Stromelysin-1/MMP-3 Protein, Human

Stromelysin-1/MMP-3, a metalloproteinase, exhibits a broad substrate specificity, capable of degrading various components of the extracellular matrix (ECM) such as fibronectin, laminin, gelatins (type I, III, IV, and V), collagens (III, IV, X, and IX), and cartilage proteoglycans. This enzyme plays a pivotal role in activating different molecules, including growth factors, plasminogen, or other matrix metalloproteinases like MMP9. Upon release into the ECM, the inactive pro-enzyme undergoes activation through the plasmin cascade signaling pathway. Stromelysin-1/MMP-3 also functions intracellularly, as observed in dopaminergic neurons where it becomes activated by the serine protease HTRA2 during stress, contributing to dopamine neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage. Additionally, this metalloproteinase plays a role in immune response and exhibits antiviral activity against various viruses, including vesicular stomatitis virus, influenza A virus (H1N1), and human herpes virus 1. Mechanistically, it translocates from the cytoplasm into the cell nucleus upon virus infection to modulate NF-kappa-B activities.