Matrix metalloproteinase-2 (MMP2) (MMP2)

Matrix metalloproteinase-2 (MMP2), also known as 72 kDa type IV collagenase or gelatinase A, is a zinc-dependent endopeptidase belonging to the matrix metalloproteinase family [1, 12]. It plays a fundamental role in the degradation of extracellular matrix (ECM) components, specifically targeting type IV collagen in the basement membrane, as well as gelatin, elastin, and fibronectin [2, 4, 14]. Under normal physiological conditions, MMP2 is essential for processes like tissue remodeling, wound healing, and angiogenesis, but its overactivity is a hallmark of pathological invasion and metastasis in various cancers [3, 9, 21]. Beyond oncology, MMP2 is heavily implicated in cardiovascular diseases such as atherosclerosis and aneurysms, where it facilitates vascular wall remodeling and plaque rupture [4, 6, 19]. Therapeutic strategies have historically focused on small-molecule hydroxamate inhibitors that chelate the catalytic zinc ion, though many failed in clinical trials due to a lack of selectivity and the resulting musculoskeletal side effects [10, 18]. Modern drug development efforts are shifting toward selective inhibitors, monoclonal antibodies, and allosteric modulators to minimize off-target toxicity while maintaining efficacy in controlling fibrosis and tumor progression [5, 7, 8].

Other names

Gelatinase A72 kDa type IV collagenase72 kDa gelatinaseTBE-1CLG4AMONA

Inhibition of proteolytic activity through zinc ion chelation, competitive binding to the catalytic active site, or allosteric modulation to prevent pro-enzyme activation