Role of Heat Shock Protein 90 in the Cause of Various Diseases: A Potential Therapeutic Target

Abstract

AbstractDifferent classes of Heat shock proteins (HSP) play a diverse role in influencing proper assembly, folding, and translocation of cellular proteins. HSP90 is one such kind of molecular chaperone which has been implicated the formation of number of diseases like cancer and various kinds of neurodegenerations. The chaperone, HSP90 assists in folding, maturation and maintains the functional stability of many proteins that includes many oncoproteins like p53 as well as neuronal proteins like tau. It also regulates transcription factors including Heat shock factor-1 (HSF-1). In addition to its well characterized functions in malignancy, recent evidence from several laboratories suggests a role for HSP90 in maintaining the functional stability of neuronal proteins of aberrant capacity, whether mutated or over-activated, allowing and sustaining the accumulation of toxic aggregates. Preclinical studies have demonstrated that disruption of much client proteins chaperoned by HSP90 is a possible strategy to reduce tumorigenesis but could suppress many neurodegeneration both in vivo and in vitro. Thus, inhibition of HSP90 has been found to be a novel strategy to target such diseases and pave the novel way of battling with these lethal diseases.KeywordsHeat shock proteinsHSP90CancerNeurodegenerationsHSP90-inhibitorsGeldanamycin