Heat shock proteins (HSPs) are highly conserved proteins, which are expressed in response to stress in all the species. Ritossa in 1962 (31), was first to observe an altered puffing pattern in giant chromosomes of salivary glands in Drosophila busckii after heat shock. On microscopic evaluation, areas of increased transcriptional activity in these giant chromosomes appear swollen and are called...

In view of the fact that certain non small cell lung carcinoma associated epidermal growth factor receptor mutations keep the receptor constitutively active, the downstream effectors of altered activity of mutant receptors are largely unknown. By 2D gel electrophoresis and MALDI-TOF/MS analysis, we showed that increased activity of EGFR mutants, L858R, L861Q and A871G induce heat shock proteins...

Heat shock proteins (Hsps) are highly conserved proteins that play a role in cytoprotection and maintaining intestinal homeostasis. Glutamine is essential for the optimal induction of intestinal epithelial Hsp expression, but its mechanisms of action are incompletely understood. Glutamine is a substrate for polyamine synthesis and stimulates the activity of ornithine decarboxylase (ODC), a key ...

When primary cultures of guinea pig gastric mucosal cells were exposed to heat (43 degree C), ethanol, hydrogen peroxide (H2O2), or diamide, heat shock proteins (HSP90, HSP70, HSP60, and HSC73) were rapidly synthesized. The extent of each HSP induction varied with the type of stress. Ethanol, H2O2, and diamide increased the syntheses of several other undefined proteins besides the HSPs. However...

Insulin induces the expression of the 70-kDa heat shock protein (Hsp70) in rat hearts. In this study, we examined insulin- and heat shock-treated hearts for improved contractile recovery after 30 min of ischemia, activation of the heat shock transcription factor, and localization of the Hsp70 in relation to dystrophin and alpha-tubulin. Adult male Sprague-Dawley rats were assigned to groups: 1)...

Cytoplasmic members of the heat shock protein hsp70 family have recently been implicated in the transport of proteins to the endoplasmic reticulum and mitochondria. In addition, other hsp70 homologues have been found in the endoplasmic reticulum and mitochondria and, at least for the endoplasmic reticulum hsp70 homologue, may be involved in the proper folding and assembly of newly transported p...

The 70 kDa heat shock proteins (HSP70) are a family of molecular chaperones that bind transiently to unfolded proteins in an ATP/ADP dependent manner. Endo.SceI comprises a unique example for mitochondrial HSP70, which exists in a stable complex with a nucleolytic subunit as a multi-site specific DNase. The HSP70-subunit in Endo.SceI was autophosphorylated by ATP in vitro. The autophosphorylati...

skeletal muscle may develop adaptive chaperone and enhancementdefense system through daily exercisestimulation. the present study investigated resistance and exhaustion training alters the expression of chaperoneproteins. these proteins function to maintain homeostasis, facilitate repair from injury and provide protection. exercise-induced production of hsps in skeletal muscle and peripheral le...

Hemin-induced differentiation of the human erythroleukemia cell line K562 results in the expression and accumulation of erythroid-specific gene products such as embryonic and fetal hemoglobins and the elevated synthesis of the major heat shock protein HSP70. This activity was suggested to represent activation of a heat shock gene during erythroid maturation independent of stress induction. In t...