MMP-7

MMP-7 (matrilysin), the smallest zinc-dependent endopeptidase in the MMP family, lacks a hemopexin domain but features a catalytic zinc-binding motif (HEXXHXXGXXH) critical for degrading extracellular matrix (ECM) components, including collagens III/IV/V, elastin, and proteoglycans. Activated via proteolytic cleavage (e.g., by MMP-3), it promotes tissue remodeling in wound healing while driving pathological processes such as tumor invasion (via E-cadherin degradation and Wnt/β-catenin activation) and fibrosis (via β-catenin-mediated renal damage). Overexpressed in epithelial cancers, MMP-7 correlates with metastasis but paradoxically shows protective genetic variants in some contexts. It also processes non-ECM substrates like TNF-α and Fas ligand, amplifying inflammation and oncogenesis. In fibrotic diseases, elevated serum MMP-7 predicts progression, serving as a diagnostic biomarker. Therapeutic strategies targeting MMP-7, including inhibitors and monoclonal antibodies, highlight its dual roles as both a driver of ECM disruption and a modulator of immune-tumor interactions.

MMP7,Matrilysin,Matrin,MPSL1,PUMP1