Heat shock, also protein

Exposure of neutrophils to heat shock also results in the synthesis of HSPs and a decrease in their ability to generate reactive oxidants. This is not due to cell death, because the response is reversible and other cellular functions are unaffected. For example, after 20 min exposure at 45 °C, the NADPH oxidase is non-functional, but arachidonic acid release is 73% of control values and PGE2 formation is unaffected. Oxidase activity returns to normal levels 150 min later. Several HSPs are synthesised (e.g. hsp70 and hsp85 at 41 °C, hsp48 and hsp60-65 at 43 °C). (The hsp numbers refer to the relative molecular masses of the proteins.)... 

Cold stress may induce synthesis of heat-shock (stress) proteins. Exposure of cells to cold shock may lead to the induction of one or more of the classes of molecular chaperones that also are induced by heat shock. This is strong evidence that low temperature, like high temperature, can lead to non-native protein structures in vivo and, therefore, to the requirement for enhanced chaperoning activity. Induction of cold-induced protein chaperones has been seen in bacteria (Salotra et al., 1995), in whole organism studies of ectothermic animals (Petersen et al., 1990 Yocum et ah, 1991),... 

Phosphorylation of HSF substantially enhances the transcriptional activity of HS gene expression which may be up to 100-fold of basal levels after HSFl binds to the promoter element. Heat shock will increase the C-terminal-domain-kinase activity in cell extracts, and this action may enhance the activity of RNA polymerase II that is bound to HS genes (Legagneux et al., 1990). Whether this kinase activity also affects HSFl phosphorylation is not known, but increased HS gene expression appears to occur as long as HSFl is bound to the promoter region. The CTD kinase complex contains multiple proteins, and it is quite possible that one or more of these proteins is also regulated by stress. 

Most medical students look askance at thermobiology. We think this is a mistake hence, we have included a section dealing with this subject. This brings us to the chapter on the heat shock response which at the very outset makes clear that many stressors besides heat are known to result in heat shock gene expression. Many of the heat shock proteins occur in unstressed cells and some of them behave as chaperones. These proteins also reach high levels in a wide range of diseases... 

It has been postulated that Chlamydia may produce a heat shock protein that causes tissue damage through a delayed hypersensitivity reaction. C. trachomatis may also possess DNA evidence of toxin-like genes that code for high-molecular-weight proteins with structures similar to Clostridium difficile cytotoxins, enabling inhibition of immune activation. This may explain the observation of a chronic C. trachomatis infection in subclinical PID. 

---