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phospholipid/nekros
Länken sparas på Urklipp
Sida 1 från 956 resultat
Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3.
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Tumor Necrosis Factor (TNF)-Related Apoptosis-Inducing Ligand (TRAIL) initiate pathways of cell death in which caspase activation is mediated either directly (without mitochondrial amplification), or indirectly via the release of apoptogenic factors from mitochondria. Phospholipid scramblases (PLS)
Nuclear magnetic resonance analysis of tumor necrosis factor-induced alterations of phospholipid metabolites and pH in Friend leukemia cell tumors and fibrosarcomas in mice.
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The alterations induced on the pool sizes of five phospholipid metabolites, glycerol 3-phosphorycholine, glycerol 3-phosphorylethanolamine, phosphorylcholine, sn-glycerol 3-phosphate, and choline were studied by nuclear magnetic resonance (NMR) spectroscopy in murine tumors injected with recombinant
Tumour necrosis factor induction by malaria exoantigens depends upon phospholipid.
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In patients with malaria, the clinical manifestations of the disease are associated with the presence of high concentrations of tumour necrosis factor (TNF) in the serum. Blood-stage parasites of human and rodent malarial parasites release serologically related exoantigens which induce the
Amino acid-mediated stimulation of renal phospholipid biosynthesis after acute tubular necrosis.
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The mechanism by which amino acid infusion stimulates membrane physpholipid biosynthesis during renal regeneration after mercuric-chloride-induced acute tubular necrosis was studied in the rat. Amino acids can act directly on regenerating renal tissue to enhance net phospholipid synthesis because
Phospholipid metabolism during renal regeneration after acute tubular necrosis.
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Renal function, structure, and membrane metabolism were studied during regeneration of proximal tubular cells in rats. A reversible syndrome of nonoliguric acute renal failure was induced by the intravenous administration of a low dose of mercuric chloride (1.0 mg Hg/kg). At day 1 there was a marked
Changes of tumor necrosis factor, surfactant protein A, and phospholipids in bronchoalveolar lavage fluid in the development and progression of coal workers' pneumoconiosis.
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OBJECTIVE
To evaluate the alterations of biomarkers in the development and progression of coal workers' pneumoconiosis (CWP).
METHODS
The type and number of cells, and the levels of tumor necrosis factor-alpha (TNF-alpha), pulmonary surfactant protein, phospholipids and fibronectin in
Augmentation and suppression of release of tumor necrosis factor from macrophages by negatively charged phospholipids.
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We recently reported that some lipid species of cell membranes and lipoproteins induced the growth of peripheral macrophages. In this study, the effects of phospholipids on tumor necrosis factor (TNF)-releasing activity of macrophages were examined. Ten to 20 micrograms/ml of cardiolipin, which is a
Increased phospholipid mass with decreased arachidonoyl molecular species is associated with decreased eicosanoid synthesis and increased tumor necrosis factor synthesis by thioglycollate-elicited rat peritoneal macrophages.
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Because the activation state of macrophages may alter their response to endotoxin, we compared phospholipid arachidonic acid content, and synthesis of eicosanoids and tumor necrosis factor by resident and thioglycollate-elicited rat peritoneal macrophages. Thioglycollate elicitation increased
Tumor necrosis factor-induced permeability increase of negatively charged phospholipid vesicles.
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The effect of human tumor necrosis factor (TNF) on the permeability properties of liposomes containing phosphatidylserine at pH 5-6, as demonstrated by the calcein efflux. However, it did not induce any permeability change in such liposomes at neutral pH. The TNF-induced calcein efflux was also
Phospholipids coupled to a carrier induce IgG antibody that blocks tumour necrosis factor induction by toxic malaria antigens.
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Phospholipid-containing antigens of malaria parasites stimulate macrophages to secrete tumour necrosis factor (TNF), induce hypoglycaemia and are toxic to mice. This TNF induction is inhibited by antisera made against the antigens, the inhibitory activity of which can be removed specifically by
Effect of tumor necrosis factor-alpha on triglyceride and phospholipid content and fatty acid composition of liver and carcass in rats.
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We have previously shown that a continuous infusion of tumor necrosis factor-alpha (TNF-alpha) in rats results in an increase in plasma triglyceride (TG), liver protein and DNA, and at the same time a reduction in muscle protein. However, there is no information on the associated effects of
Mechanism of human lymphotoxin and tumor necrosis factor induced destruction of cells in vitro: phospholipase activation and deacylation of specific-membrane phospholipids.
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The role of phospholipase (PLase) activation and lipid metabolism in lymphotoxin (LT)- and tumor necrosis factor (TNF)-mediated destruction of murine L929 cells was examined. At the levels of LT and TNF employed, cell destruction began at 4-6 h and was 99% complete by 30 h. Cell membrane
Tumor necrosis factor-alpha alters phospholipid content in the bronchoalveolar lavage-accessible space of isolated perfused rat lungs.
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OBJECTIVE
To examine the effect of tumor necrosis factor-alpha (TNF-alpha) on pulmonary artery pressure and on total protein, phospholipid, lysophosphatidylcholine, phosphatidylcholine, phosphatidylinositol, and phosphatidylglycerol content in the bronchoalveolar lavage-accessible space of the
Recombinant tumor necrosis factor and interleukin-1 both stimulate human synovial cell arachidonic acid release and phospholipid metabolism.
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Stimulation of [3H]-arachidonic acid labeled human synovial cells with 3.0 X 10(-10)M recombinant interleukin-1 or tumor necrosis factor resulted in the release of incorporated radiolabel (41.1% and 27.7% respectively). Analysis of [3H]-arachidonic acid labeled phospholipids showed that
Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis.
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In tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis, tBid is targeted to mitochondria and causes cytochrome c release. We investigated the regulation of tBid-induced cytochrome c release and apoptosis by phospholipid scramblase 3 (PLS3). Overexpression of PLS3 enhanced, whereas
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