Premium
Interleukin‐1 signaling is dependent on free thiols
Author(s) -
Böl GabyFleur,
Tewes Frank,
BrigeliusFlohé Regina
Publication year - 1999
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520100213
Subject(s) - phenylarsine oxide , phosphorylation , signal transduction , microbiology and biotechnology , chemistry , serine , biochemistry , biology , receptor
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.