Abstract:
:Meprin α and β, 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 NH(2)-terminus LVLFPGDL, generated by incubation with meprin α, 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Geurts N,Becker-Pauly C,Martens E,Proost P,Van den Steen PE,Stöcker W,Opdenakker Gdoi
10.1016/j.febslet.2012.10.033subject
Has Abstractpub_date
2012-12-14 00:00:00pages
4264-9issue
24eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00816-2journal_volume
586pub_type
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