Background |
Extracellular proteases mediate the digestion of neighboring extracellular matrix components in initial tumor growth, allow desquamation of tumor cells into the surrounding environment, provide the basis for invasion of basement membranes in targeted metastatic organs and are required for release and activation of many growth and angiogenic factors. Hepsin (also known as TMPRSS1) is a type II transmembrane serine protease in mammalian cells that is highly expressed on the surface of hepatocytes. Hepsin is frequently overexpressed in several tumors, suggesting that it is a candidate protease in the invasive process and growth capacity of tumor cells. The basal promoter region of the Hepsin gene contains potential binding sites for SP1, AP2, C/EBP, LF-A1 and E box, which may be responsible for the ubiquitous expression of the protein, which shows preferential expression in liver and kidney. Hepsin is located at the plasma membrane, with its catalytic subunit (C-terminal half) at the cell surface and its N-terminus facing the cytosol. Hepsin has been shown to play a role in normal cell growth, embryogenesis, hepatocyte growth, blood coagulation and fertilization. In addition, Hepsin converts zymogen Factor VII to Factor VIIa, which is capable of initiating a coagulation pathway on the cell surface and ultimately leads to Thrombin formation. |