Matrix Metalloproteinase-3 (MMP-3), also known as Stromelysin-1, is an enzyme that plays a crucial role in the degradation of extracellular matrix (ECM) components. This enzyme is part of the matrix metalloproteinase (MMP) family, which is involved in various physiological and pathological processes, including tissue remodeling, wound healing, and cancer metastasis .
MMP-3 is encoded by the MMP3 gene located on chromosome 11q22.3 . The enzyme has an estimated molecular weight of 54 kDa . MMP-3 can degrade multiple ECM components such as proteoglycans, fibronectin, laminin, and type IV collagen . It also activates other pro-MMPs, initiating a cascade of MMP-mediated degradation reactions .
The human recombinant form of MMP-3 is produced using recombinant DNA technology. This involves inserting the MMP3 gene into a suitable expression system, such as E. coli or HEK293 cells, to produce the enzyme in large quantities . The recombinant enzyme is often tagged with Glutathione S-transferase (GST) to facilitate purification and detection. The GST tag allows the enzyme to be purified using affinity chromatography, which is a highly efficient method for isolating recombinant proteins .
Recombinant MMP-3 is widely used in research to study its role in various biological processes and diseases. It is used to investigate the mechanisms of ECM degradation, tissue remodeling, and the activation of other MMPs. Additionally, MMP-3 is studied for its potential therapeutic applications in conditions such as arthritis, cancer, and cardiovascular diseases .