| pubmed-article:7583171 | pubmed:abstractText | Septic shock, multiorgan dysfunction, and the acute respiratory distress syndrome are major contributors to morbidity and mortality in the ICU setting. Animal studies have shown that these forms of injury can be attenuated or prevented if a phenomenon, called the stress response, is activated. The stress response, characterized by a transient downregulation of most cellular products and by the upregulation of the heat-shock proteins (HSPs), has been shown to provide protection to cells and experimental animals if triggered prior to an otherwise lethal injury. The mechanisms by which the stress response is protective are not known with certainty, but HSPs appear to play an important role. HSPs are constitutively present in all cells studied to date and can also be induced by artificial fever and by nonthermal means. They act as molecular chaperones, interacting transiently with newly synthesized proteins and proteins experiencing difficulty in proper folding. HSPs also escort and help proteins to cross membranes. This chaperone function is essential for cellular protection since it provides a mechanism by which defective polypeptides may be directed to lisosomes for degradation. This article summarizes the current literature on the effects of the stress response in protecting cells and animals from lethal forms of systemic and organ damage. | lld:pubmed |
