vitamin-k-semiquinone-radical and oxophenylarsine

Stimulation of the Interleukin-1 receptor type I (IL-1-RI) with IL-1 activates an associated serine/threonine kinase, IRAK, which phosphorylates downstream targets, resulting in NFkappaB activation. The signaling cascade is accompanied by oxidative processes and contains putative targets for redox regulation. Preincubation of the murine T cell line EL-4 and the human umbilical cord vein endothelial cell line ECV 304 with thiol modifying compounds like diamide, menadione or phenylarsine oxide inhibited the IL-1-induced phosphorylation of an endogenous substrate with a molecular mass of 60 kD. In the endothelial cell line, a second target of about 85 kD was phosphorylated after IL-1 stimulation, which was also inhibited by thiol modification. These data suggest that IL-1 signal transduction depends on free thiols which might be targets for redox regulation not only in lymphocytes, but also in endothelial cells.

Topics: Animals; Arsenicals; Cells, Cultured; Diamide; Endothelium, Vascular; Enzyme Inhibitors; Humans; Interleukin-1; Mice; Molecular Weight; NF-kappa B; Oxidation-Reduction; Phosphorylation; Receptors, Interleukin-1; Receptors, Interleukin-1 Type I; Signal Transduction; Sulfhydryl Compounds; Thymoma; Thymus Neoplasms; Tumor Cells, Cultured; Umbilical Veins; Vitamin K