Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3.

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 Lett

journal_title

FEBS letters

authors

Geurts N,Becker-Pauly C,Martens E,Proost P,Van den Steen PE,Stöcker W,Opdenakker G

doi

10.1016/j.febslet.2012.10.033

subject

Has Abstract

pub_date

2012-12-14 00:00:00

pages

4264-9

issue

24

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00816-2

journal_volume

586

pub_type

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