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Journal Article

Protein kinase C-mediated endothelial barrier regulation is caveolin-1-dependent

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Kurzchalia,  Teymuras V
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Waschke, J., Golenhofen, N., Kurzchalia, T. V., & Drenckhahn, D. (2006). Protein kinase C-mediated endothelial barrier regulation is caveolin-1-dependent. Histochem Cell Biol, 126(1), 17-26.


Cite as: https://hdl.handle.net/21.11116/0000-0001-1092-7
Abstract
Protein kinase C (PKC) is activated in response to various inflammatory mediators and contributes significantly to the endothelial barrier breakdown. However, the mechanisms underlying PKC-mediated permeability regulation are not well understood. We prepared microvascular myocardial endothelial cells from both wild-type (WT) and caveolin-1-deficient mice. Activation of PKC by phorbol myristate acetate (PMA) (100 nM) for 30 min induced intercellular gap formation and fragmentation of VE-cadherin immunoreactivity in WT but not in caveolin-1-deficient monolayers. To test the effect of PKC activation on VE-cadherin-mediated adhesion, we allowed VE-cadherin-coated microbeads to bind to the endothelial cell surface and probed their adhesion by laser tweezers. PMA significantly reduced bead binding to 78+/-6% of controls in WT endothelial cells without any effect in caveolin-1-deficient cells. In WT cells, PMA caused an 86+/-18% increase in FITC-dextran permeability whereas no increase in permeability was observed in caveolin-1-deficient monolayers. Inhibition of PKC by staurosporine (50 nM, 30 min) did not affect barrier functions in both WT and caveolin-1-deficient MyEnd cells. Theses data indicate that PKC activation reduces endothelial barrier functions at least in part by the reduction of VE-cadherin-mediated adhesion and demonstrate that PKC-mediated permeability regulation depends on caveolin-1.