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• W2149432986 abstract "β2-Integrin adhesion molecules play crucial roles in monocyte transmigration and adherence to the inflamed extracellular matrix. While integrin engagement contributes to inflammatory cell activation, little is known about the precise signaling pathways that are important to integrin-dependent monocyte activation. We examined the role of tyrosine phosphorylation and extracellular-signal regulated kinase (ERK) activity in β2-integrin signaling in monocytes. Cross-linking of the LFA-1 (CD11a/CD18) and MAC-1 (CD11b/CD18) integrins on the surface of THP-1 monocytic cells induced the accumulation of tyrosine phosphoproteins. As part of this signal both ERK-1 and ERK-2 are tyrosine phosphorylated.In vitrokinase assays documented an increase in ERK-2 activity following both LFA-1 and MAC-1 cross-linking. β2-Integrin cross-linking also led to a marked increase in 4-h procoagulant activity (PCA) in THP-1 cells and purified human monocytes. Inhibition of tyrosine phosphorylation by genistein (10 μg/ml), or selective ERK inhibition with PD98059 (10 μM), was able to block the integrin-dependent induction of PCA in both THP-1 cells and human monocytes. Thus, β2integrin signaling in monocytic cells can flow through the tyrosine phosphorylation and activation of the ERK mitogen activated protein kinases, which is essential for the subsequent expression of tissue factor. These results suggest that the ERK proteins likely function to integrate various adhesion-dependent signals during the process of monocyte transmigration." @default.
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• W2149432986 date "1998-12-01" @default.
• W2149432986 modified "2023-10-12" @default.
• W2149432986 title "MAP-Kinase Dependent Induction of Monocytic Procoagulant Activity by β2-Integrins" @default.
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• W2149432986 doi "https://doi.org/10.1006/jsre.1998.5319" @default.
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