Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases

References

Abrink, M., Grujic, M., and Pejler, G. (2004). Serglycin is essential for maturation of mast cell secretory granule. J. Biol. Chem.279, 40897–40905.10.1074/jbc.M405856200Search in Google Scholar

Caughey, G. (2002). New developments in the genetics and activation of mast cell proteases. Mol. Immunol.38, 1353–1357.10.1016/S0161-5890(02)00087-1Search in Google Scholar

Chancey, A.L., Brower, G.L., and Janicki, J.S. (2002). Cardiac mast cell-mediated activation of gelatinase and alteration of ventricular diastolic function. Am. J. Physiol. Heart Circ. Physiol.282, H2152–H2158.10.1152/ajpheart.00777.2001Search in Google Scholar

Crabbe, T., O'Connell, J.P., Smith, B.J., and Docherty, A.J. (1994). Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase A. Biochemistry33, 14419–14425.10.1021/bi00252a007Search in Google Scholar

Fang, K.C., Raymond, W.W., Blount, J.L., and Caughey, G.H. (1997). Dog mast cell α-chymase activates progelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain. J. Biol. Chem.272, 25628–25635.10.1074/jbc.272.41.25628Search in Google Scholar

Gruber, B.L., Marchese, M.J., Suzuki, K., Schwartz, L.B., Okada, Y., Nagase, H., and Ramamurthy, N.S. (1989). Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest.84, 1657–1662.10.1172/JCI114344Search in Google Scholar

Hallgren, J., Estrada, S., Karlson, U., Alving, K., and Pejler, G. (2001). Heparin antagonists are potent inhibitors of mast cell tryptase. Biochemistry40, 7342–7349.10.1021/bi001988cSearch in Google Scholar

Hernandez-Barrantes, S., Toth, M., Bernardo, M.M., Yurkova, M., Gervasi, D.C., Raz, Y., Sang, Q.A., and Fridman, R. (2000). Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J. Biol. Chem.275, 12080–12089.10.1074/jbc.275.16.12080Search in Google Scholar

Huhtala, P., Eddy, R.L., Fan, Y.S., Byers, M.G., Shows, T.B., and Tryggvason, K. (1990). Completion of the primary structure of the human type IV collagenase preproenzyme and assignment of the gene (CLG4) to the q21 region of chromosome 16. Genomics6, 554–559.10.1016/0888-7543(90)90486-ESearch in Google Scholar

Itoh, Y., Binner, S., and Nagase, H. (1995). Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate. Biochem. J.308, 645–651.10.1042/bj3080645Search in Google Scholar PubMed PubMed Central

Jippo, T., Lee, Y.-M., Katsu, Y., Tsujino, K., Morii, E., Kim, D.-K., Kim, H.-M., and Kitamura, Y. (1999). Deficient transcription of mouse mast cell protease 4 gene in mutant mice of mi/mi genotype. Blood93, 1942–1950.10.1182/blood.V93.6.1942.406k08_1942_1950Search in Google Scholar

Karlson, U., Pejler, G., Tomasini-Johansson, B., and Hellman, L. (2003). Extended substrate specificity of rat mast cell protease 5, a rodent α-chymase with elastase-like primary specificity. J. Biol. Chem.278, 39625–39631.10.1074/jbc.M301512200Search in Google Scholar

Kolset, S.O., Prydz, K., and Pejler, G. (2004). Intracellular proteoglycans. Biochem. J.379, 217–227.10.1042/bj20031230Search in Google Scholar

Kunori, Y., Koizumi, M., Masegi, T., Kasai, H., Kawabata, H., Yamazaki, Y., and Fukamizu, A. (2002). Rodent α-chymases are elastase-like proteases. Eur. J. Biochem.269, 5921–5930.10.1046/j.1432-1033.2002.03316.xSearch in Google Scholar

Lutzelschwab, C., Pejler, G., Aveskogh, M., and Hellman, L. (1997). Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations. J. Exp. Med.185, 13–29.Search in Google Scholar

Martignetti, J.A., Aqeel, A.A., Sewairi, W.A., Boumah, C.E., Kambouris, M., Mayouf, S.A., Sheth, K.V., Eid, W.A., Dowling, O., Harris, J., et al. (2001). Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nat. Genet.28, 261–265.10.1038/90100Search in Google Scholar

Mazzieri, R., Masiero, L., Zanetta, L., Monea, S., Onisto, M., Garbisa, S., and Mignatti, P. (1997). Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants. EMBO J.16, 2319–2332.10.1093/emboj/16.9.2319Search in Google Scholar

Meier, H.L., Heck, L.W., Schulman, E.S., and MacGlashan, D.W. Jr. (1985). Purified human mast cells and basophils release human elastase and cathepsin G by an IgE-mediated mechanism. Int. Arch. Allergy Appl. Immunol.77, 179–183.10.1159/000233779Search in Google Scholar

Metcalfe, D.D., Baram, D., and Mekori, Y.A. (1997). Mast cells. Physiol. Rev.77, 1033–1079.10.1152/physrev.1997.77.4.1033Search in Google Scholar

Miller, H.R. and Pemberton, A.D. (2002). Tissue-specific expression of mast cell granule serine proteinases and their role in inflammation in the lung and gut. Immunology105, 375–390.10.1046/j.1365-2567.2002.01375.xSearch in Google Scholar

Nagase, H. (1997). Activation mechanisms of matrix metalloproteinases. Biol. Chem.378, 151–160.Search in Google Scholar

Overall, C., Wrana, J., and Sodek, J. (1991). Transcriptional and post-transcriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-β1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression. J. Biol. Chem.266, 14064–14071.Search in Google Scholar

Reponen, P., Sahlberg, C., Huhtala, P., Hurskainen, T., Thesleff, I., and Tryggvason, K. (1992). Molecular cloning of murine 72-kDa type IV collagenase and its expression during mouse development. J. Biol. Chem.267, 7856–7862.10.1016/S0021-9258(18)42592-6Search in Google Scholar

Schechter, N.M., Irani, A.M., Sprows, J.L., Abernethy, J., Wintroub, B., and Schwartz, L.B. (1990). Identification of a cathepsin G-like proteinase in the MCTC type of human mast cell. J. Immunol.145, 2652–2661.10.4049/jimmunol.145.8.2652Search in Google Scholar

Sternlicht, M.D. and Werb, Z. (2001). How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol.17, 463–516.10.1146/annurev.cellbio.17.1.463Search in Google Scholar PubMed PubMed Central

Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A., and Goldberg, G.I. (1995). Mechanism of cell surface activation of 72-kDa type IV collagenase. J. Biol. Chem.270, 5331–5338.10.1074/jbc.270.10.5331Search in Google Scholar PubMed

Tchougounova, E., Forsberg, E., Angelborg, G., Kjellen, L., and Pejler, G. (2001). Altered processing of fibronectin in mice lacking heparin. a role for heparin-dependent mast cell chymase in fibronectin degradation. J. Biol. Chem.276, 3772–3777.10.1074/jbc.M008434200Search in Google Scholar PubMed

Tchougounova, E., Pejler, G., and Abrink, M. (2003). The chymase, mouse mast cell protease 4, constitutes the major chymotrypsin-like activity in peritoneum and ear tissue. A role for mouse mast cell protease 4 in thrombin regulation and fibronectin turnover. J. Exp. Med.198, 423–431.Search in Google Scholar

Tchougounova, E., Lundequist, A., Fajardo, I., Winberg, J.O., Abrink, M., and Pejler, G. (2005). A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J. Biol. Chem.280, 9291–9296.10.1074/jbc.M410396200Search in Google Scholar PubMed

Wang, Z., Juttermann, R., and Soloway, P.D. (2000). TIMP-2 is required for efficient activation of proMMP-2 in vivo. J. Biol. Chem.275, 26411–26415.10.1074/jbc.M001270200Search in Google Scholar PubMed PubMed Central

Yurt, R.W., Leid, R.W. Jr., Spragg, J., and Austen, K.F. (1977). Immunologic release of heparin from purified rat peritoneal mast cells. J. Immunol.118, 1201–1207.10.4049/jimmunol.118.4.1201Search in Google Scholar