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Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes.

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Stoppelli, M P, Corti, A, Soffientini, A, Cassani, G, Blasi, F, Assoian, R K·1985·Proceedings of the National Academy of Sciences

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.

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Metadata

Authors
Stoppelli, M. P., Corti, A., Soffientini, A., Cassani, G., Blasi, F., & Assoian, R. K.
Venue
Proceedings of the National Academy of Sciences
Published
1985-08
Volume
82
Issue
15
Pages
4939-4943
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2115947409
Cited by
443
References
0
FWCI
13.51
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. https://app.cochat.ai/papers/10.1073/pnas.82.15.4939
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Stoppelli, M. P., Corti, A., Soffientini, A., Cassani, G., Blasi, F., & Assoian, R. K. (1985). Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.15.4939

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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