Abstract
Histone Deacetylase Inhibitor Trichostatin A Sustains Sodium Pervanadate-induced NF-κB Activation by Delaying IκBα mRNA Resynthesis
Highlights
nuclear factor (NF)-B is a crucial transcription factor tightly regulated by protein interactions and post-translational modifications, like phosphorylation and acetylation
We compared the influence of trichostatin A (TSA), a large spectrum histone deacetylase inhibitor, on two different NF-B activation pathways: (i) the atypical pathway involving multiple tyrosine kinases mediated either by PV or hydrogen peroxide (H2O2), and (ii) the classical pathway induced either by the pro-inflammatory cytokine tumor necrosis factor (TNF)␣ or the phorbol ester PMA
Influence of histone deacetylases (HDAC) Inhibitor on NF-B Activation, and the Associated IB␣ Degradation, Induced by Various Inducers—We investigated the kinetics of NF-B activation elicited by four inducers (PV, TNF␣, PMA, and H2O2) in the presence or absence of an HDAC inhibitor, TSA or suberoylanilide hydroxamic acid (SAHA), in two cell types, HeLa cells or Jurkat T cells
Summary
NF-B is a crucial transcription factor tightly regulated by protein interactions and post-translational modifications, like phosphorylation and acetylation. TSA addition on PV inducsion induced by co-stimulation of PV and TSA is likely due to, at tion does not influence global ERK and p38 MAPK activation least in part, a delay of RNA Pol II recruitment and histone H3 acetylation on Lys14 and phosphorylation on Ser10.
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