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Intracellular redox regulation by a cystine derivative suppresses UV‐induced NF‐κB activation
Author(s) -
Kitazawa Manabu,
Nakano Takashi,
Chuujou Hiromi,
Shiojiri Eiji,
Iwasaki Keiji,
Sakamoto Kazutami
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03152-6
Subject(s) - intracellular , redox , chemistry , oxidative stress , cystine , cysteine , dna , glutathione , nf κb , nfkb1 , dna damage , biochemistry , signal transduction , transcription factor , enzyme , organic chemistry , gene
Nuclear factor (NF)‐κB pathways are influenced by the intracellular reduction–oxidation (redox) balance. While NF‐κB is activated through inhibitor (I)‐κB degradation by oxidative stress, its DNA binding is accelerated in the reduced state. We found that N , N ′‐diacetyl‐ L ‐cystine dimethylester (DACDM) suppressed the UVB‐induced NF‐κB binding activity at a much lower concentration (50–100 μM) than N ‐acetyl‐ L ‐cysteine (NAC, 10–30 mM). While NAC suppressed the I‐κB degradation but not the DNA binding, DACDM prevented the activated NF‐κB from binding DNA, without influencing the I‐κB degradation. These properties of DACDM make it possible to effectively regulate the intracellular redox balance.