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IκBL, a novel member of the nuclear IκB family, inhibits inflammatory cytokine expression
Author(s) -
Chiba Tomoki,
Miyashita Keiko,
Sugoh Tatsuya,
Warita Takayuki,
Inoko Hidetoshi,
Kimura Minoru,
Sato Takehito
Publication year - 2011
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/j.febslet.2011.10.024
Subject(s) - gene isoform , nuclear localization sequence , alternative splicing , cell nucleus , ankyrin repeat , rna splicing , arthritis , transcription factor , cytokine , nf κb , nuclear protein , signal transduction , microbiology and biotechnology , nucleus , transcription (linguistics) , chemistry , biology , immunology , genetics , gene , rna , linguistics , philosophy
We previously reported that IκBL prevents experimental autoimmune arthritis. The molecular mechanism, however, still remains unclear. In contrast to four splicing‐isoforms of IκBL in human, two isoforms were identified in mouse. The major isoform IκBL‐α(S) suppressed LPS‐induced NF‐κB activation and transcription of TNFα and IL‐6, but not IL‐1β. The suppressive activity required the nuclear localization signal and the ankyrin repeat domain of IκBL. IκBL did not affect the nuclear translocation of the NF‐κB dimer. These findings point to IκBL as being a novel member of the nuclear IκB family, which functions in the nucleus and controls various inflammatory responses including autoimmune arthritis.