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Expression of Human Collagenase I (MMP-1) andTIMP-1 in a Baculovirus-Based Expression System

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Matrix Metalloproteinase Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 151))

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Abstract

Resident cells of tissues are capable of secreting an array of structurally related zinc endopeptidases known as matrix metalloproteinases (MMPs). They initiate the degradation of the surrounding macromolecules of the extracellular matrix (ECM), mostly proteoglycans and specific types of collagen. ECM degradation presumably contributes to the initial phase of tissue remodeling inherent to the physiological processes of morphogenesis, angiogenesis, involution of the uterus, bone resorption, inflammation, and wound healing. The aberrant activity of MMPs has been found to be involved in a variety of pathological processes, e.g., rheumatoid joint destruction, corneal ulceration, metastasis of tumor cells, and various genetic diseases (1,2).

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References

  1. Matrisian L. M. (1992) The matrix degrading metalloproteinases. Bioessays 14, 455–463.

    Article  PubMed  CAS  Google Scholar 

  2. Birkedal-Hansen H., Moore W. G. I., Bodden M. K., Windsor L. J., Birkedal-Hansen B., DeCarlo A., and Engler J. A. (1993) Matrix metalloproteinase. A review. Crit. Rev. Oral. Biol. Med. 4, 197–250.

    PubMed  CAS  Google Scholar 

  3. Dioszegi M., Cannon P., and van Wart H. (1995) Verterbrate collagenases. Methods Enzymol. 248, 413–431.

    Article  PubMed  CAS  Google Scholar 

  4. Sang Q. A. and Douglas D. A. (1996) Computational sequence analysis of matrix metalloproteinases. J. Protein Chem. 15, 137–160.

    Article  PubMed  CAS  Google Scholar 

  5. Murphy G. and Willenbrock F. (1995) Tissue inhibitors of metalloendopep-tidases. Methods Enzymol. 248, 496–510.

    Article  PubMed  CAS  Google Scholar 

  6. Greene J., Wang M., Raymond L. A., Liu Y. E., Rosen C., and Shi Y. E. (1996) TIMP-4, a novel human tissue inhibitor of metalloproteinase, was identified and cloned. J. Biol. Chem. 271, 30,375–30,380.

    Article  PubMed  CAS  Google Scholar 

  7. Angel P. and Karin M. (1991) The role of jun, fos and the AP-1 complex in cell proliferation and transformation. Biochem. Biophys. Acta. 1072, 129–157.

    PubMed  CAS  Google Scholar 

  8. Vincenti M. P., White L. A., Schrön D. J., Benbow U., and Brinckerhoff C. E. (1996) Regulating expression of the gene for matrix metalloproteinase-1 (colla-genase): mechanisms that control enzyme activity, transcription, and mRNA stability. Crit. Rev. Eukaryot. Gene Expr. 6(4), 391–411.

    PubMed  CAS  Google Scholar 

  9. Borden P. and Heller R. A. (1997) Transcriptional control of matrix metalloproteinases and the tissue inhibitors of matrix metalloproteinases. Crit. Rev. Eukaryot. Gene Expr. 7(1–2), 159–178.

    PubMed  CAS  Google Scholar 

  10. Docherty A.J., O’Connell J., Crabbe T., Angal S., and Murphy G. (1992) The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases. Trends Biotechnol. 10(6), 200–207.

    Article  PubMed  CAS  Google Scholar 

  11. O’Hare M. C., Clarke N. J., and Cawston T. E. (1992) Production in Escherichia coli of porcaine type I collagenase as a fusion protein with β-galactosidase. Gene 111, 245–248.

    Article  PubMed  Google Scholar 

  12. Housley T. J., Baumann A. B., Braun I. D., Davis G., Seperack P. K., and Wilhelm S. M. (1993) Recombinant Chinese hamster ovary cell matrix metallo-protease-3 (MMP-3, stromelysin-1). Role of calcium in promatrix metal-loprotease-3 (pro-MMP-3, prostromelysin-1) activation and thermostability of the low mass catalytic domain of MMP-3. J. Biol. Chem. 268(6), 4481–4487.

    PubMed  CAS  Google Scholar 

  13. Windsor L. J., Bodden M. K., Birkedal-Hansen B., and Engler J. A., and Bir-kedal-Hansen H. (1994) Mutational analysis of residues in and around the active site of human fibroblast-type collagenase. J. Biol. Chem. 269, 26,201–26,207.

    PubMed  CAS  Google Scholar 

  14. Freimark B. D., Feeser W. S., and Rosenfeld S. A. (1994) Multiple sites of the propeptide region of human stromelysin-1 are required for maintaining a latent form of the enzyme. J. Biol. Chem. 269(43), 26,982–26,987.

    PubMed  CAS  Google Scholar 

  15. Rosenfeld S. A., Ross O. H., Hillman M. C., Corman J. I., and Dowling R. L. (1996) Production and purification of human fibroblast collagenase (MMP-1) expressed in the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 7(4), 423–430.

    Article  PubMed  CAS  Google Scholar 

  16. Zhang Y. and Gray R. D. (1996) Characterization of folded, intermediate, and unfolded states of recombinant human interstitial collagenase. J. Biol. Chem. 271(14), 8015–80211.

    Article  PubMed  CAS  Google Scholar 

  17. Knäuper V., Cowell S., Smith B., López-Otin C., O’Shea M., Morris H., Zardi L., and Murphy G. (1997) The role of C-terminal domain of human colla-genase-3 (MMP-13) in the activation of procollagenase-3 substrate specificity and tissue inhibitor of metalloproteinse interaction. J. Biol. Chem. 272(12), 7608–7616.

    Article  PubMed  Google Scholar 

  18. Lemaitre V., Jungbluth A., and Eeckhout Y. (1997) The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleavingits aminotelopeptides. Biochem. Biophys. Res. Commun. 230(1), 202–205.

    Article  PubMed  CAS  Google Scholar 

  19. Gomez D. E., Lindsay C. K., Cottam D. W., Nason A. M., and Thorgeirsson U. P. (1994) Expression and characterization of human tissue inhibitor of metalloproteinases-1 in a baculovirus-insect cell system. Biochem. Biophys. Res. Commun. 203(1), 237–243.

    Article  PubMed  CAS  Google Scholar 

  20. Cocuzzi E. T., Walther S. E., and Denhardt D. T. (1994) Expression and secretion of active mouse TIMP-1 using a baculovirus expression vector. Inflammation 18(1), 35–43.

    Article  PubMed  CAS  Google Scholar 

  21. Bergmann U., Tuuttila A., Stetler-Stevenson W. G., and Tryggvason K. (1995) Autolytic activation of recombinant human 72 kilodalton type IV collagenase. Biochemistry 34(9), 2819–2825.

    Article  PubMed  CAS  Google Scholar 

  22. Kurschat P., Graeve L., Erren A., Gatsios P., Rose-John S., Roeb E., Tschesche H., Koj A., and Heinrich P. C. (1995) Expression of a biologically active murine tissue inhibitor of metalloproteinases-1 (TIMP-1) in baculovirus-infected insect cells. Purification and tissue distribution in the rat. Eur. J. Biochem. 234(2) 485–491.

    Article  PubMed  CAS  Google Scholar 

  23. Vallon R., Müller R., Moosmayer D., Gerlach E., and Angel P. (1997) The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1). Eur. J. Biochem. 244(1), 81–88.

    Article  PubMed  CAS  Google Scholar 

  24. Liu Y. E., Wang M., Greene J., Su J., Ullrich S., Li H., Sheng S., Alexander P., Sang Q. A., and Shi Y. E. (1997) Preparation and characterization of recombinant tissue inhibitor of metalloproteinase 4 (TIMP-4). J. Biol. Chem. 272(33) 20,479–20,483.

    Article  PubMed  CAS  Google Scholar 

  25. Whitham S. E., Murphy G., Angel P., Rahmsdorf H. J., Smith B. J., Lyons A., Harris T. J. Reynolds J. J., Herrlich P., and Docherty A. (1986) Comparison of human stromelysin and collagenase by cloning and sequence analysis. Biochem. J. 240, 913–916.

    PubMed  CAS  Google Scholar 

  26. Annweiler A., Hipskind R. A., and Wirth T. (1991) A strategy for efficient in vitro translation using the rabbit β-globin leader sequence. Nucleic Acids Res. 19, 3750.

    Article  PubMed  CAS  Google Scholar 

  27. Angel P. Hattori K., Smeal T., and Karin M. (1988a) The Jun proto-oncogene is positively autoregulated by its product, Jun/AP1. Cell 55, 875–885.

    Article  PubMed  CAS  Google Scholar 

  28. Docherty A. J. P., Lyons A., Smith B. J., Wright E. M., Stephens P. E., Harris T. J. R., Murphy G., and Reynolds J. J. (1985) Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature 318, 66–69.

    Article  PubMed  CAS  Google Scholar 

  29. Angel P., Allegretto E. A., Okino S., Hattori K., Boyle W. J., Hunter T., and Karin M. (1988) Oncogene Jun encodes a sequence specific trans-activator similar to AP1. Nature 332, 166–171.

    Article  PubMed  CAS  Google Scholar 

  30. Reed L. J. and Muench H. (1938). A simple method of estimating fifty percent endpoints. Amer. J. Hygiene 27, 493–497.

    Google Scholar 

  31. Springman E. B., Angleton E. L., Birkedal-Hansen H., and van Wart H. E. (1990) Multiple modes of activation of latent human fibroblast collagenase. Evidence for the role of a Cys-73 active-size zinc complex in latency and a “cysteine switch” mechanism for activation. Proc. Natl. Acad. Sci. USA 87, 364–368.

    Article  PubMed  CAS  Google Scholar 

  32. Cawston T. E. and Murphy G. (1981) Mammalian collagenase. Methods Enzymol. 80, 711–722.

    Article  PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Forschungszentrum Karlsruhe, Institut für Genetik, Karlsruhe, Germany

    Rüdiger Vallon

  2. German Cancer Research Center, Division of Signal Transduction and Growth Control, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany

    Peter Angel

Authors
  1. Rüdiger Vallon
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  2. Peter Angel
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Editor information

Editors and Affiliations

  1. University of East Anglia, Norwich, UK

    Ian M. Clark PhD

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© 2001 Humana Press Inc.

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Vallon, R., Angel, P. (2001). Expression of Human Collagenase I (MMP-1) andTIMP-1 in a Baculovirus-Based Expression System. In: Clark, I.M. (eds) Matrix Metalloproteinase Protocols. Methods in Molecular Biology™, vol 151. Humana Press. https://doi.org/10.1385/1-59259-046-2:207

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  • DOI: https://doi.org/10.1385/1-59259-046-2:207

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-733-5

  • Online ISBN: 978-1-59259-046-9

  • eBook Packages: Springer Protocols

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