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• W4313333770 abstract "Abstract We investigated the mechanisms by which proinflammatory mediator, thrombin, released during intravascular coagulation and tissue injury, induces ICAM-1 (CD54) expression in endothelial cells. Stimulation of HUVEC with thrombin resulted in dose- and time-dependent increases in ICAM-1 mRNA and cell surface expression and in ICAM-1-dependent endothelial adhesivity toward polymorphonuclear leukocytes. Transient transfection of endothelial cells with ICAM-1 promoter luciferase reporter gene (ICAM-1LUC) constructs indicated that deletion of upstream NF-κB site (−533 bases from translation start site) had no effect on thrombin responsiveness, whereas mutation/deletion of downstream NF-κB site (−223 bases from the translation start site) prevented the activation of ICAM-1 promoter, indicating that the downstream NF-κB site is critical for thrombin inducibility. NF-κB-directed luciferase activity increased ∼3-fold when cells transfected with the plasmid pNF-κBLUC containing five copies of consensus NF-κB site linked to a minimal adenovirus E1B promoter-luciferase gene were exposed to thrombin, indicating that activation of NF-κB was essential for thrombin response. Gel supershift assays demonstrated that thrombin induced binding of NF-κBp65 (Rel A) to downstream NF-κB site of the ICAM-1 promoter. Thrombin receptor activation peptide, a 14-amino-acid peptide representing the new NH2 terminus of proteolytically activated receptor-1, mimicked thrombin’s action in inducing ICAM-1 expression. These data indicate that thrombin activates endothelial ICAM-1 expression and polymorphonuclear leukocyte adhesion by NF-κBp65 binding to the downstream NF-κB site of ICAM-1 promoter after proteolytically activated receptor-1 activation." @default.
• W4313333770 created "2023-01-06" @default.
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• W4313333770 date "1999-05-01" @default.
• W4313333770 modified "2023-10-16" @default.
• W4313333770 title "Thrombin-Induced p65 Homodimer Binding to Downstream NF-κB Site of the Promoter Mediates Endothelial ICAM-1 Expression and Neutrophil Adhesion" @default.
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• W4313333770 doi "https://doi.org/10.4049/jimmunol.162.9.5466" @default.
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