Matrix metallopeptidase 3 (MMP-3)

Matrix metallopeptidase 3 (MMP-3), also known as stromelysin-1, is a secreted zinc-dependent endopeptidase belonging to the matrix metalloproteinase family. It is encoded by the MMP3 gene in humans and comprises 475–478 amino acids. MMP-3 degrades multiple components of the extracellular matrix and also activates other MMPs, making it a key regulator of connective tissue remodeling under physiological (e.g., development, wound healing) and pathological conditions (e.g., cancer invasion, arthritis progression). While prominent in disease tissue degradation and tumor metastasis, MMP-3 also has essential physiological roles, including transcriptional modulation. Measurement of MMP-3 levels is used as a biomarker in diseases like rheumatoid arthritis and cancer. Despite longstanding interest as a drug target, direct therapeutic inhibition of MMP-3 poses safety challenges, and recent focus in drug development includes both modulation and biomarker utility.

Other names

Stromelysin-1Matrix metalloproteinase-3Transin-1SL-1

Competitive inhibition of the MMP-3 catalytic site (for synthetic inhibitors); Regulation of ECM composition and remodeling (therapeutic strategies target excess activity in disease states); Indirect reduction via upstream immunomodulation (e.g., anti-inflammatory DMARD therapy results in reduced MMP-3 levels)