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Heat Shock Proteins in Critical Illness: Markers of Cellular Stress or More?

  • Conference paper
Yearbook of Intensive Care and Emergency Medicine 1994

Part of the book series: Yearbook of Intensive Care and Emergency Medicine 1994 ((YEARBOOK,volume 1994))

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Abstract

Heat shock proteins (HSPs) are synthesized by cells in response to an increase in temperature, as well as to various other stressful stimuli. Their main function is to insure intracellular protein homeostasis, thus preserving the cells’ viability in the face of aggression. Many inducers of HSP synthesis are part of the complex pathophysiological mechanisms underlying critical illness, in particular oxidative injury. Currently available evidence points to a potential protective role for HSPs in several aspects of critical disease, such as ischemia-reperfusion, ARDS, and multiple organ dysfunction syndrome (MODS). The purpose of this chapter is to briefly review the current evidence for the role HSPs might play in such conditions.

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Authors
  1. P. Jolliet
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  2. D. O. Slosman
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  3. B. S. Polla
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Editor information

Editors and Affiliations

  1. Department of Intensive Care Erasme Hospital, Free University of Brussels, Route de Lennik 808, B-1070, Brussels, Belgium

    Jean-Louis Vincent (Clinical Director) (Clinical Director)

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© 1994 Springer-Verlag Berlin Heidelberg

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Jolliet, P., Slosman, D.O., Polla, B.S. (1994). Heat Shock Proteins in Critical Illness: Markers of Cellular Stress or More?. In: Vincent, JL. (eds) Yearbook of Intensive Care and Emergency Medicine 1994. Yearbook of Intensive Care and Emergency Medicine 1994, vol 1994. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-85068-4_3

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  • DOI: https://doi.org/10.1007/978-3-642-85068-4_3

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-57613-6

  • Online ISBN: 978-3-642-85068-4

  • eBook Packages: Springer Book Archive

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