Matrix metalloproteinase-2 (MMP-2)

Matrix metalloproteinase‑2 is a zinc-dependent endopeptidase enzyme encoded by the *MMP2* gene on chromosome 16. It is also known as gelatinase A or 72 kDa type IV collagenase. This enzyme plays a central role in degrading components of the extracellular matrix—especially type IV collagen—during normal physiological processes such as embryonic development, menstruation/endometrial breakdown, angiogenesis, wound healing/tissue repair, bone remodeling, and regulation of inflammation. Dysregulation or overexpression contributes to pathological conditions including cancer invasion/metastasis through basement membrane degradation; cardiovascular diseases via vascular remodeling; diabetic complications; fibrotic disorders; arthritis; rare inherited bone/joint syndromes like MONA/Torg-Winchester syndrome. The activity is tightly regulated by proteolytic activation from its proenzyme form at cell surfaces involving other membrane-type MMPs and specific endogenous inhibitors called TIMPs. While considered an important therapeutic target—especially in oncology—the dual roles in both health and disease present challenges for drug development due to potential side effects on normal tissue maintenance.

Other names

72 kDa type IV collagenaseGelatinase AMatrix metallopeptidase 2

Inhibition of enzymatic activity to prevent extracellular matrix degradation and tumor metastasis by blocking the active site or chelating the zinc ion required for catalysis.