Disease relevance of LOC290549

• Heat shock protein (hsp) induction by stressful stimuli such as heat and ischemia is known to protect cardiac cells from severe stress [1].
• Heat shock protects cultured neurons from glutamate toxicity [2].
• Heat shock response in the liver: expression and regulation of the hsp70 gene family and early response genes after in vivo hyperthermia [3].
• Heat shock at 42 degrees caused a rapid inhibition of protein synthesis in Reuber H35 hepatoma cells [4].
• Heat shock proteins are induced at normal temperatures by oxidants and during reoxygenation following hypoxia [5].

Psychiatry related information on LOC290549

• Heat shock protein-70 mRNA was not increased by water deprivation [6].
• Heat shock induces rapid dephosphorylation of tau in both female and male rats followed by hyperphosphorylation only in female rats: implications for Alzheimer's disease [7].
• Heat-shock protein concentrations in the blood increase after exposure to a variety of stressors, including trauma and psychological stress [8].

High impact information on LOC290549

• Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70 [9].
• Heat shock protein 70 prevents secretagogue-induced cell injury in the pancreas by preventing intracellular trypsinogen activation [10].
• Heat shock induces resistance in rat pancreatic islet cells against nitric oxide, oxygen radicals and streptozotocin toxicity in vitro [11].
• Heat shock inhibited excitotoxicity in cells exposed to glutamate at 3 or 24 hr following heat exposure, but not when the interval between heat and glutamate exposure was shortened to 15 min or lengthened to 48 hr [2].
• Heat-shock treatment significantly increased myocardial catalase compared with control animals (180.5 +/- 4.8, n = 6, versus 86.2 +/- 14.7, n = 5, units/g wet wt; P < .05) [12].

Chemical compound and disease context of LOC290549

• Heat shock response and cytotoxicity in C6 rat glioma cells: structure-activity relationship of different alcohols [13].
• CONCLUSIONS: Heat shock protein 70, induced by lipopolysaccharide pretreatment, forms complexes with inhibitory kappaBalpha and attenuates activation of nuclear factor kappaB and myocardial infarct size [14].
• Heat shock treatment protects against angiotensin II-induced hypertension and inflammation in aorta [15].
• Heat shock protein 27 delivered via a herpes simplex virus vector can protect neurons of the hippocampus against kainic-acid-induced cell loss [16].
• Heat shock- and ethanol-induced ionic changes in C6 rat glioma cells determined by NMR and fluorescence spectroscopy [17].

Biological context of LOC290549

• Heat-shock protein expression preceded cell death (assessed with acid fuchsin staining) in all regions [18].
• Heat shock response in cultured cells has been studied extensively; however few data are available on heat shock response in an intact organ of a living animal [3].
• Heat shock induces c-Jun N-terminal kinase (JNK) activation as well as heat shock protein (HSP) expression through activation of the heat shock factor (HSF), but its signal pathway is not clearly understood [19].
• Heat shock or transfection with heat shock protein 70 (Hsp70) genes has been shown to protect tumor cell lines against immune mechanisms of cytotoxicity [20].
• Heat shock and oxidative stress-induced exposure of hydrophobic protein domains as common signal in the induction of hsp68 [21].

Anatomical context of LOC290549

• Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress [22].
• Heat shock protein 27: developmental regulation and expression after peripheral nerve injury [23].
• Heat shock response inhibits cytokine-inducible nitric oxide synthase expression in rat hepatocytes [24].
• Heat shock protein (Hsp)60 and IGF-1 receptor signaling protect cardiac muscle against injury [25].
• Heat shock protein 65-reactive T cells are involved in the pathogenesis of non-antigenic dimethyl dioctadecyl ammonium bromide-induced arthritis [26].

Associations of LOC290549 with chemical compounds

• Heat shock inhibited MPT pore opening induced by 50 microm CaCl(2) plus 5 microm HgCl(2) or 1 microm mastoparan and by 200 microm CaCl(2) alone [27].
• Heat shock treatment decreased mitochondrial reactive oxygen species formation by 27% but did not change mitochondrial respiration, membrane potential, Ca(2+) uptake, or total glutathione in mitochondrial and cytosolic extracts of liver [27].
• Heat shock also increased the threshold of unregulated (Ca(2+)-independent and cyclosporin A-insensitive) MPT pore opening induced by higher doses of HgCl(2) and mastoparan [27].
• Heat shock caused disruption of the actin filament and cell death when phosphorylation of HSP25 was inhibited by SB203580 and/or PD098059 [28].
• Heat shock prevents lipopolysaccharide-induced tumor necrosis factor-alpha synthesis by rat mononuclear phagocytes [29].

Physical interactions of LOC290549

• Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell [30].
• (6) Heat shock protein 90 bound to monomyristoylated lysozyme, but not to control unmodified lysozyme [31].

Regulatory relationships of LOC290549

• Heat shock-induced attenuation of hydroxyl radical generation and mitochondrial aconitase activity in cardiac H9c2 cells [32].
• CONCLUSIONS: Heat shock preconditioning suppressed the production of TNF-alpha and CINC in the liver during reperfusion and consequently reduced neutrophil infiltration [33].
• Heat shock induces neurite outgrowth in PC12m3 cells via the p38 mitogen-activated protein kinase pathway [34].
• Heat shock protein 27 delays Ca2+-induced cell death in a caspase-dependent and -independent manner in rat retinal ganglion cells [35].
• Heat shock inhibits the hypoxia-induced effects on iodide uptake and signal transduction and enhances cell survival in rat thyroid FRTL-5 cells [36].

Other interactions of LOC290549

• OBJECTIVE AND DESIGN: Heat shock (HS) treatment (42 degrees C for 15 min) and the expression of heat shock proteins (Hsps) protect against angiotensin (Ang) II-induced inflammation in aorta and heart by suppressing the activation of the pro-inflammatory transcription factor NF-kappaB [37].
• Heat shock protein 90alpha-dependent translocation of annexin II to the surface of endothelial cells modulates plasmin activity in the diabetic rat aorta [38].
• Heat shock led to a decrease in liver superoxide dismutase (SOD) activity at 1 hour in the antioxidant-supplemented group, but this was unchanged in the liver of all other groups and in the skin [39].
• Heat shock protein 27 shows a distinctive widespread spatial and temporal pattern of induction in CNS glial and neuronal cells compared to heat shock protein 70 and caspase 3 following kainate administration [40].
• Heat shock treatment resulted in an increased number of the cells exhibiting a nuclear location of 100 kDa [41].

Analytical, diagnostic and therapeutic context of LOC290549

• Heat shock protein induction in rat hearts. A role for improved myocardial salvage after ischemia and reperfusion [42]?
• Heat shock treatment in PC12 cells induces the synthesis of two HSP70 transcripts of 2.55 and 3.05 kb in size, while only a 70-kDa protein is shown by SDS-PAGE [43].
• Heat shock protein 27 in chronic allograft nephropathy: a local stress response [44].
• Heat shock protein 70, a cytoprotective molecule, was evaluated by western blotting [45].
• Heat shock induced SP71 synthesis in freshly prepared cells and in cell cultures at each age examined, whereas Cd2+ was effective only in cultures at 7 days of age and older [46].

References