Abstract
Hsp90 is the most studied member of the family of heat shock proteins (Hsps), which are characterized by induction by increased temperature and various other types of stress. It is a highly conserved molecular chaperone that plays a significant role in many cellular processes.
Hsp90 is required for the proper conformation and activation of a number of client cellular proteins, including protein kinases, transcription factors and steroid receptors that play an important role in signal transduction. It also regulates activation of innate immunity, antigen presentation, and the induction of proinflammatory cytokines and chemokines by macrophages and dendritic cells.
These properties predispose Hsp90 to a potential role in the pathogenesis of autoimmune inflammatory rheumatic diseases. This article provides an overview of the available knowledge about the potential role of Hsp90 in currently studied rheumatic diseases as a promising candidate for targeted therapy or biomarker of disease activity and severity or a predictor of therapeutic response.