The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (676 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
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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:
Not available.
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:
Not available.
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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12 Records (12 excluding Abstracts).
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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).
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