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Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes
- Source :
- Proceedings of the National Academy of Sciences. 82:4939-4943
- Publication Year :
- 1985
- Publisher :
- Proceedings of the National Academy of Sciences, 1985.
-
Abstract
- The purified amino-terminal fragment (ATF) of human urokinase plasminogen activator (residues 1-135), which is not required for activation of plasminogen, binds with high affinity to specific plasma membrane receptors on U937 monocytes. Intact urokinase efficiently competes for 125I-labeled ATF binding; 50% competition occurs with 1 nM urokinase. A large part of receptor-bound urokinase remains on the cell surface for at least 2 hr at 37 degrees C. Differentiation of U937 monocytes into macrophage-like cells specifically increases ATF binding 10- to 20-fold. These results suggest an important role for urokinase in monocyte/macrophage biology: the native enzyme binds to the cells with the amino-terminal domain; the catalytic, carboxyl-terminal domain remains exposed on the cell surface to stimulate localized proteolysis and facilitate cell migration.
- Subjects :
- Cellular differentiation
Receptors, Cell Surface
Biology
Binding, Competitive
Monocytes
Receptors, Urokinase Plasminogen Activator
Cell membrane
Cell surface receptor
medicine
Humans
Amino Acid Sequence
Receptor
Urokinase
Multidisciplinary
Macrophages
Monocyte
Cell Membrane
Cell Differentiation
Cell migration
Urokinase-Type Plasminogen Activator
Molecular biology
Peptide Fragments
Urokinase receptor
medicine.anatomical_structure
Tetradecanoylphorbol Acetate
Research Article
medicine.drug
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 82
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....adf11e25cdf1f4d7c865bd850fa210eb