phosphatidic acid/نخر

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Phosphatidic acid and tumor necrosis factor-alpha induce the expression of CD83 through mitogen activated protein kinase pathway in a CD34+ hematopoietic progenitor cell line, KG1.

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To elucidate the signaling pathways involved in the expression of CD83, which is linked to the differentiation and maturation states of dendritic cells, we examined the effect of phosphatidic acid (PA) on the expression of CD83 in KG1, a CD34(+) hematopoietic progenitor cell. In the presence of

Tumor necrosis factor alpha priming of phospholipase D in human neutrophils. Correlation between phosphatidic acid production and superoxide generation.

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Tumor necrosis factor alpha (TNF) primes human neutrophils (PMN) for enhanced superoxide (O2-) production if cells are subsequently stimulated with the chemotactic peptide, n-formyl-Met-Leu-Phe (fMLP). fMLP activates phospholipase D to form phosphatidic acid (PA), and a correlation may exist between

Loss of lipin 1-mediated phosphatidic acid phosphohydrolase activity in muscle leads to skeletal myopathy in mice.

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Lipin 1 regulates glycerolipid homeostasis by acting as a phosphatidic acid phosphohydrolase (PAP) enzyme in the triglyceride-synthesis pathway and by regulating transcription factor activity. Mutations in human lipin 1 are a common cause of recurrent rhabdomyolysis in children. Mice with

Phosphatidic acid as a regulator of matrix metalloproteinase-9 expression via the TNF-alpha signaling pathway.

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Phosphatidic acid (PA) is implicated in pathophysiological processes associated with cellular signaling events and inflammation, which include the expressional regulation of numerous genes. Here, we show that PA stimulation increases matrix metalloproteinase-9 (MMP-9) expression in macrophages

Lisofylline, an inhibitor of unsaturated phosphatidic acid generation, ameliorates interleukin-1 beta-induced dysfunction in cultured rat islets.

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Interleukin-1 beta (IL-1 beta) causes rat islet cell dysfunction through mechanisms that involve inducible nitric oxide synthase (iNOS). However, IL-1 beta also activates several lipid pathways, including those generating phosphatidic acid (PA). Lisofylline (LSF), a water-soluble, nontoxic,

Controlled release by Ca(2+)-sensitive recombinant human tumor necrosis factor-alpha liposomes.

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Recombinant human tumor necrosis factor-alpha (rHuTNF) was entrapped in liposomes consisting of Egg phosphatidylcholine (EggPC) alone, EggPC-egg phosphatidic acid (EggPA) or EggPC-egg phosphatidylglycerol (EggPG). These liposomes, stored in vials, were stable for a month at 4 degrees C. The rHuTNF

Phosphatidylcholine-specific phospholipase C and phospholipase D are respectively implicated in mitogen-activated protein kinase and nuclear factor kappaB activation in tumour-necrosis-factor-alpha-treated immature acute-myeloid-leukaemia cells.

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Tumour necrosis factor-alpha (TNFalpha) has been reported to induce potent growth inhibition of committed myeloid progenitor cells, whereas it is a potential growth stimulator of human CD34(+)CD38(-) multipotent haematopoietic cells. The present study was aimed at evaluating the respective role of

Potential role for phosphatidic acid in mediating the inflammatory responses to TNF alpha and IL-1 beta.

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Tumor necrosis factor alpha (TNF alpha), interleukin 1 beta (IL-1 beta), and endotoxin (LPS) are potent pro-inflammatory mediators which induce multiple and diverse biological responses in a wide variety of cell types. However, these pro-inflammatory mediators also have significant overlap and

Phosphatidic acid induces the differentiation of human acute promyelocytic leukemic cells into dendritic cell-like.

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We investigated whether phosphatidic acid (PA) can differentiate the promyelocytic leukemia (PML)-retinoic acid receptor alpha (RAR alpha)-expressing acute promyelocytic leukemic cell line, NB4, to dendritic cell (DC)-like cells. Dioctanoyl-PA alone upregulated the expression of DC markers. The

Secretions of MMP-9 by soluble glucocorticoid-induced tumor necrosis factor receptor (sGITR) mediated by protein kinase C (PKC)delta and phospholipase D (PLD) in murine macrophage.

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The secretion of matrix metalloproteinase (MMP-9) is stimulated by the glucocorticoid-induced tumor necrosis factor receptor (GITR), a new tumor necrosis factor receptor (TNFR) family, in murine macrophages via an activation of protein kinase C (PKC)delta and phospholipase D (PLD). Secretions of

Tumor necrosis factor-alpha/cachectin activates the O2(-)-generating system of human neutrophils independently of the hydrolysis of phosphoinositides and the release of arachidonic acid.

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We have investigated the mechanisms of transmembrane signalling implicated in the activation of the respiratory burst of adherent neutrophils by tumor necrosis factor-alpha/cachectin (TNF). The activation of the respiratory burst by TNF is insensitive to pertussis toxin and weakly sensitive to

Induction of cytosolic phospholipase A2 activity by phosphatidic acid and diglycerides in permeabilized human neutrophils: interrelationship between phospholipases D and A2.

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Relationships between phospholipases are poorly understood, but phosphatidic acid (PA) and diglycerides (DGs), produced by phospholipase D (PLD) and phosphatidate phosphohydrolase actions, might function as second messengers coupling cell stimulation to cellular responses. This study investigates

Phospholipase D activation in human natural killer cells through the Kp43 and CD16 surface antigens takes place by different mechanisms. Involvement of the phospholipase D pathway in tumor necrosis factor alpha synthesis.

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We have recently described a novel glycoprotein, Kp43, expressed on the surface of human natural killer (NK) cells that appears to regulate their functional activity. In this report, signaling mechanisms through the Kp43 surface antigen have been studied. Incubation of interleukin 2 (IL-2)-treated

Tumor necrosis factor induces rapid production of 1'2'diacylglycerol by a phosphatidylcholine-specific phospholipase C.

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Tumor necrosis factor (TNF) is a proinflammatory polypeptide that is able to induce a great diversity of cellular responses via modulating the expression of a number of different genes. One major pathway by which TNF receptors communicate signals from the membrane to the cell nucleus involves

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

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