Journal
FEBS LETTERS
Volume 586, Issue 24, Pages 4264-4269Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.10.033
Keywords
Meprin; ProMMP-9; Aminoterminal cleavage
Funding
- Fund for Scientific Research-Flanders (FWO-Vlaanderen)
- Geconcerteerde OnderzoeksActies [GOA 2012-017]
- Deutsche Forschungsgemeinschaft (DFG) [BE 4086/1-2, SFB877]
- Cluster of Excellence Inflammation at Interfaces
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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.
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