P09238

The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-10, also known as Stromelysin-2, is expressed in small intestine and at lower levels in lung and heart. MMP-10 functions similarly to MMP-3 in that it can degrade Fibronectin and gelatins type I, III, IV and IV, however its action on collagens III, IV and V is very weak. Significantly, expression of MMP-10 is upregulated in ras-transformed HaCaT II-4 keratinocytes, therefore enabling the cells to undergo epithelial-to-mesenchymal transition. This evidence suggests that MMP-10, as well as other matrix metalloproteinases, may play a significant role in tumor metastasis.