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Receptor for plasmin on human carcinoma cells
1Laboratoire d'Immunochimie, Centre National de la Recherche Scientifique, Villejuif, France.
Journal of the National Cancer Institute
|July 20, 1988
Summary
Human tumor cells bind plasminogen and plasmin via specific receptors. Urokinase enhances plasminogen binding, suggesting a mechanism for localized plasmin generation on tumor surfaces.
Area of Science:
- Biochemistry
- Cell Biology
- Oncology
Background:
- Plasmin and plasminogen play roles in tumor cell invasion and metastasis.
- Tumor cells may express specific receptors to interact with the fibrinolytic system.
Purpose of the Study:
- To investigate the presence and characteristics of plasmin and plasminogen receptors on human tumor cells.
- To explore the role of urokinase in modulating plasminogen binding to tumor cells.
Main Methods:
- Utilized human tumor cell line SW 1116.
- Performed binding assays to determine receptor affinity for plasmin and plasminogen.
- Investigated the effect of urokinase and anti-urokinase serum on plasminogen binding.
Main Results:
- SW 1116 cells possess receptors for both plasmin and plasminogen.
- Receptors exhibit higher affinity for plasmin (Kd = 6 x 10^-8 M) than plasminogen (Kd = 5 x 10^-6 M).
- Urokinase significantly increased plasminogen binding, while anti-urokinase serum inhibited it.
Conclusions:
- Tumor cells bind plasminogen and plasmin through shared receptors.
- Urokinase on tumor cell surfaces likely facilitates plasminogen conversion to active plasmin.
- Bound plasmin retains enzymatic activity, indicating the active site is not involved in binding.