A large variety of stress conditions including physicochemical factors induce the synthesis of more than 20 heat shock proteins (HSPs). In E. coli, the heat shock response to temperature upshift from 30 to 42 degrees C consists of the rapid induction of these HSPs, followed by an adaptation period where the rate of HSP synthesis decreases to reach a new steady-state level. Major HSPs are molecu...

Background: Cellular tolerance to heat stress is mediated by shock proteins (HSPs). The HSPs act as molecular chaperones and are transcribed in response stress. Among different families of these proteins, HSP70 considered be related the development temperature tolerance. Unraveling polymorphism protein genes could a step towards identification genetic markers for selecting heat-tolerant cattle....

conclusions we have highlighted the role of rns3 plus rnt-gp96 mediated by α5integrin in producing il-12 and tnfα. it can be suggested that rnt-gp96 could enhance immunity characteristic of rns3 protein via production of pro-inflammatory cytokines. results our results showed that rnt-gp96 alone significantly increases the expression level of il-12, tnfα and α5integrin in thp-1 macrophages and d...

Since the elucidation of their functions in protein folding and translocation, heat shock protein chaperones have been a target of research in all spheres of biomedicine. Within the last five years, research efforts have intensified, following the discovery of raised levels of heat shock protein (Hsp) expression in the brains of patients suffering from many neurodegenerative disorders, includin...

Heat shock proteins (Hsps) are highly conserved biomolecules that are constitutively expressed and generally upregulated in response to various stress conditions (biotic and abiotic). Hsps have diverse functions, categorizations, and classifications. Their adaptive expression in fungi indicates their significance in these diverse species, particularly in dimorphic pathogens. Histoplasma capsula...

P rotection of the ischemic heart has been the subject of experimental and clinical research for more than a decade. Myocardial infarct size is a function of cell necrosis occurring during ischemial and reperfusion,2 and numerous investigators have attempted to limit ischemic-and reperfusion-induced injury by pharmacological means. On balance, if the number of articles indicating successful int...

Heat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis. Therefore, the ability of the im...

The 70-kDa heat shock proteins (HSP70s) are well-studied and characterized heat shock proteins (HSPs). They constitute essential components of a quality control system of protein synthesis, and function as molecular chaperones to prevent proteins from misfolding and aggregating during both de novo synthesis and under conditions of stress. Moreover, it is now well established that HSP70s play im...

Heat shock proteins (HSPs) constitute an endogenous cellular defense mechanism against environmental stresses. In the past few years, studies have shown that overexpression of HSPs can protect cardiac myocytes against ischemia-reperfusion injury. In an attempt to increase the HSPs in cardiac tissue, we used the compound radicicol that activates HSP expression by binding to the HSP 90 kDa (HSP90...