Protective functions of intracellular heat-shock protein (HSP) 70-expression in patients with severe sepsis.
Intracellular expression of heat-shock-protein 70 (HSP70) arose early in evolutionary development as a tool to protect cellular homeostasis. HSP70 detects proteins that are incorrectly folded or denatured. They form a complex with such proteins which can lead to correct folding, compartmentalization in organelles, or to proteolytic degradation. HSP70 also appears to protect proteins from degeneration. Intracellular HSP70-expression is induced by a wide variety of stimuli including heat, fever, hypoxia, oxygen radicals, endotoxins, cytokines, and heavy metal ions. Pre-emptive induction of HSP70-expression reduces organ dysfunction and mortality in animal models of sepsis.
Bruemmer-Smith
S
S
Department of Anesthesiology and Critical Care Medicine, Royal Brompton Hospital, Sydney Street, London SW3 6NP, UK.
Stüber
F
F
Schroeder
S
S
D000818:Animals; D019610:Cytoprotection; D004195:Disease Models, Animal; D005786:Gene Expression Regulation; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008954:Models, Biological; D018805:Sepsis / Q000276:immunology / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins