Extracellular matrix-degrading enzyme

Extracellular matrix-degrading enzymes are a diverse group of proteins responsible for the proteolytic breakdown of components of the extracellular matrix (ECM), including collagens, elastin, fibronectin, laminin, and proteoglycans[2][3][4]. Major classes include **matrix metalloproteinases (MMPs)**, **a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)**, serine proteases (e.g. plasmin), and certain cysteine proteases. These enzymes are critical mediators of tissue remodeling, wound healing, immune cell migration, inflammatory responses, and cancer progression due to their ability to modify ECM architecture and bioavailability of signaling molecules[2][3][4][5]. Dysregulation or overexpression of these enzymes is implicated in a range of pathologies, notably cancer metastasis, chronic inflammation, and fibrosis[5]. They are considered therapeutic targets, and several broad-spectrum and specific inhibitors have been investigated, though clinical utility has been limited by safety and specificity concerns[3][4]. Note: This entry is flagged as **is_incorrect: true** because "extracellular matrix-degrading enzymes" refers to a broad class or functional group of targets, not one molecular entity. For structured data, it is preferable to use entries such as "Matrix metalloproteinase 9" or "A disintegrin and metalloproteinase with thrombospondin motifs 4" for specificity.

Other names

Matrix-degrading enzymeECM-degrading enzymeMatrix metalloproteinase (for MMPs)ADAMTS proteasePlasmin (for specific enzymes in this group)Protease (general)MetalloproteinaseProteinase

Inhibition of enzyme catalytic activity (prevents ECM breakdown), Chelation of zinc (for metalloproteinases)