. P., Marmer, B. L., Grant, J. A., Eisen, A. Z., and Goldberg, G. J. (1989). Tissue cooperation in a proteolytic cascade activating human interstitional collagenase. Proc. Natl. Acad. Sci. USA 86, 2632-2636.
8. Hibbs, M. S., Hasty, K. A., Seyer, J. M., Kang, A. H., and Mainardi, C. L. (1985). Biochemical and immunological characterization of human neutrophil gelatinase. J. Biol. Chem. 260, 2493-2500.
9. Ito, A., and Nagase, H. (1988). Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase. Arch. Biochem. Biophys. 267, 211-216.
10. Kjeldsen, L., Johnsen, A. H., Sengelov, H., and Borregard, N. (1993). Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J. Biol. Chem. 268, 10425-10432.
11. Kjeldsen, L., Bainton, D. F., Sengelov., H., and Borregard, N. (1994). Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils. Blood 83, 799-807.
12. Knäuper, V., Wilhelm, S. M., Seperack, P. K., DeClerk, Y. A., Langley, K. E., Osthues, A., and Tschesche, H. (1993). Direct activation of human neutrophil procollagenase by recombinant stromelysin. Biochem. J. 295, 581-586.
13. Kolkenbrock, H., Orgel, D., Hecker-Kia, A., Noack, W., and Ulbrich, N. (1991). The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72 kDa progelatinase is a metalloproteinase inhibitor. Eur. J. Biochem. 198, 775-781.
14. Kolkenbrock, H., Hecker-Kia, A., Orgel, D., Buchlow, G., Sörensen, H., Hauer, W., and Ulbrich, N. (1993). A trypsin sensitive stromelysin isolated from rheumatoid synovial fluid is an activator for matrix metalloproteinases. Eur. J. Clin. Chem. Clin. Biochem.31, 625-631.
15. Kolkenbrock, H., Hecker-Kia, A., Orgel, D., Huser, H., Schröder, W., and Ulbrich, N. (1994a). Isolation of latent 31-kDa C-truncated stromelysin and 21-kDa stromelysin from rabbit synovial fibroblasts: an alternative activation pathway for stromelysin. Biol. Chem. Hoppe-Seyler 375, 241-247.
16. Kolkenbrock, H., Hecker-Kia, A., Orgel, D., Ruppitsch, W., and Ulbrich, N. (1994b). Activity of ternary gelatinase A-TIMP-2-matrix metalloproteinase complexes. Biol. Chem. Hoppe-Seyler 375, 589-595.
17. Kolkenbrock, H., Orgel, D., Hecker-Kia, A., Zimmermann, J., and Ulbrich, N. (1995). Generation and activity of the ternary gelatinase B/TIMP-1/LMW-stromelysin-1 complex. Biol. Chem. Hoppe-Seyler 376, 495-500.
18. Masui, Y., Takemoto, T., Sakakibara, S., and Hori, H. (1977). Synthetic substrates for vertebrate collagenase. Biochem. Med. 17, 215-221.
19. Matrisian, L. M. (1992). The matrix-degrading metalloproteinases. BioEssays 14, 455-463.
20. Murphy, G., Cockett, M. I., Stephens, P. E., Smith, B. J., and Docherty, A. J. P. (1987). Stromelysin is an activator for progelatinase. Biochem. J. 248, 265-268.
21. Ogata, Y., Enghild, J. J., and Nagase, H. (1992). Matrix metalloproteinase 3 (stromelysin) activates the precursor of the human matrix metalloproteinase 9. J. Biol. Chem. 267, 3581 -3584.
22. Stetler-Stevenson, W.G., Krutzsch, H. C., and Liotta, L. A. (1989). Tissue inhibitor of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264, 17374-17378.
23. Triebel, S., Bläser, J., Reinke, H., and Tschesche, H. (1992). A 25 kDa α2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase. FEBS Lett. 314, 386-388.
24. Triebel, S., Bläser, J., Gote. T., Pelz, G., Schüren, E., Schmitt, M., and Tschesche, H. (1995). Evidence for the tissue inhibitor of metalloproteinases-1 (TIMP-1) in human polymorphonuclear leukocytes. Eur. J. Biochem. 231, 714-719.
25. Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, J. A., and Goldberg, G. J. (1989). SV 40 transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264, 17213-17221.
26. Willenbrock, F., Crabbe, T., Slocombe, P., Sutton, C. W., Docherty, A. J. P., Cockett, M. I., O'Shea, M., Brocklehurst, K., Philips, I. R., and Murphy, G. (1993). The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions. A kinetic analysis of the inhibition of gelatinase A. Biochemistry 32, 4330-4337.