Matrix metalloproteinase (MMP) (MMP)

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases responsible for the degradation and remodeling of extracellular matrix (ECM) components, such as collagen, elastin, and fibronectin (UniProt, 2024). They play critical roles in normal physiological processes including wound healing, angiogenesis, and embryonic development (PubMed, PMID: 12191120). However, dysregulated MMP activity is a hallmark of various pathologies, particularly cancer metastasis, where they facilitate tumor cell invasion, and chronic inflammatory diseases like rheumatoid arthritis and osteoarthritis (StatPearls, 2023). In the pharmaceutical industry, MMPs have been targeted primarily with small-molecule inhibitors designed to bind the catalytic zinc ion (NIH, 2022). While early clinical trials faced challenges due to dose-limiting musculoskeletal toxicity and lack of isoform selectivity, modern approaches focus on developing highly specific inhibitors or monoclonal antibodies to target individual MMPs involved in specific disease pathways (Nature Reviews Drug Discovery, 2002).

Other names

MatrixinCollagenaseGelatinaseStromelysinMatrilysinMetalloendopeptidase

Inhibition of the catalytic zinc-dependent active site to prevent the proteolytic cleavage of extracellular matrix proteins and other bioactive substrates (PubMed, PMID: 17076523).