Abstract
Heat shock proteins (HSP) are a family of ubiquitous and phylogenically highly conserved proteins which play an essential role as molecular chaperones in protein folding and transport. Heat Shock Protein 90 (Hsp90) is not mandatory for the biogenesis of most proteins, rather it participate in structural maturation and conformational regulation of a number of signaling molecules and transcription factors. Hsp90 has been shown to play an important role in antigen presentation, activation of lymphocytes, macrophages, maturation of dendritic cells, and in the enhanceosome mediated induction of inflammation. Systemic lupus erythematosus (SLE) is a chronic autoimmune inflammatory disease with complex immunological and clinical manifestations. Dysregulated expression of Type I interferon α, activation of B cells and production of autoantibodies are hallmarks of SLE. The enhanced levels of Hsp90 were detected in the serum of SLE patients. The elevated level of Hsp90 in SLE has also been correlated with increased levels of IL-6 and presence of autoantibodies to Hsp90. This suggests that Hsp90 may contribute to the inflammation and disease progression and that targeting of Hsp 90 expression may be a potential treatment of SLE. The pharmacologic inhibition of Hsp90 was successfully applied in mouse models of autoimmune encephalomyelitis and SLE—like autoimmune diseases. Thus targeting Hsp90 may be an effective treatment for SLE, especially if combined with other targeted therapeutic approaches.
Highlights
Heat shock proteins (HSPs) are a family of ubiquitous and phylogenically highly conserved proteins and play an essential role as molecular chaperones in protein folding and transport within the cell [1]. These proteins are named according to their molecular weight, which ranges from 17 kDa small HSP families to more than 100 kDa, and they are classified into six families, namely, the HSP100, HSP90, HSP70, HSP60, and HSP40
Using the nomenclature adopted after the Cold Spring Harbor Meeting of 1996 [2], family names are written in capitals, for example, HSP70
HSPs are regarded as intracellular molecules; upon necrotic, but not apoptotic, cell death, HSPs are released into the extracellular compartments [7]
Summary
Heat shock proteins (HSPs) are a family of ubiquitous and phylogenically highly conserved proteins and play an essential role as molecular chaperones in protein folding and transport within the cell [1]. HSPs are present in circulation of normal individuals [10], and their circulating levels are decreased in aging [11], and increased in a number of pathological conditions [12] Their increased expression in tissues that are subjected to various proteotoxic stressors (including heat, heavy metals, hypoxia, and acidosis) is an adaptive response that enhances cell survival. The HSF2 has been shown to be bound to the HSE promoter elements of other heat-shock genes, including Hsp and Hsp, as well as the protooncogene c-Fos [19] These data suggest that HSF2 is important for constitutive as well as stress-inducible expression of HSE-containing genes
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