Premium
Trichostatin A Inhibits LPS‐induced Cyclooxygenase 2 Expression Through Inhibition of C/EBPδ Gene Expression in RAW264.7 Cells
Author(s) -
Hung JanJong
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.878.4
Subject(s) - trichostatin a , psychological repression , chemistry , mapk/erk pathway , p38 mitogen activated protein kinases , c jun , microbiology and biotechnology , phosphorylation , cyclooxygenase , histone deacetylase , gene expression , histone , transcription factor , gene , biology , enzyme , biochemistry
Cyclooxygenase 2 (COX‐2) is an important inflammatory factor. Previous studies have indicated that COX‐2 could be induced under LPS treatment, and could be inhibited by trichostatin A (TSA). Our previous research reveals that C/EBPδ induced by LPS is through the activation of the pathway of ERK/JNK1/2/p38 and NF‐κB, followed by the recruitment of c‐Rel and c‐Jun to the C/EBPδ promoter. Herein we found trichostatin A (TSA) could inhibit LPS‐induced Cox‐2 gene expression is due to the inhibition of C/EBPδ. Furthermore, the inhibition of C/EBPδ was through preventing c‐Jun recruitment by Sp1 to the C/EBPδ promoter, but not due to the repression of ERK or NF‐κB pathway. In addition, we also found that the interaction of Sp1 and c‐Jun was inhibited under TSA treatment. At last, it is interesting that c‐terminus of c‐Jun was phosphorylated under TSA treatment. To detect the level of PP2B under TSA treatment found that the level of PP2B was reduced. Taken together, inhibition of LPS‐induced COX‐2 by TSA was due to repression of C/EBPδ, and C/EBPδ down‐regulation was through the inhibition of PP2B led the highly phosphorylation at c‐terminus of to repress the interaction of c‐Jun and Sp1.