MMP7

MMP7 Full Name

matrix metallopeptidase 7 (matrilysin, uterine)

MMP7 Introduction

MMP7 (Matrix Metallopeptidase 7), also known as matrilysin or PUMP-1, is a member of the peptidase M10 family of matrix metalloproteinases (MMPs) and is located on chromosome 11q21-q22. Unlike most MMP family members, MMP7 exhibits a unique structural feature: it lacks a conserved C-terminal hemopexin domain, which typically mediates protein-protein interactions and substrate specificity. This makes MMP7 the smallest known MMP, consisting primarily of an N-terminal pro-domain with a cysteine switch motif and a catalytic domain containing a zinc-dependent metalloprotease active site. The encoded preproprotein undergoes proteolytic processing to generate the mature, secreted endopeptidase, which requires zinc ions for its enzymatic activity. MMP7 exhibits broad substrate specificity, capable of degrading proteoglycans, fibronectin, elastin, casein, and various extracellular matrix components.

Figure 1. Strcuture of MMP7.

Physiological Functions in Tissue Repair and Mucosal Immunity
MMP7 plays essential roles in normal physiological processes, particularly in wound healing and epithelial defense mechanisms. Following tissue injury, MMP7 expression is rapidly induced in epithelial cells bordering the wound site, where it coordinates cell migration and inflammatory responses necessary for proper repair. The enzyme contributes to wound closure by cleaving specific substrates in a temporally regulated manner: early after injury, it sheds syndecan-1 to facilitate cell migration and neutrophil recruitment, while later it cleaves E-cadherin to help resolve inflammation by promoting influx of immunosuppressive cells. In the intestinal mucosa, MMP7 regulates the activity of defensins—antimicrobial peptides essential for host defense against bacteria—by processing their pro-forms into active peptides. Additionally, MMP7 participates in the defense response against both Gram-negative and Gram-positive bacteria, highlighting its critical role in mucosal immunity. Studies in Mmp7-null mice reveal impaired wound healing, decreased bacterial defense, and altered inflammatory responses.

Emerging Roles in Inflammatory and Fibrotic Diseases
Recent research has uncovered significant roles for MMP7 in inflammatory and fibrotic conditions beyond cancer. In biliary atresia, a neonatal cholestatic disease, MMP7 is upregulated via TLR4/NF-κB signaling in response to viral-bacterial cooperative stimulation, contributing to both extracellular matrix remodeling and amplification of inflammatory signaling. The loss of endotoxin tolerance in this condition leads to uncontrolled inflammation and tissue damage, with MMP7 acting as a dual-function molecule linking matrix degradation to immune dysregulation. In chronic kidney disease (CKD), MMP7 has emerged as a key regulator exerting more pronounced influence than other MMPs, contributing to renal fibrosis and disease progression. Studies investigating therapeutic targeting have identified compounds like manidipine that reduce MMP7 enzymatic activity, enhance autophagy, suppress inflammasome activation, and attenuate renal fibrosis, suggesting MMP7 as a promising therapeutic target in CKD.

Alternate Names for MMP7

MMP7; matrix metallopeptidase 7 (matrilysin, uterine); MMP-7; MPSL1; PUMP-1; matrilysin; matrin; pump-1 protease; uterine matrilysin; uterine metalloproteinase; matrix metalloproteinase-7; matrix metalloproteinase 7 (matrilysin, uterine);