Abstract
Heat shock protein 90 (HSP90) is a molecular chaperone that folds and promotes the activity of a wide range of client proteins, including key signaling proinflammatory molecules involved in aberrant inflammation. RGRN-305 is a novel HSP90 inhibitor that has been reported to exhibit antiinflammatory properties in autoimmune skin diseases. Here, the antiinflammatory effects of RGRN-305 were investigated in vitro and in a mouse model in vivo. In primary human keratinocytes stimulated with 12-O-tetradecanoylphorbol-13-acetate (TPA; inducer of inflammation), the mRNA expression of the proinflammatory cytokines TNFα, IL-1β, IL-6 and IL-8 were significantly reduced by preincubation with RGRN-305, when measured by quantitative real-time PCR.
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