arachidonate/cariës

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Arachidonate metabolic pathways in cells harvested from rat pleural cavity at various times after carrageenan administration.

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Cells were harvested from rat pleural cavity before and during the inflammatory response stimulated by carrageenan injection. The conversion of [14C]arachidonate by intact cells into products of the cyclooxygenase and 5-lipoxygenase pathways was studied in the absence and presence of ionophore.

Vascular permeabilization by intravenous arachidonate in the rat peritoneal cavity: antagonism by antioxidants.

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Arachidonic acid was investigated for its vascular permeabilizing potential in the rat peritoneal cavity and for its mechanism of action. The antagonistic potential of antioxidants (vitamin E, vitamin C and troxerutin) was also evaluated. Vascular permeability was equated to the rate of

Vascular permeabilization by intravenous arachidonate in the rat peritoneal cavity: antagonism by ethamsylate.

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The hemostatic agent, ethamsylate, inhibits arachidonic acid metabolism by a mechanism independent of cyclooxygenase activity and blocks carrageenan-induced rat paw edema. Here, ethamsylate was investigated for (i) in vivo actions on the free radical-dependent, permeabilizing responses to

Immune complex mediated inflammation in the mouse peritoneal cavity. A method for investigating inhibitors of arachidonate metabolism.

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Intraperitoneal injection of washed, preformed ovalbumin/anti-ovalbumin immune complexes caused the production of slow-reacting substance (SRS), prostaglandin E2, 6 keto prostaglandin Fla, vascular permeability (measured as extravazation of pontamine sky blue injected previously into the

Glucocorticoids induce the formation and release of anti-inflammatory and anti-phospholipase proteins into the peritoneal cavity of the rat.

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1 Dexamethasone and hydrocortisone induced the release of anti-phospholipase proteins into the peritoneal cavities of rats. 2 Adrenocorticotrophic hormone (ACTH) also releases these proteins in normal but not in adrenalectomized rats. 3 Peritoneal lavage proteins were separated by ion-exchange and

Influence of endotoxin on arachidonate metabolism in isolated rabbit peritoneum.

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The serous membranes of the rabbit peritoneal cavity are tissues in which cyclo-oxygenase and lipoxygenase pathways of arachidonate metabolism can be studied simultaneously. After elaboration of the optimum conditions, the metabolism of two concentrations of arachidonic acid (AA) was studied in the

Characterization of arachidonate 12-lipoxygenase found in the liver of mongrel dog and its immunohistochemical localization in neutrophils.

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The cytosol fraction of non-parenchymal cells isolated from the liver of adult mongrel dogs converted arachidonic acid to 12S-hydroxy-5,8,10,14-eicosatetraenoic acid. The arachidonate 12-lipoxygenase enzyme reacted with linoleic and alpha- and gamma-linolenic acids as well as arachidonic acid. The

Bothrops lanceolatus (Fer de lance) venom stimulates leukocyte migration into the peritoneal cavity of mice.

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The ability of Bothrops lanceolatus venom to induce neutrophil migration into the peritoneal cavity of mice was investigated. Intraperitoneal injection of venom caused dose- and time-dependent neutrophil migration, which peaked with 750 ng of venom/cavity 4h after venom injection. The neutrophil

Crystal structure of human prostaglandin F synthase (AKR1C3).

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Prostaglandin H(2) (PGH(2)) formed from arachidonic acid is an unstable intermediate and is efficiently converted into more stable arachidonate metabolites (PGD(2), PGE(2), and PGF(2)) by the action of three groups of enzymes. Prostaglandin F synthase (PGFS) was first purified from bovine lung and

A major role for phospholipase A2 in antigen-induced arachidonic acid release in rat mast cells.

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Cross-linking of IgE receptors by antigen stimulation leads to histamine release and arachidonic acid release in rat peritoneal mast cells. Investigators have reported a diverse distribution of [3H]arachidonate that is dependent on labelling conditions. Mast cells from rat peritoneal cavity were

Lipoxygenase-derived mediators may be involved in in vivo neutrophil migration induced by Bothrops erythromelas and Bothrops alternatus venoms.

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Bothrops erythromelas (BEV) and B. alternatus (BAV) venoms induced a dose-dependent neutrophil migration when injected into rat peritoneal cavities (20-160 micrograms/cavity). These venoms (80 micrograms/rat) also induced neutrophil migration in the air pouch model of inflammation. This migratory

Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies.

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The association of the adipocyte lipid-binding protein (ALBP) with arachidonic acid (all cis, 20:4 delta 5,8,11,14) and oleic acid (cis, 18:1 delta 9) has been examined by titration calorimentry. In addition, the crystal structure of ALBP with bound arachidonic acid has also been obtained.

Carrageenan-stimulated release of arachidonic acid and of lactate dehydrogenase from rat pleural cells.

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Cells isolated from the rat pleural cavity consist mainly of macrophages, mast cells, eosinophils, and lymphocytes. Isolated pleural cells labeled with [14C]arachidonic acid released appreciable amounts (approximately 12%) of radiolabel upon exposure to pharmacological concentrations of carrageenan

Phorbol myristate acetate-stimulated release of cyclooxygenase products in rat pleural cells: derivatization of prostaglandins with 9-anthryldiazomethane for fluorometric determination by high performance liquid chromatography.

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White cells were collected from the wash of rat pleural cavity after exsanguination. The incubation mixture of the pleural cells with 1 microM phorbol myristate acetate (PMA) was extracted with acidified ethanol and purified with a Sep-pak C18. The resultant fraction containing prostaglandins (PG)

Lipopolysaccharides, cytokines, and nitric oxide affect secretion of prostaglandins and leukotrienes by bovine mammary gland epithelial cells.

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The aims of this study were to determine the effects of lipopolysaccharides (LPS), tumor necrosis factor (TNF), interleukin 1 alpha (IL-1α), nitric oxide donor (NONOate), or the combination of TNF + IL-1α + NONOate on the following: (i) secretion of prostaglandin (PG)-F(2α), PGE(2), leukotriene

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