Heat shock protein synthesis

Cleget, M. Polla, B.S. (1990). Erythrophagocytosis induces heat shock protein synthesis by human monocytes-macrophages. Proc. Natl. Acad. Sci. USA 87, 1081-1085. 

Fassen, A.E., O Leary, J.J., Rodysill, K.J., Bergh, N., Hallgren, H.M. (1989). Diminished heat shock protein synthesis following mitogen stimulation of lymphocytes from aged donors. Exp. Cell. Res. 183,326-334. 

Yost, HJ. Lindquist, S. (1986). RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis. Cell 45, 185-193. 

Yost, H.J., Petersen, R.B., Lindquist, S. (1990). Post-transcriptional regulation of heat shock protein synthesis in Drosophila In Stress Proteins in Biology and Medicine (Morimoto, R., Tissieres, A. Georgopoulos, C., eds.), pp. 379-409, CSH Laboratory Press, Cold Spring Harbor. 

Nieto-Sotelo, J. Ho, T.-H.D. (1987). Absence of heat shock protein synthesis in isolated mitochondria and plastids from maize. Journal of Biological Chemistry, 262, 12288-92. 

Gehring, W.J., and R. Wehner (1995). Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert. Proc. Natl. Acad. Sci. USA 92 2992-2998. 

SecB is an acidic, soluble, tetramer of identical 17-kDa subunits. It comprises only 0.08% of the cytosolic proteins. The secB gene is conditionally essential in that secB null strains cannot grow on rich media or at subbasal levels of heat-shock protein synthesis, but can grow on minimal media. Overexpression of heat-shock proteins can partially suppress the export and growth defects in secB null strains. SecB is not a heat-shock protein, and ATP has no known effect on its function. 

Initiation factor phosphorylation. The phosphorylation of eIF-2 in response to certain circumstances (e.g., heat shock, viral infections, and growth factor deprivation) has been observed to decrease protein synthesis generally. However, the translation of certain mRNA increases. For example, hsp (heat shock protein) synthesis increases in response to heat shock and other stressful conditions. The specific mechanisms are unknown. 

Furthermore, NO produced by NO donors induces heat shock protein synthesis (hsp 70) in HEP G2 cells isolated from a human hepatoma. In one hand, hsp 70 inhibits iNOS transcription by reducing NFkB translocation, in an other hand, it prevents ATP depletion due to NO [159],... 

Koishi, M. et al.. Quercetin, an inhibitor of heat shock protein synthesis, inhibits the acquisition of thermotolerance in a human colon carcinoma cell line, Jpn. J. Cancer Res., 83, 1216,1992. 

Wiegant FA, Malyshev lY et al (1999) Dinitrosyl iron complexes with thiol-containing ligands and S-nitroso-D, L-penicillamine as inductors of heat shock protein synthesis in H35 hepatoma cells. FEBS Lett 455 179-182... 

Li GC (1983) Induction of thermotolerance and enhanced heat shock protein synthesis in Chinese hamster fibroblasts by sodium arsenite and by ethanol. J Cell Physiol 115 116-122... 

Matsubara J, Tajima Y, Karasawa M (1987) Promotion of radioresistance by metallothionein induction prior to irradiation. Environ Res 43 66-74 Miller L, Qureshi MA (1992) Heat-shock protein synthesis in chicken macrophages influence of in vivo and in vitro heat shock, lead acetate, and lipopolysaccharide. Poult Sci 71 988-998... 

Cardiac hypertrophy appears to be mediated by HS proteins (Izumo et al., 1988). Cardiac myocytes exposed to a hemodynamic stress have been found to increase their levels of heat shock proteins (Delcayre et al., 1988). Although experiments involving interference with HS protein synthesis were not done in these studies. 

Beere, H.M., Morimoto, R.I., Hickman, J.A. (1993). Investigations of mechanisms of drug-induced changes in gene expression N methylformamide-induced changes in synthesis of the M(r) 72,000 constitutive heat shock protein during commitment of HL-60 cells to granulocyte differentiation. Cancer Res. 53, 3034—3039. 

Chang, C.C., Konno, S., Wu, J.M. (1991). Enhanced expression of heat shock protein and mRNA synthesis by type I interferon in human HL-60 leukemic cells. Biochem Inti. 24, 369-377. 

Currie, R.W. (1987). Effects of ischemia and perfusion temperature on the synthesis of stress-induced (heat shock) proteins in isolated and perfused rat hearts. J. Mol. Cell. Cardiol. 19, 795-808. 

Perez, N., Sugar, J., Chatya, S., Johnson, G., Merril, C., Bierer, L., Perl, D., Haroutunian, V., Wallace, W. (1991). Increased synthesis and accumulation of heat shock proteins in Alzheimer s disease Brain Res. Mol. Brain Res. 11,249-254. 

Kloppstech, K., Meyer, G., Schuster, G. Ohad, I. (1985). Synthesis, transport and localization of nuclear coded 22-kd heat-shock protein in the chloroplast membranes of peas and Chlamydomonas. EMBO Journal, 4, 1901-9. 

Lin, C.Y., Roberts, J.K. Key, J.L. (1984). Acquisition of thermotolerance in soybean seedlings synthesis and accumulation of heat shock proteins and their cellular localization. Plant Physiology, 74,152-60. 

When bacterial cells are shifted directly from a low growth temperature to a lethal temperature, the cells are rapidly killed. However, if the cells are first preadapted by growth at a non-lethal temperature for 30 min, the rate of killing upon a shift to lethal temperature is dramatically decreased these cells have acquired thermotolerance. During the pre-adaptation phase a heat shock response is induced which leads to increased synthesis of heat shock proteins. 

Heat shock proteins (HSPs) are synthesized by cells in response to an increase in temperature, as well to various other stressful stimuli. Their main function is to ensure intracellular protein homeostasis, thus preserving the cells viability in the presence of aggression. Current evidence points to a protective role for HSPs in several aspects of critical disease, such as ischemia-reperfusion, ARDS, and multiple organ failure. The increase of a few degrees Celsius above the normal environmental temperature of cells leads to the heat shock response 1) rapid expression of heat shock genes, 2) suppression of normal protein synthesis, and 3) the ability of cells to survive a second and otherwise lethal heat challenge (thermotolerance). 

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