Histone acetylation regulated by histone acetyltransferases (HATs) and histone 
deacetylases (HDACs) plays a critical role in the expression of inflammatory 
genes, such as vascular cell adhesion molecule-1 (VCAM-1). Oxidative processes 
have been shown to induce VCAM-1 expression. Here, we investigated the 
mechanisms underlying IL-1beta-induced VCAM-1 expression in human tracheal 
smooth muscle cells (HTSMCs). Our results showed that IL-1beta enhanced 
HTSMCs-monocyte adhesion through up-regulation of VCAM-1, which was inhibited by 
pretreatment with selective inhibitors of PKCalpha (Gö6976), c-Src (PP1), NADPH 
oxidase [diphenylene iodonium (DPI) and apocynin (APO)], intracellular calcium 
chelator (BAPTA/AM), PI-PLC (U73122), CaM (calmidazolium chloride), CaM kinase 
II (KN62), p300 (garcinol), NF-kappaB (Bay11-7082), HDAC (trichostatin A), and 
ROS scavenger [N-acetyl-L-cysteine (NAC)] or transfection with siRNAs of MyD88, 
PKCalpha, Src, p47(phox), p300, and HDAC4. Moreover, IL-1beta stimulated 
NF-kappaB and CaMKII phosphorylation through MyD88-dependent 
PI-PLC/PKCalpha/c-Src/ROS and PI-PLC/Ca2+/CaM pathways, respectively. Activation 
of NF-kappaB and CaMKII may eventually lead to the acetylation of histone 
residues and phosphorylation of histone deacetylases. These findings suggested 
that IL-1beta induced VCAM-1 expression via these multiple signaling pathways in 
HTSMCs. Blockade of these pathways may reduce monocyte adhesion via VCAM-1 
suppression and attenuation of the inflammatory responses in airway diseases.