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Evidence that tyrosine phosphorylation may increase tight junction permeability
J M Staddon1, K Herrenknecht, C Smales
1Eisai London Research Laboratories Ltd, University College London, UK.
Journal of Cell Science
|February 1, 1995
Summary
Tyrosine phosphorylation regulates tight junction permeability. Inhibiting tyrosine phosphatases decreased permeability and increased tyrosine phosphorylation of proteins, including beta-catenin and ZO-1, in epithelial and brain endothelial cells.
Area of Science:
- Cell Biology
- Physiology
- Biochemistry
Background:
- Tight junction (TJ) integrity is crucial for physiological and pathological processes.
- Understanding the regulation of TJ permeability is essential for various biological functions.
Purpose of the Study:
- To investigate the role of tyrosine phosphorylation in regulating TJ permeability.
- To identify specific proteins involved in TJ regulation through tyrosine phosphorylation.
Main Methods:
- Utilized Madin-Darby Canine Kidney (MDCK) epithelial cells and brain endothelial cells.
- Measured TJ permeability using transcellular electrical resistance (TER).
- Employed tyrosine phosphatase inhibitors (pervanadate and phenylarsine oxide) and immunocytochemistry.
Main Results:
- Tyrosine phosphatase inhibition decreased TER in both cell types.
- Phenylarsine oxide treatment increased tyrosine phosphorylation of beta-catenin and ZO-1.
- Tyrosine phosphorylation of junction-associated proteins was observed following inhibitor treatment.
Conclusions:
- Tight junction permeability is regulated by tyrosine phosphorylation.
- Adherens junction and tight junction proteins are implicated in this regulatory mechanism.