6533b838fe1ef96bd12a5223
RESEARCH PRODUCT
Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3
Paul ProostPhilippe E. Van Den SteenWalter StöckerGhislain OpdenakkerChristoph Becker-paulyNathalie GeurtsErik Martenssubject
ProteasesNeutrophilsMolecular Sequence DataBiophysicsMatrix metalloproteinaseBiochemistryMonocytesProtein–protein interactionAminoterminal cleavageStructural BiologyGeneticsHumansProMMP-9ZymographyAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChemistryActivator (genetics)TioproninMeprinCell BiologyTissue inhibitor of metalloproteinaseEnzymeMatrix Metalloproteinase 9BiochemistryCulture Media ConditionedMatrix Metalloproteinase 3Astacindescription
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 NH2-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 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)
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-10-16 | FEBS Letters |