HSP90: The Unsung Villain of Sepsis?

  • J. P. Burnie
  • R. C. Matthews
Conference paper

Abstract

Heat shock protein 90 (HSP90) is a molecular chaperone that ensures the correct folding and conformational maturation of specific proteins involved in a wide variety of cellular processes [1, 2]. Large multidomain proteins are prone to aggregation or to becoming involved in kinetically trapped intermediates; HSP90 is required for a specific set of difficult to fold proteins. When cells are stressed (e.g., because of growth at an unfavorable temperature, osmotic pressure, oxygen tension, pH, or in the presence of noxious chemicals or antibiotics), they upregulate HSP90 production in order to help combat the effects of protein degradation. HSP90 also aids protein stabilization and facilitates activation of many regulated proteins. HSPs have also been shown to be immunodominant and are major targets for the immune system in many infections [3, 4]. Inhibitors of HSP90 have been shown to deplete multiple proteins important in signal transduction, cell cycle regulation, apoptosis, invasion, angiogenesis, metastasis, immortalization [1].

Keywords

Heat Shock Protein Natural Antibody Systemic Candidiasis Human HSP90 Antigenic Band 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science + Business Media Inc. 2006

Authors and Affiliations

  • J. P. Burnie
    • 1
  • R. C. Matthews
    • 1
  1. 1.Department of Medical MicrobiologyManchester Royal InfirmaryManchesterUK

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