Matrix metallopeptidase 7 (MMP7)

Matrix metallopeptidase 7 (MMP7), also known as matrilysin, is a zinc-dependent endopeptidase of the matrix metalloproteinase (MMP) family, encoded by the MMP7 gene in humans[1][2][7]. MMP7 is distinguished by its small size and unique lack of a hemopexin domain compared to other MMPs, but retains substrate specificity for extracellular matrix components such as casein, fibronectin, various types of gelatin, and proteoglycans[1][2]. MMP7 is highly expressed in epithelial tissues, particularly in organs including intestine, lung, and kidney, where it is involved in physiological processes like matrix degradation, tissue remodeling, inflammation, and regulatory cleavage of cell surface molecules[1][3][4]. Pathologically, MMP7 plays a role in tumor growth, metastasis, tissue fibrosis, inflammation, and post-injury repair, often being associated with cancer progression and poorer patient outcomes when overexpressed[2][3][4]. Drugs targeting MMP7 typically act by inhibiting its proteolytic function, with their development hampered by specificity and safety challenges[2][4]. MMP7 is considered both a potential therapeutic target and a disease biomarker across several conditions[2][3][4].

Other names

MatrilysinPump-1 proteaseUterine metalloproteinaseMMP-7PUMP-1 proteinaseMetalloproteinase pump-1MatrinPutative metalloproteinaseMatrix metalloproteinase pump 1

Inhibition of proteolytic breakdown of extracellular matrix proteins. Suppression of tumor invasion and metastasis by inhibiting MMP7 activity. Blockade of MMP7-dependent activation of signaling molecules or cytokines.