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Urokinase as a multidomain protein and polyfunctional cell regulator
1Russian Cardiology Research Center, Ministry of Health of Russian Federation, Cherepovskaya ul. 15, Moscow, 121552, Russia. V.Stepanova@cardio.ru
Biochemistry. Biokhimiia
|February 14, 2002
Summary
Urokinase type plasminogen activator (urokinase) regulates cell adhesion and migration by cleaving plasminogen and activating cell surface receptors. This review explores its structure-function relationships and signaling mechanisms in tissue remodeling.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Urokinase type plasminogen activator (urokinase) is crucial for tissue remodeling.
- It regulates cell adhesion and migration.
- Urokinase possesses multifaceted functions beyond plasminogen activation.
Purpose of the Study:
- To review the functional properties of urokinase.
- To examine urokinase fragments generated during cell surface processing.
- To discuss urokinase-mediated cellular regulation via membrane receptors.
Main Methods:
- Literature review of urokinase function.
- Analysis of urokinase structure-domain relationships.
- Examination of urokinase-receptor interactions and signaling.
Main Results:
- Urokinase's three domains (proteolytic, kringle, EGF-homologous) dictate its functions.
- Proteolytic processing on cell surfaces generates active fragments.
- Urokinase binding to cell surface receptors triggers intracellular signaling.
Conclusions:
- Urokinase is a key regulator of cell behavior in tissue remodeling.
- Its domain structure and proteolytic processing are critical for its diverse roles.
- Understanding urokinase-receptor interactions provides insights into cellular regulation.