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• W2034954165 abstract "Abstract Endothelial cell leakiness is regulated by mediators such as thrombin, which promotes endothelial permeability, and anti-inflammatory agents, such as angiopoietin-1. Here we define a new pathway involved in thrombin-induced permeability that involves the atypical protein kinase C isoform, PKCζ. Chemical inhibitor studies implicated the involvement of an atypical PKC isoform in thrombin-induced permeability changes in human umbilical vein endothelial cells. Thrombin stimulation resulted in PKCζ, but not the other atypical PKC isoform, PKCλ, translocating to the membrane, an event known to be critical to enzyme activation. The involvement of PKCζ was confirmed by overexpression of constitutively active PKCζ, resulting in enhanced basal permeability. Dominant-negative PKCζ prevented the thrombin-mediated effects on endothelial cell permeability and inhibited thrombin-induced activation of PKCζ. Rho activation does not appear to play a role, either upstream or downstream of PKCζ, as C3 transferase does not block thrombin-induced PKCζ activation and dominant-negative PKCζ does not block thrombin-induced Rho activation. Finally, we show that angiopoietin-1 inhibits thrombin-induced PKCζ activation, Rho activation, and Ca++ flux, thus demonstrating that the powerful antipermeability action of angiopoietin-1 is mediated by its action on a number of signaling pathways induced by thrombin and implicated in permeability changes. (Blood. 2004; 104:1716-1724)" @default.
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• W2034954165 date "2004-09-15" @default.
• W2034954165 modified "2023-10-16" @default.
• W2034954165 title "Role of protein kinase Cζ in thrombin-induced endothelial permeability changes: inhibition by angiopoietin-1" @default.
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• W2034954165 doi "https://doi.org/10.1182/blood-2003-11-3744" @default.
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