Cryptic urokinase binding sites on human foreskin fibroblasts |
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| Authors: | A Bajpai J B Baker |
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| Affiliation: | 1. Institute for Advanced Materials and Technology, University of Science and Technology Beijing, Beijing, 100083, China;2. Beijing Key Laboratory for Advanced Powder Metallurgy and Particulate Materials, University of Science and Technology Beijing, Beijing, 100083, China;3. Beijing Laboratory of Metallic Materials and Processing for Modern Transportation, University of Science and Technology Beijing, Beijing, 100083, China;4. School of Chemical Engineering, The University of Queensland, Brisbane, QLD, 4072, Australia;5. The State Key Laboratory for Advanced Metals and Materials, University of Science and Technology Beijing, Beijing, 100083, China;1. Providence College, 259 Arthur and Patricia Ryan Center, 1 Cunningham Square, Providence, RI, United States;2. Providence College, 249 Arthur and Patricia Ryan Center, 1 Cunningham Square, Providence, RI, United States;3. Department of Marketing, The University of Alabama, 123 Alston Hall, Box 870225, Tuscaloosa, AL 35406, United States |
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| Abstract: | Human foreskin cells possess sites on their surfaces that specifically bind both active and diisopropylphosphofluoridate-inactivated 2 chain 54 K Da [125I]-urokinase, but do not bind the 54 K Da single chain form of urokinase. 125I-urokinase bound to these sites is not internalized and is very slow to dissociate. There are about 40,000 available binding sites per cell. Brief incubation with pH 2.5 buffer at 5 degrees C unmasks another two to six fold more sites and also extracts plasminogen activator that, based on its accessibility to trypsin, appears to be at the cell surface. This suggests that the cryptic urokinase binding sites could be sites occupied with endogenous plasminogen activator. |
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