The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (460 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.871, 5-year impact factor: 4.303
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-59149094419&partnerID=40&md5=bb0287fbd44ec55112d6b69147937514
Keywords: Collagen Binding Domain, Gelatinase B, Kinetics, Matrix Metalloproteinases, Type Iv Collagen Fragmentation, Collagen Type 4, Fibronectin, Matrix Metalloproteinase Inhibitor, Analytic Method, Article, Binding Site, Catalysis, Cell Migration, Collagen Degradation, Conformational Transition, Controlled Study, Edman Sequencing, Enzyme Activity, Human, Human Cell, Mass Spectrometry, Neutrophil, Placenta, Priority Journal, Protein Binding, Protein Degradation, Protein Domain, Surface Plasmon Resonance, Environmental Monitoring, Peptides, Protein Interaction Mapping, Sequence Analysis, Temperature,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine and Biochemical Sciences, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Rome, Italy
Department of Oral Biological and Medical Sciences, Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC V6T1Z3, Canada
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC V6T1Z3, Canada
Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, P.za Umberto I 1, I-70100 Bari, Italy
Rega Institute for Medical Research, Laboratory of Immunobiology, University of Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium
Department of Chemistry, University of Catania, V.le A. Doria, Catania, Italy
Institute of Biostructure and Bioimaging, CNR, V.le A. Doria, Catania, Italy
References:
Overall, C.M., Blobel, C.P., In search of partners: linking extracellular proteases to substrates (2007) Nat. Rev. Mol. Cell Biol., 8, pp. 245-25
Sternlicht, M.D., Werb, Z., How matrix metalloproteinases regulate cell behavior (2001) Annu. Rev. Cell Dev. Biol., 17, pp. 463-516
Allan, J.A., Docherty, A.J., Barker, P.J., Huskisson, N.S., Reynolds, J.J., Murphy, G., Binding of gelatinases A and B to type-I collagen and other matrix components (1995) Biochem. J., 309, pp. 299-306
Van den Steen, P.E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., The hemopexin and O-glycosylated domains tune gelatinase B/MMP9 bioavailability via inhibition and binding to cargo receptors (2006) J. Biol. Chem., 281, pp. 18626-18637
Bachmeier, B.E., Iancu, C.M., Jocum, M., Nerlich, A.G., Matrix metalloproteinases in cancer: comparison of known and novel aspects of their inhibition as a therapeutic approach (2005) Exp. Rev. Anticancer Ther., 5, pp. 149-163
Mook, O.R., Frederiks, W.M., Van Noorden, J., The role of gelatinases in colorectal cancer progression and metastasis (2004) Biochim. Biophys. Acta, 1705, pp. 69-89
Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A., Goldberg, G.I., Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease (1995) J. Biol. Chem., 270, pp. 5331-5338
Seiki, M., Membrane-type matrix metalloproteinases (1999) Acta Pathol., Microbiol. Immunol. Scand., 107, pp. 137-143
Ramos-DeSimone, N., Hahn-Dantona, E., Sipley, J., Nagase, H., French, D.L., Quigley, J.P., Activation of matrix metalloproteinase-9 (MMP9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion (1999) J. Biol. Chem., 274, pp. 13066-13076
Opdenakker, G., Van den Steen, P.E., Van Damme, J., Gelatinase B: a tuner and amplifier of immune functions (2001) Trends Immunol., 22, pp. 571-579
Robinson, S.N., Pisarev, V.M., Chavez, J.M., Singh, R.K., Talmadge, J.E., Use of matrix metalloproteinase MMP9 knockout mice demonstrates that MMP9 activity is not absolutely required for G-CSF or Flt-3 ligand-induced hematopoietic progenitor cell mobilization or engraftment (2003) Stem Cells, 21, pp. 417-427
Asahi, M., Sumii, T., Fini, M.E., Itohara, S., Lo, E.H., Matrix metalloproteinase 2 gene knockout has no effect on acute brain injury after focal ischemia (2001) NeuroReport, 12, pp. 3003-3007
Itoh, T., Ikeda, T., Gomi, H., Nakao, S., Suzuki, T., Itohara, S., Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice (1997) J. Biol. Chem., 272, pp. 22389-22392
Leclercq, A., Houard, X., Philippe, M., Ollivier, V., Sebbag, U., Meilhac, O., Michel, J.B., Involvement of intraplaque hemorrhage in atherothrombosis evolution via neutrophil protease enrichment (2007) J. Leukocyte Biol., 82, pp. 1420-1429
Reichel, C.A., Rehberg, M., Bihari, P., Moser, C.M., Linder, S., Khandaga, A., Krombach, F., Gelatinases mediate neutrophil recruitment in vivo: evidence for stimulus specificity and a critical role in collagen IV remodelling (2008) J. Leukocyte Biol., 83, pp. 864-874
Kühn, K., Basement membrane (type IV) collagen (1995) Matrix Biol., 14, pp. 439-445
Prockop, D.J., Kivirikko, K.I., Collagens: molecular biology, diseases, and potentials for therapy (1995) Annu. Rev. Biochem., 64, pp. 403-434
Dolz, R., Engel, J., Kühn, K., Folding of collagen IV (1988) Eur. J. Biochem., 178, pp. 357-366
Timpl, R., Wiedemann, H., van Delden, V., Furthmayr, H., Kühn, K., A network model for the organization of type IV collagen molecules in basement membranes (1981) Eur. J. Biochem., 120, pp. 203-211
Timpl, R., Structure and biological activity of basement membrane proteins (1989) Eur. J. Biochem., 180, pp. 487-502
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Lauer-Fields, J.L., Cudic, M., Wei, S., Mari, F., Fields, G.B., Brew, K., Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors (2007) J. Biol. Chem., 282, pp. 26948-26955
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Tam, E.M., Moore, T.R., Butler, G.S., Overall, C.M., Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin C domains and the MMP2 fibronectin type II modules in collagen triple helicase activities (2004) J. Biol. Chem., 279, pp. 43336-43344
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Mackay, A.R., Hartzler, J.L., Pelina, M.D., Thorgeirsson, U.P., Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen (1990) J. Biol. Chem., 265, pp. 21929-21934
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Himelstein, B.P., Canete-Soler, R., Bernhard, E.J., Dilks, D.W., Muschel, R.J., Metalloproteinases in tumor progression: the contribution of MMP9 (1994) Invasion Metastasis, 14, pp. 246-258
Ueda, Y., Imai, K., Tsuchiya, H., Fujimoto, N., Nakanishi, I., Katsuda, S., Matrix metalloproteinase 9 (gelatinase B) is expressed in multinucleated giant cells of human giant cell tumor of bone and is associated with vascular invasion (1996) Am. J. Pathol., 148, pp. 611-622
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Opdenakker, G., Nelissen, I., van Damme, J., Functional roles and therapeutic targeting of gelatinase B and chemokines in multiple sclerosis (2003) Lancet Neurol., 2, pp. 747-756
Gutiérrez-Fernández, A., Inada, M., Balbín, M., Fueyo, A., Pitiot, A.S., Astudillo, A., Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP8) (2007) FASEB J., 21, pp. 2580-2591
Longo, G.M., Xiong, W., Greiner, T.C., Zhao, Y., Fiotti, N., Baxter, B.T., Matrix metalloproteinases 2 and 9 work in concert to produce aortic aneurysms (2002) J. Clin. Invest., 110, pp. 625-632
Itoh, T., Matsuda, H., Tanioka, M., Kuwabara, K., Itohara, S., Suzuki, R., The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis (2002) J. Immunol., 169, pp. 2643-2647
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Bányai, L., Patthy, L., Evidence for the involvement of type II domains in collagen binding by 72-kDa type IV procollagenase (1991) FEBS Lett., 282, pp. 23-25
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Masure, S., Proost, P., Van Damme, J., Opdenakker, G., Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8 (1991) Eur. J. Biochem., 198, pp. 391-398
Laemmlli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Ventzki, R., Rüggeberg, S., Leicht, S., Franz, T., Stegemann, J., Comparative 2-DE protein analysis in a 3-D geometry gel (2007) BioTechniques, 42, pp. 271-275
Ishihama, Y., Rappsilber, J., Mann, M., SCX-Stage tip separation using C18-SCX-C18 Stage tip analyzed by LC-MS (2006) J. Proteome Res., 5, pp. 988-999
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Felkel, C., Schöll, U., Mäder, M., Schwartz, P., Felgenhauer, K., Hardeland, R., Migration of human granulocytes through reconstituted basement membrane is not dependent on matrix metalloproteinase-9 (MMP9) (2001) J. Neuroimmunol., 116, pp. 49-55
Overall, C. M., Blobel, C. P., In search of partners: linking extracellular proteases to substrates (2007) Nat. Rev. Mol. Cell Biol., 8, pp. 245-25
Sternlicht, M. D., Werb, Z., How matrix metalloproteinases regulate cell behavior (2001) Annu. Rev. Cell Dev. Biol., 17, pp. 463-516
Allan, J. A., Docherty, A. J., Barker, P. J., Huskisson, N. S., Reynolds, J. J., Murphy, G., Binding of gelatinases A and B to type-I collagen and other matrix components (1995) Biochem. J., 309, pp. 299-306
Van den Steen, P. E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., The hemopexin and O-glycosylated domains tune gelatinase B/MMP9 bioavailability via inhibition and binding to cargo receptors (2006) J. Biol. Chem., 281, pp. 18626-18637
Bachmeier, B. E., Iancu, C. M., Jocum, M., Nerlich, A. G., Matrix metalloproteinases in cancer: comparison of known and novel aspects of their inhibition as a therapeutic approach (2005) Exp. Rev. Anticancer Ther., 5, pp. 149-163
Mook, O. R., Frederiks, W. M., Van Noorden, J., The role of gelatinases in colorectal cancer progression and metastasis (2004) Biochim. Biophys. Acta, 1705, pp. 69-89
Strongin, A. Y., Collier, I., Bannikov, G., Marmer, B. L., Grant, G. A., Goldberg, G. I., Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease (1995) J. Biol. Chem., 270, pp. 5331-5338
Robinson, S. N., Pisarev, V. M., Chavez, J. M., Singh, R. K., Talmadge, J. E., Use of matrix metalloproteinase MMP9 knockout mice demonstrates that MMP9 activity is not absolutely required for G-CSF or Flt-3 ligand-induced hematopoietic progenitor cell mobilization or engraftment (2003) Stem Cells, 21, pp. 417-427
Reichel, C. A., Rehberg, M., Bihari, P., Moser, C. M., Linder, S., Khandaga, A., Krombach, F., Gelatinases mediate neutrophil recruitment in vivo: evidence for stimulus specificity and a critical role in collagen IV remodelling (2008) J. Leukocyte Biol., 83, pp. 864-874
K hn, K., Basement membrane (type IV) collagen (1995) Matrix Biol., 14, pp. 439-445
Prockop, D. J., Kivirikko, K. I., Collagens: molecular biology, diseases, and potentials for therapy (1995) Annu. Rev. Biochem., 64, pp. 403-434
K hn, K., Wiedemann, H., Timpl, R., Risteli, J., Dieringer, H., Voss, T., Glanville, R. W., Macromolecular structure of basement membrane collagens (1981) FEBS Lett., 125, pp. 123-128
Kamphaus, G. D., Colorado, P. C., Panka, D. J., Hopfer, H., Ramchandran, R., Torre, A., Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor growth (2000) J. Biol. Chem., 275, pp. 1209-1215
Lauer-Fields, J. L., Cudic, M., Wei, S., Mari, F., Fields, G. B., Brew, K., Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors (2007) J. Biol. Chem., 282, pp. 26948-26955
Tam, E. M., Moore, T. R., Butler, G. S., Overall, C. M., Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin C domains and the MMP2 fibronectin type II modules in collagen triple helicase activities (2004) J. Biol. Chem., 279, pp. 43336-43344
Mackay, A. R., Hartzler, J. L., Pelina, M. D., Thorgeirsson, U. P., Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen (1990) J. Biol. Chem., 265, pp. 21929-21934
Hostikka, S. L. A., Tryggvason, K., Extensive structural differences between genes for the alpha-1 and alpha-2 chains of type IV collagen despite conservation of coding sequences (1987) FEBS Lett., 224, pp. 297-305
Ardi, V. C., Kupriyanova, T. A., Deryugina, E. I., Quigley, J. P., Human neutrophils uniquely release TIMP-free MMP9 to provide a potent catalytic stimulator of angiogenesis (2007) Proc. Natl Acad. Sci. USA, 104, pp. 20262-20267
Himelstein, B. P., Canete-Soler, R., Bernhard, E. J., Dilks, D. W., Muschel, R. J., Metalloproteinases in tumor progression: the contribution of MMP9 (1994) Invasion Metastasis, 14, pp. 246-258
Vidovszky, T. J., Cabanela, M. E., Rock, M. G., Berry, D. J., Morrey, B. F., Bolander, M. E., Histologic and biochemical differences between osteolytic and nonosteolytic membranes around femoral components of an uncemented total hip arthroplasty (1998) J. Arthroplasty, 13, pp. 320-330
Guti rrez-Fern ndez, A., Inada, M., Balb n, M., Fueyo, A., Pitiot, A. S., Astudillo, A., Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP8) (2007) FASEB J., 21, pp. 2580-2591
Longo, G. M., Xiong, W., Greiner, T. C., Zhao, Y., Fiotti, N., Baxter, B. T., Matrix metalloproteinases 2 and 9 work in concert to produce aortic aneurysms (2002) J. Clin. Invest., 110, pp. 625-632
B nyai, L., Patthy, L., Evidence for the involvement of type II domains in collagen binding by 72-kDa type IV procollagenase (1991) FEBS Lett., 282, pp. 23-25
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Laemmlli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Ventzki, R., R ggeberg, S., Leicht, S., Franz, T., Stegemann, J., Comparative 2-DE protein analysis in a 3-D geometry gel (2007) BioTechniques, 42, pp. 271-275
Knight, C. G., Willenbrock, F., Murphy, G., A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases (1992) FEBS Lett., 296, pp. 263-266
Felkel, C., Sch ll, U., M der, M., Schwartz, P., Felgenhauer, K., Hardeland, R., Migration of human granulocytes through reconstituted basement membrane is not dependent on matrix metalloproteinase-9 (MMP9) (2001) J. Neuroimmunol., 116, pp. 49-55
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.871, 5-year impact factor: 4.303
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-59149094419&partnerID=40&md5=bb0287fbd44ec55112d6b69147937514
Keywords: Collagen Binding Domain, Gelatinase B, Kinetics, Matrix Metalloproteinases, Type Iv Collagen Fragmentation, Collagen Type 4, Fibronectin, Matrix Metalloproteinase Inhibitor, Analytic Method, Article, Binding Site, Catalysis, Cell Migration, Collagen Degradation, Conformational Transition, Controlled Study, Edman Sequencing, Enzyme Activity, Human, Human Cell, Mass Spectrometry, Neutrophil, Placenta, Priority Journal, Protein Binding, Protein Degradation, Protein Domain, Surface Plasmon Resonance, Environmental Monitoring, Peptides, Protein Interaction Mapping, Sequence Analysis, Temperature,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine and Biochemical Sciences, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Rome, Italy
Department of Oral Biological and Medical Sciences, Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC V6T1Z3, Canada
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC V6T1Z3, Canada
Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, P.za Umberto I 1, I-70100 Bari, Italy
Rega Institute for Medical Research, Laboratory of Immunobiology, University of Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium
Department of Chemistry, University of Catania, V.le A. Doria, Catania, Italy
Institute of Biostructure and Bioimaging, CNR, V.le A. Doria, Catania, Italy
References:
Overall, C.M., Blobel, C.P., In search of partners: linking extracellular proteases to substrates (2007) Nat. Rev. Mol. Cell Biol., 8, pp. 245-25
Sternlicht, M.D., Werb, Z., How matrix metalloproteinases regulate cell behavior (2001) Annu. Rev. Cell Dev. Biol., 17, pp. 463-516
Allan, J.A., Docherty, A.J., Barker, P.J., Huskisson, N.S., Reynolds, J.J., Murphy, G., Binding of gelatinases A and B to type-I collagen and other matrix components (1995) Biochem. J., 309, pp. 299-306
Van den Steen, P.E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., The hemopexin and O-glycosylated domains tune gelatinase B/MMP9 bioavailability via inhibition and binding to cargo receptors (2006) J. Biol. Chem., 281, pp. 18626-18637
Bachmeier, B.E., Iancu, C.M., Jocum, M., Nerlich, A.G., Matrix metalloproteinases in cancer: comparison of known and novel aspects of their inhibition as a therapeutic approach (2005) Exp. Rev. Anticancer Ther., 5, pp. 149-163
Mook, O.R., Frederiks, W.M., Van Noorden, J., The role of gelatinases in colorectal cancer progression and metastasis (2004) Biochim. Biophys. Acta, 1705, pp. 69-89
Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A., Goldberg, G.I., Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease (1995) J. Biol. Chem., 270, pp. 5331-5338
Seiki, M., Membrane-type matrix metalloproteinases (1999) Acta Pathol., Microbiol. Immunol. Scand., 107, pp. 137-143
Ramos-DeSimone, N., Hahn-Dantona, E., Sipley, J., Nagase, H., French, D.L., Quigley, J.P., Activation of matrix metalloproteinase-9 (MMP9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion (1999) J. Biol. Chem., 274, pp. 13066-13076
Opdenakker, G., Van den Steen, P.E., Van Damme, J., Gelatinase B: a tuner and amplifier of immune functions (2001) Trends Immunol., 22, pp. 571-579
Robinson, S.N., Pisarev, V.M., Chavez, J.M., Singh, R.K., Talmadge, J.E., Use of matrix metalloproteinase MMP9 knockout mice demonstrates that MMP9 activity is not absolutely required for G-CSF or Flt-3 ligand-induced hematopoietic progenitor cell mobilization or engraftment (2003) Stem Cells, 21, pp. 417-427
Asahi, M., Sumii, T., Fini, M.E., Itohara, S., Lo, E.H., Matrix metalloproteinase 2 gene knockout has no effect on acute brain injury after focal ischemia (2001) NeuroReport, 12, pp. 3003-3007
Itoh, T., Ikeda, T., Gomi, H., Nakao, S., Suzuki, T., Itohara, S., Unaltered secretion of beta-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice (1997) J. Biol. Chem., 272, pp. 22389-22392
Leclercq, A., Houard, X., Philippe, M., Ollivier, V., Sebbag, U., Meilhac, O., Michel, J.B., Involvement of intraplaque hemorrhage in atherothrombosis evolution via neutrophil protease enrichment (2007) J. Leukocyte Biol., 82, pp. 1420-1429
Reichel, C.A., Rehberg, M., Bihari, P., Moser, C.M., Linder, S., Khandaga, A., Krombach, F., Gelatinases mediate neutrophil recruitment in vivo: evidence for stimulus specificity and a critical role in collagen IV remodelling (2008) J. Leukocyte Biol., 83, pp. 864-874
Kühn, K., Basement membrane (type IV) collagen (1995) Matrix Biol., 14, pp. 439-445
Prockop, D.J., Kivirikko, K.I., Collagens: molecular biology, diseases, and potentials for therapy (1995) Annu. Rev. Biochem., 64, pp. 403-434
Dolz, R., Engel, J., Kühn, K., Folding of collagen IV (1988) Eur. J. Biochem., 178, pp. 357-366
Timpl, R., Wiedemann, H., van Delden, V., Furthmayr, H., Kühn, K., A network model for the organization of type IV collagen molecules in basement membranes (1981) Eur. J. Biochem., 120, pp. 203-211
Timpl, R., Structure and biological activity of basement membrane proteins (1989) Eur. J. Biochem., 180, pp. 487-502
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Tam, E. M., Moore, T. R., Butler, G. S., Overall, C. M., Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin C domains and the MMP2 fibronectin type II modules in collagen triple helicase activities (2004) J. Biol. Chem., 279, pp. 43336-43344
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Himelstein, B. P., Canete-Soler, R., Bernhard, E. J., Dilks, D. W., Muschel, R. J., Metalloproteinases in tumor progression: the contribution of MMP9 (1994) Invasion Metastasis, 14, pp. 246-258
Vidovszky, T. J., Cabanela, M. E., Rock, M. G., Berry, D. J., Morrey, B. F., Bolander, M. E., Histologic and biochemical differences between osteolytic and nonosteolytic membranes around femoral components of an uncemented total hip arthroplasty (1998) J. Arthroplasty, 13, pp. 320-330
Guti rrez-Fern ndez, A., Inada, M., Balb n, M., Fueyo, A., Pitiot, A. S., Astudillo, A., Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP8) (2007) FASEB J., 21, pp. 2580-2591
Longo, G. M., Xiong, W., Greiner, T. C., Zhao, Y., Fiotti, N., Baxter, B. T., Matrix metalloproteinases 2 and 9 work in concert to produce aortic aneurysms (2002) J. Clin. Invest., 110, pp. 625-632
B nyai, L., Patthy, L., Evidence for the involvement of type II domains in collagen binding by 72-kDa type IV procollagenase (1991) FEBS Lett., 282, pp. 23-25
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
Laemmlli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Ventzki, R., R ggeberg, S., Leicht, S., Franz, T., Stegemann, J., Comparative 2-DE protein analysis in a 3-D geometry gel (2007) BioTechniques, 42, pp. 271-275
Knight, C. G., Willenbrock, F., Murphy, G., A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases (1992) FEBS Lett., 296, pp. 263-266
Felkel, C., Sch ll, U., M der, M., Schwartz, P., Felgenhauer, K., Hardeland, R., Migration of human granulocytes through reconstituted basement membrane is not dependent on matrix metalloproteinase-9 (MMP9) (2001) J. Neuroimmunol., 116, pp. 49-55
The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase
Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive gelatinase A (MMP2) and the inducible gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites. © 2008 Elsevier Ltd. All rights reserved.
Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive gelatinase A (MMP2) and the inducible gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites. © 2008 Elsevier Ltd. All rights reserved.
The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase
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The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase
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* BRAF(V600E) mutation and the biology of papillary thyroid cancer (545 views)
Endocr Relat Cancerendocrine Related Cancer (ISSN: 1351-0088), 2008; 15(1): 191-205.
Impact Factor: 5.236
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Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
* A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111) (357 views)
Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Impact Factor: 3.664
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Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
* In situ AP/MALDI-MS characterization of anchored matrix metalloproteinases (433 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2006 Dec; 41(12): 1561-1569.
Impact Factor: 2.945
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Grasso G, D'Agata R, Rizzarelli E, Spoto G, D'Andrea LD, Pedone C, Picardi A, Romanelli A, Fragai M, Yeo KJ
* Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS (577 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
Impact Factor: 3.574
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12 Records (12 excluding Abstracts).
Total impact factor: 48.304 (48.304 excluding Abstracts).
Total 5 year impact factor: 50.237 (50.237 excluding Abstracts).
Total impact factor: 48.304 (48.304 excluding Abstracts).
Total 5 year impact factor: 50.237 (50.237 excluding Abstracts).
460 views. Last view on Monday 24 April 2023, 9:51:53
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