Many different processes in the physiology and pathophysiology of human beings are regulated protein/protein interactions such as receptor/ligand interactions. A more detailed knowledge of the nature of receptor/ligand binding sites and mechanisms of interaction is necessary as well in order to understand the process of cancer spread and metastasis. For instance, the cell surface receptor uPAR (CD87) and its ligand, the serine protease urokinase-type plasminogen activator (uPA), facilitate tumor invasion and metastasis in solid malignant tumors.
View Article and Find Full Text PDFThe urokinase-type plasminogen activation system, including the serine protease uPA (urokinase-type plasminogen activator) and its cell surface receptor (uPAR, CD87), are important key molecules in tumor invasion and metastasis. Besides its proteolytic function, binding of uPA to uPAR on tumor cells exerts various cell responses such as migration, adhesion, proliferation, and differentiation. Hence, the uPA/uPAR system is a potential target for tumor therapy.
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