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Human hsp27, Drosophila hsp27 and human alphaB‐crystallin expression‐mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha‐induced cell death.
Expression of small stress proteins (shsp) enhances the survival of mammalian cells exposed to heat or oxidative injuries. Recently, we have shown that the expression of shsp from different species,Expand
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Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery.
The protective activity of small stress proteins (sHsp) against H2O2-mediated cell death in the highly sensitive murine L929 fibroblast has been analyzed. We report here that the human Hsp27- andExpand
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Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929
Hyperthermia and other forms of stress that induce and/or stimulate heat shock or stress protein (hsp) expression enhance the cellular resistance to TNF-alpha. One of the stress proteins, hsp70, hasExpand
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Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein.
Mammalian cells grown at 37 degrees C contain a single low-molecular-weight heat shock (or stress) protein with an apparent mass of 28 kilodaltons (kDa) whose synthesis increases in cells afterExpand
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Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras
The mammalian small stress protein hsp27 is an oligomeric phosphoprotein which interferes with the cell death induced by several stimuli. In that sense, we and others have recently shown that humanExpand
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Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones.
The REG and PRO cell clones were obtained from a colon adenocarcinoma induced in a BDIX rat by 1,2-dimethylhydrazine. When injected s.c. into syngeneic hosts, REG cells induce tumors that regress inExpand
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The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization.
The oligomeric small heat-shock protein hsp27, also denoted hsp28, is constitutively expressed in several mammalian cells and displays a phosphorylation status that is related to cellular growth andExpand
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Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update
Heat shock proteins (HSP) are a subset of the molecular chaperones, best known for their rapid and abundant induction by stress. HSP genes are activated at the transcriptional level by heat shockExpand
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Small Stress Proteins as Novel Regulators of Apoptosis
Small stress protein expression enhances the survival of mammalian cells exposed to numerous injuries that induce necrotic cell death. The cell surface receptor Fas/APO-1 and its ligand have beenExpand
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Tumor necrosis factor‐α induces changes in the phosphorylation, cellular localization, and oligomerization of human hsp27, a stress protein that confers cellular resistance to this cytokine
The stress protein hsp27 is constitutively expressed in several human cells and shows a rapid phosphorylation following treatment with tumor necrosis factor‐α (TNF‐α). hsp27 usually displays nativeExpand
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