Interleukin‐1 signaling is dependent on free thiols

Article type: Research Article

Authors: Böl, Gaby‐Fleur^; | Tewes, Frank^; | Brigelius‐Flohé, Regina^;

Affiliations: German Institute of Human Nutrition, Potsdam‐Rehbrücke, Germany | Institute of Nutritional Science, University of Potsdam, Germany

Note: [] Address correspondence to: Gaby‐Fleur Böl, German Institute of Human Nutrition, Department of Vitamins and Atherosclerosis, Arthur‐Scheunert‐Allee 114‐116, D‐14558 Potsdam‐Rehbrücke, Germany. Fax: +49 33200 88 419; E‐mail: boel@ www.dife.de.

Abstract: 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 NF\kappaB 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.

Journal: Biofactors, vol. 10, no. 2-3, pp. 175-178, 1999