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Title: | Meprins process matrix metalloproteinase-9 ( MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3 | Authors: | GEURTS, Nathalie Becker-Pauly, Christoph Martens, Erik Proost, Paul Van den Steen, Philippe E. Stöcker, Walter OPDENAKKER, Ghislain |
Issue Date: | 2012 | Publisher: | ELSEVIER SCIENCE BV | Source: | FEBS LETTERS, 586 (24), p. 4264-4269 | Abstract: | Meprin alpha and beta, members of the astacin family of zinc metalloproteinases, are unique plasma membrane and secreted proteases known to cleave a wide range of biological substrates involved in inflammation, cancer and fibrosis. In this study, we identified proMMP-9 as a novel substrate and show that aminoterminal meprin-mediated clipping improves the activation kinetics of proMMP-9 by MMP-3, an efficient activator of proMMP-9. Interestingly, the NH2-terminus LVLFPGDL, generated by incubation with meprin alpha, is identical to the form produced in conditioned media from human neutrophils and monocytes. Hence, this meprin-mediated processing and enhancement of MMP-9 activation kinetics may have biological relevance in the context of in vivo inflammatory processes. Structured summary of protein interactions: Meprin beta cleaves MMP-9 by enzymatic study (View interaction) Meprin beta cleaves MMP-9 by zymography (View interaction) Meprin alpha cleaves MMP-9 by zymography (View interaction) Meprin alpha cleaves MMP-9 by enzymatic study (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | Notes: | [Geurts, Nathalie; Martens, Erik; Van den Steen, Philippe E.; Opdenakker, Ghislain] Univ Louvain, Rega Inst Med Res, Immunobiol Lab, B-3000 Louvain, Belgium. [Becker-Pauly, Christoph] Univ Kiel, Unit Degrad Protease Web, Inst Biochem, D-24118 Kiel, Germany. [Proost, Paul] Univ Louvain, Rega Inst Med Res, Lab Mol Immunol, B-3000 Louvain, Belgium. [Stoecker, Walter] Johannes Gutenberg Univ Mainz, Inst Zool, Dept Cell & Matrix Biol, D-55128 Mainz, Germany. | Keywords: | Meprin; ProMMP-9; Aminoterminal cleavage;biochemistry & molecular biology; biophysics; cell biology | Document URI: | http://hdl.handle.net/1942/16910 | ISSN: | 0014-5793 | e-ISSN: | 1873-3468 | DOI: | 10.1016/j.febslet.2012.10.033 | ISI #: | 000312004400003 | Rights: | © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | Category: | A1 | Type: | Journal Contribution |
Appears in Collections: | Research publications |
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