FEBS Letters | |
Modulation of the DNA binding activity of transcription factors CREP, NFκB and HSF by H2O2 and TNFα. Differences between in vivo and in vitro effects | |
Petersen, Hilke1  Junod, Alain F1  Jornot, Lan1  | |
[1] Respiratory Division, Department of Internal Medicine, University Hospital, Geneva, Switzerland | |
关键词: Aminotriazole; Buthionine sulfoximine; Dihydrorhodamine 123; Oxidant; Endothelium; Thioredoxin; AT; aminotriazole; BSO; buthionine sulfoximine; CREP; cyclic AMP responsive element binding proteins; DHR123; dihydrorhodamine 123; HEPES; N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid; HUVEC; human umbilical vein endothelial cells; HSF; heat shock factor; NFκB; nuclear factor κB; ROI; reactive oxygen intermediates; TR; thioredoxin; TRX; thioredoxin reductase; | |
DOI : 10.1016/S0014-5793(97)01244-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Human endothelial cells exposed to H2O2 showed reduced CREP DNA binding activity, enhanced HSF activation, and no induction of NFκB binding activity. Interestingly, H2O2 was able to induce NFκB subunit p65 translocation in the nucleus. In contrast, cells exposed to TNFα showed enhanced CREP binding activity, activation of NFκB and no induction of HSE-HSF complex. Addition of H2O2, diamide and iodoacetic acid to the binding reaction mixture markedly reduced the DNA binding ability of the three transcription factors. Thus free sulfhydryls were important in DNA binding activity of CREP, NFκB and HSF, and the lack of induction of NFκB by H2O2 in intact cells was likely caused by oxidation on a thiol, and not by a deficiency in the activation pathway.
【 授权许可】
Unknown
【 预 览 】
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