| Modulation of the proteolytic activity of matrix metalloproteinase-2 (gelatinase A) on fibrinogen. | |
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MedLine Citation:
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PMID: 17087661 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The proteolytic processing of bovine fibrinogen by MMP-2 (gelatinase A), which brings about the formation of a product unable to form fibrin clots, has been studied at 37 degrees C. Catalytic parameters, although showing a somewhat lower catalytic efficiency with respect to thrombin and plasmin, indeed display values indicating a pathophysiological significance of this process. A parallel molecular modelling study predicts preferential binding of MMP-2 to the beta-chain of fibrinogen through its haemopexin-like domain, which has been directly demonstrated by the inhibitory effect in the presence of the exogenous haemopexin-like domain. However, the removal of this domain does not impair the interaction between MMP-2 and fibrinogen, but it dramatically alters the proteolytic mechanism, producing different fragmentation intermediates. The investigation at various pH values between 6.0 and 9.3 indicates a proton-linked behaviour, which is relevant for interpreting the influence on the process by environmental conditions occurring at the site of an injury. Furthermore, the action of MMP-2 on peroxynitrite-treated fibrinogen has been investigated, a situation possibly occurring under oxidative stress. The chemical alteration of fibrinogen, which has been shown to abolish its clotting activity, brings about only limited modifications of the catalytic parameters without altering the main enzymatic mechanism. |
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Authors:
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Susanna Monaco; Magda Gioia; Janet Rodriguez; Giovanni Francesco Fasciglione; Donato Di Pierro; Giulio Lupidi; Ludwig Krippahl; Stefano Marini; Massimo Coletta |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 402 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2007 Mar |
Date Detail:
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Created Date: 2007-02-22 Completed Date: 2007-03-19 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 503-13 Citation Subset: IM |
Affiliation:
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Department of Experimental Medicine and Biochemical Sciences, University of Roma Tor Vergata, Via Montpellier 1, I-00133 Roma, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Animals Catalysis Cattle Fibrinogen / chemistry, metabolism* Hemopexin / metabolism Hydrogen-Ion Concentration Kinetics Matrix Metalloproteinase 2 / chemistry, metabolism* Models, Molecular Peroxynitrous Acid Protein Structure, Quaternary |
| Chemical | |
Reg. No./Substance:
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14691-52-2/Peroxynitrous Acid; 9001-32-5/Fibrinogen; 9013-71-2/Hemopexin; EC 3.4.24.24/Matrix Metalloproteinase 2 |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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