TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Jin, Wen
A1  - Bernhardt, Rita
A1  - Lehmann, Claudia
A1  - Stöcklein, Walter F. M.
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Funktionalisierung von Elektroden für den direkten heterogenen Elektrotransfer
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Song, Hui
A1  - Bergstrasser, Claudia
A1  - Rafat, Neysan
A1  - Hoeger, Simone
A1  - Schmidt, Marc
A1  - Endres, N.
A1  - Goebeler, Matthias
A1  - Hillebrands, Jan-Luuk
A1  - Brigelius-Flohé, Regina
A1  - Banning, Antje
A1  - Beck, Grietje
A1  - Loesel, Ralf
A1  - Yard, Benito A.
T1  - The carbon monoxide releasing molecule (CORM-3) inhibits expression of vascular cell adhesion molecule-1 and E- selectin independently of haem oxygenase-1 expression
N2  - Background and purpose: Although carbon monoxide (CO) can modulate inflammatory processes, the influence of CO on adhesion molecules is less clear. This might be due to the limited amount of CO generated by haem degradation. We therefore tested the ability of a CO releasing molecule (CORM-3), used in supra-physiological concentrations, to modulate the expression of vascular cell adhesion molecule (VCAM)-1 and E-selectin on endothelial cells and the mechanism(s) involved. Experimental approach: Human umbilical vein endothelial cells (HUVECs) were stimulated with tumour necrosis factor (TNF)-alpha in the presence or absence of CORM-3. The influence of CORM-3 on VCAM-1 and E- selectin expression and the nuclear factor (NF)-kappa B pathway was assessed by flow cytometry, Western blotting and electrophoretic mobility shift assay. Key results: CORM-3 inhibited the expression of VCAM-1 and E-selectin on TNF-alpha- stimulated HUVEC. VCAM-1 expression was also inhibited when CORM-3 was added 24 h after TNF-alpha stimulation or when TNF-alpha was removed. This was paralleled by deactivation of NF-kappa B and a reduction in VCAM-1 mRNA. Although TNF- alpha removal was more effective in this regard, VCAM-1 protein was down-regulated more rapidly when CORM-3 was added. CORM-3 induced haem oxygenase-1 (HO-1) in a dose- and time-dependent manner, mediated by the transcription factor, Nrf2. CORM-3 was still able to down-regulate VCAM-1 expression in HUVEC transfected with siRNA for HO-1 or Nrf2. Conclusions and implications: Down-regulation of VCAM and E-selectin expression induced by CORM-3 was independent of HO-1 up- regulation and was predominantly due to inhibition of sustained NF-kappa B activation.
Y1  - 2009
UR  - http://www3.interscience.wiley.com/journal/121548564/home
U6  - https://doi.org/10.1111/j.1476-5381.2009.00215.x
SN  - 0007-1188
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Utepbergenov, D.
A1  - Haseloff, R. F.
A1  - Blasig, Ingolf E.
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
A1  - Brigelius-Flohé, Regina
T1  - An optical method for the detection of oxidative stress using protein-RNA interaction
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by a selenoenzyme
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Böl, Gaby Fleur
A1  - Jurrmann, Nadine
A1  - Brigelius-Flohé, Regina
T1  - Cellular trafficking of the IL-1RI-associated kinase-1 requires intact kinase activity
N2  - Upon stimulation of cells with interleukin-1 (IL-1) the IL-1 receptor type 1 (IL-1RI) associated kinase-1 (IRAK- 1) transiently associates to and dissociates front the IL-IRI and thereafter translocates into the nucleus. Here we show that nuclear translocation of IRAK-I depends on its kinase activity since translocation was not observed in EL-4 cells overexpressing a kinase negative IRAK-1 mutant (EL-4(IRAK-1-K239S)). IRAK-1 itself, an endogenous substrate with an apparent molecular weight of 24 kDa (p24). and exogenous substrates like histone and myelin basic protein are phosphorylated by nuclear located IRAK-1. Phosphorylation of p24 cannot be detected in EL-4(IRAK-1-K239S) cells. IL-1- dependent recruitment of IRAK-1 to the IL-1RI and subsequent phosphorylation of IRAK-l is a prerequisite for nuclear translocation of IRAK-1. It is therefore concluded that intracellular localization of IRAK-1 depends on its kinase activity and that IRAK-1 may also function as a kinase in the nucleus as shown by a new putative endogenous substrate. (c) 2005 Elsevier Inc. All rights reserved
Y1  - 2005
SN  - 0006-291X
ER  -