Matrix metalloproteinase-2 (gelatinase A) and Matrix metalloproteinase-9 (gelatinase B) (MMP-2 (for gelatinase A), MMP-9 (for gelatinase B))

Gelatinases are a subgroup of matrix metalloproteinases (MMPs)—specifically, MMP-2 (gelatinase A) and MMP-9 (gelatinase B)—that depend on zinc ions and hydrolyze gelatin and type IV collagen, among other extracellular matrix components. These enzymes contain a catalytic domain that coordinates zinc, a hemopexin-like domain for substrate and inhibitor interactions, and a unique fibronectin type II-like domain that mediates collagen binding. Their activity regulates processes such as tissue remodeling, cell migration, angiogenesis, and wound healing, but dysregulation is linked to cancer progression, arthritis, and other diseases. As proteases produced by both human and microbial cells, they may act as virulence factors in infections. Therapeutic inhibition is challenging due to overlap in physiological and pathological functions and risk of adverse side effects.

Other names

Gelatinase A (MMP-2)Gelatinase B (MMP-9)Type IV collagenase72-kDa gelatinase (MMP-2)92-kDa gelatinase (MMP-9)

Inhibition of the proteolytic activity by blocking active site zinc or allosteric regions - Chelation of catalytic zinc - Competitive blocking of substrate binding - Inhibition of enzyme activation (proenzyme forms)