MMP-7

MMP-7 (matrix metalloproteinase-7, matrilysin-1) is a secreted zinc-dependent endopeptidase that participates in extracellular matrix remodeling and the proteolytic processing of multiple non-matrix substrates, thereby influencing cell proliferation, apoptosis, epithelial repair, and tissue homeostasis^[1]. Unlike many other matrix metalloproteinases, MMP-7 is one of the smallest family members and lacks the conserved C-terminal hemopexin domain, a structural distinction that contributes to its unique substrate profile and biological functions^[1]. Mechanistically, Wnt/β-catenin signaling is a major upstream regulator of MMP-7 transcription, and MMP-7 is a well-established downstream target of β-catenin/TCF-mediated gene activation^[2][3]. Through cleavage of substrates including E-cadherin, Fas ligand, and nephrin, MMP-7 regulates epithelial integrity, cell survival, epithelial-mesenchymal transition, and tissue remodeling processes^[1]. In disease settings, elevated MMP-7 expression is associated with tumor progression, invasion, metastasis, and angiogenesis across multiple cancer types, while persistent induction of MMP-7 is also linked to kidney injury, fibrosis, and chronic kidney disease progression^[1][4]. Compared with related isoforms such as MMP-2 and MMP-9, MMP-7 exhibits distinct biological activities; notably, MMP-7 can cleave nephrin and promote proteinuria, a function not reported for MMP-2 or MMP-9^[1]. For experimental applications, selective MMP-7 inhibitors have recently demonstrated efficacy in reducing kidney fibrosis in preclinical models, supporting the use of MMP-7 as both a mechanistic target and a translational biomarker in disease research^[4].