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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/16910

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
Citation: 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.
URI: http://hdl.handle.net/1942/16910
DOI: 10.1016/j.febslet.2012.10.033
ISI #: 000312004400003
ISSN: 0014-5793
Category: A1
Type: Journal Contribution
Appears in Collections: Research publications

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