Elsevier on behalf of the Federation of European Biochemical Societies
FEBS Letters vol:586 issue:24 pages:4264-4269
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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Meprin betacleavesMMP-9 by enzymatic study (View interaction) Meprin betacleavesMMP-9 by zymography (View interaction) Meprin alphacleavesMMP-9 by zymography (View interaction) Meprin alphacleavesMMP-9 by enzymatic study (View interaction).