Plastic model of the urokinase molecule
Urokinase is an enzyme found mainly in animals and humans. This enzyme regulates the degradation of blood clots in blood vessels. Urokinase is used as a thrombolytic agent in the treatment of heart attacks, pulmonary embolism and other disorders (it is commercially available as Abbokinase) [1]. Urokinase is a member of the family of serine proteases. The main function of urokinase is the conversion of plasminogen into plasmin, which plays a crucial role in the degradation of blood clots [2].
Mature urokinase consists of two polypeptide chains bound together with disulphide bonds. The protein consists of 3 different domains, a protease domain on one chain, and a kringle and EGF-like domain on the other chain. The kringle and EGF-like domains are needed for the interaction of the protein with blood-clotting factors and the release of the protein from the cell, respectively [3][4]. Interestingly, the expression level of urokinase appears to correlate with the process of tumor expansion [5]. The high activity of the urokinase enzyme is considered to lead to degradation of the extracellular matrix and the formation of metastases [6], which suggests that urokinase could be a potential target for cancer therapy [7].
Cast
- Molecular-modeller:
- Ivan Konstantinov
- Technologist:
- Artem Sokolov
Date: Dec 19, 2011
References
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