ABSTRACT
Heat shock protein 90 (HSP90) is involved in conformational and structural maturation of signalling molecules and transcription factors in immune reaction. HSP90 inhibitors induce immune modulation via anti-inflammatory effect, regulating humoral and cellular immune responses. Therefore, HSP90 inhibitors potentially useful target for the autoimmune disease and chronic inflammatory diseases.
Subject(s)
Autoimmune Diseases , Heat-Shock Proteins , Immunity, Cellular , Interleukin-17 , Transcription FactorsABSTRACT
In this present study, we show that 3HK-induced reactive oxygen species (ROS) accumulation and caspase activation lead to apoptotic cell death. Pretreatment with N-acetylcysteine (NAC), an effective antioxidant, significantly attenuated 3HK-induced apoptosis by way of a reduction of ROS accumulation and caspase activity. SKN-SN cells were protected from 3HK-induced cytotoxicity by heat shock protein (HSP). HSP90 effectively attenuated 3HK-mediated ROS accumulation and apoptosis. In addition, the protective effect of HSP90 was abolished by pretreatment with HSP90 anti-sense oligonucleotide, but not when pretreated with anti-senses for other HSPs. These results suggest that HSP90 protects SKN-SH cells from 3HK-induced cytotoxicity by reducing ROS levels and caspase activity.