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Physiological Reviews, Vol. 81, No. 4, October 2001, pp. 1461-1497
Copyright ©2001 by the American Physiological Society
Department of Physiology, Faculty of Medicine, Cardiovascular Research Institute Maastricht, Maastricht University, Maastricht, The Netherlands
Snoeckx, Luc H. E. H.,
Richard N. Cornelussen,
Frans A. Van Nieuwenhoven,
Robert S. Reneman, and
Ger J. Van
der Vusse.
Heat Shock Proteins and Cardiovascular Pathophysiology. Physiol. Rev. 81: 1461-1497, 2001.
In the eukaryotic cell an
intrinsic mechanism is present providing the ability to defend itself
against external stressors from various sources. This defense mechanism
probably evolved from the presence of a group of chaperones, playing a
crucial role in governing proper protein assembly, folding, and
transport. Upregulation of the synthesis of a number of these proteins
upon environmental stress establishes a unique defense system to
maintain cellular protein homeostasis and to ensure survival of the
cell. In the cardiovascular system this enhanced protein synthesis
leads to a transient but powerful increase in tolerance to such
endangering situations as ischemia, hypoxia, oxidative injury, and
endotoxemia. These so-called heat shock proteins interfere with
several physiological processes within several cell organelles and, for
proper functioning, are translocated to different compartments
following stress-induced synthesis. In this review we describe the
physiological role of heat shock proteins and discuss their protective
potential against various stress agents in the cardiovascular system.
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