Suppression of Heat Shock Protein-70 by Ceramide in Heat Shock-induced HL-60 Cell Apoptosis
نویسندگان
چکیده
منابع مشابه
Regulation of heat shock protein 70 synthesis by heat shock in the preimplantation murine embryo.
Induced thermotolerance in murine embryos occurs at the 8-cell stage when embryos are maintained in vitro but not until the blastocyst stage if development proceeds in vivo. Present results indicate that ability of embryos to undergo induced thermotolerance is not limited by heat shock protein 70 (HSP70) synthesis. Exposure of 8-cell embryos to 40 degrees C enhanced synthesis of 2 constitutive ...
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Alzheimer's disease (AD) is the most common neurodegenerative disease that caused dementia which has no effective treatment. Growing evidence has demonstrated that AD is a "protein misfolding disorder" that exhibits common features of misfolded, aggregation-prone proteins and selective cell loss in the mature nervous system. Heat shock protein 70 (HSP70) attracts extensive attention worldwide, ...
متن کاملCytosolic heat shock protein 60, apoptosis, and myocardial injury.
BACKGROUND Heat shock proteins (HSPs) are well known for their ability to "protect" the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic eff...
متن کاملExtracellular heat shock protein 60, cardiac myocytes, and apoptosis.
RATIONALE Previously, we have found that changes in the location of intracellular heat shock protein (HSP)60 are associated with apoptosis. HSP60 has been reported to be a ligand of toll-like receptor (TLR)-4. OBJECTIVE We hypothesized that extracellular HSP60 (exHSP60) would mediate apoptosis via TLR4. METHODS AND RESULTS Adult rat cardiac myocytes were treated with HSP60, either recombina...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.275.12.8872