calcimycin and diethyl-maleate

calcimycin has been researched along with diethyl-maleate* in 3 studies

Other Studies

3 other study(ies) available for calcimycin and diethyl-maleate

ArticleYear
Effect of intracellular glutathione on the production of prostaglandin D2 in RBL-2H3 cells oxidized by tert-butyl hydroperoxide.
    Journal of biochemistry, 1999, Volume: 125, Issue:1

    The liberation of arachidonic acid and the production of prostaglandin D2 (PGD2) were significantly influenced by peroxide and the level of intracellular glutathione (GSH). The productions of free arachidonic acid and PGD2 in RBL-2H3 cells were enhanced considerably by exposure to tert-butyl hydroperoxide (t-BHP). The liberation of arachidonic acid induced by t-BHP was not inhibited by EGTA. The productions of PGD2 and arachidonic acid induced by t-BHP were significantly facilitated by the depletion of intracellular GSH using buthionine sulfoximine (BSO) or diethyl maleate (DEM), although the depletion of GSH had no effect on the production of PGD2 induced by A23187. t-BHP failed to activate the conversion of free arachidonic acid to PGD2, since the formation of PGD2 from exogenously added arachidonic acid was not enhanced by treatment with t-BHP. The level of lipid hydroperoxides in t-BHP-treated cells was significantly elevated by treatment with DEM. These results suggest that hydroperoxides increase the free arachidonic acid available for the synthesis of PGD2 by activating phospholipase A2 (PLA2) and that the depletion of GSH by DEM accelerates the activation of PLA2 by raising peroxide levels in cells. Thus, the observed alterations in GSH levels are large enough to cause increased PGD2 synthesis in RBL-2H3 cells exposed to oxidative stress.

    Topics: Animals; Arachidonic Acid; Buthionine Sulfoximine; Calcimycin; Cyclooxygenase 1; Glutathione; Intramolecular Oxidoreductases; Ionophores; Isoenzymes; Leukemia, Experimental; Lipocalins; Maleates; Membrane Proteins; Oxidants; Oxidation-Reduction; Phospholipids; Prostaglandin D2; Prostaglandin-Endoperoxide Synthases; Rats; tert-Butylhydroperoxide; Tumor Cells, Cultured

1999
Effects of diethyl maleate (DEM), a glutathione depletor, on prostaglandin synthesis in the isolated perfused spleen of rabbits.
    Archives of toxicology, 1990, Volume: 64, Issue:2

    To investigate the role of glutathione (GSH) on prostaglandin (PG) synthesis, isolated rabbit spleens were perfused with Tyrode's solution with or without the addition of diethyl maleate (DEM) in concentrations up to 1 mM. In the absence of DEM, PG synthesis was stimulated by the Ca2+ ionophore A23187 (20 nmole) or arachidonate (0.4 mumole). Prostaglandin (PG) E2 was a major product, accounting for 60-70% of the total cyclooxygenase products. Small amounts of PGF2 alpha, 6-keto-PGF1 alpha, PGD2 and thromboxane (Tx) B2 were also produced. When DEM was added to the perfusion medium, GSH content decreased dose-dependently with increasing DEM concentration. Lactate dehydrogenase activity was not detected in the venous effluent, indicating that DEM depleted intrasplenic GSH without causing any lysis of cellular membranes. A23187-induced production of PGs and of Tx was decreased with increasing concentrations of DEM up to 0.5 mM, whereas at 1.0 mM DEM, these products showed a tendency to increase as compared with levels at 0.5 mM DEM. However, this increase was only significant for TxB2, which returned to levels obtained in the absence of DEM. DEM 1 mM did not cause cell lysis, but it appears to perturb the cell membrane to a degree similar to that which occurs with stimulation of phospholipase A2. The small but significant increase of TxB2 with 1.0 mM DEM could be a result of decreased PGE2 isomerase activity. Perfusion with arachidonate gave virtually identical results: 1.0 mM DEM attenuated the production of all prostanoids except for TxB2 as compared with untreated controls. These results suggest that GSH contributes to the regulation and/or maintenance of PGs synthesis.

    Topics: Animals; Arachidonic Acid; Arachidonic Acids; Calcimycin; Glutathione; In Vitro Techniques; Isotonic Solutions; L-Lactate Dehydrogenase; Male; Maleates; Oxidation-Reduction; Perfusion; Prostaglandin-Endoperoxide Synthases; Prostaglandins; Rabbits; Radioimmunoassay; Spleen

1990
Inhibitory effect of salicylate on 2,4-dinitrophenol and diethyl maleate in isolated rat intestinal epithelial cells.
    Biochimica et biophysica acta, 1988, Jun-08, Volume: 970, Issue:1

    Studies on the mechanism of chemically induced intestinal epithelial injury were carried out using isolated, rat small intestinal epithelial cells. Compounds such as 2,4-dinitrophenol (DNP) and diethyl maleate (DEM), caused NADH loss, an increase in cytosolic Ca2+ concentration and protein thiol loss. Further, these compounds accelerated cell aggregation and decreased cell viability. Calmodulin antagonists inhibited protein thiol loss induced by either of the compound, inhibited cell aggregation and prolonged cell viability, but did not influence NADH loss. It has been reported that the calmodulin-binding protein may regulate cytoskeletal activity. Therefore, the inhibition of protein thiol loss by calmodulin antagonist may be due to a dissociation of calmodulin-binding proteins from cytoskeletal elements. Salicylate also inhibited protein thiol loss induced by DNP and DEM, and inhibited cell aggregation. However, salicylate may have a direct effect in reducing the cytosolic free Ca2+ concentration by complexation and subsequent facilitated release of Ca2+ from cells. Further, in the present study, the induction of cell aggregation may be caused by the appearance of specific sites on the cell membrane surface to which arsenazo III could adsorb, since adsorption of arsenazo III to the isolated epithelial cells seemed to correlate with increased cell aggregation.

    Topics: Animals; Calcimycin; Calcium; Cell Aggregation; Cell Survival; Chlorpromazine; Dinitrophenols; Dithiothreitol; Drug Interactions; In Vitro Techniques; Intestinal Mucosa; Kinetics; Maleates; NAD; Rats; Salicylates; Salicylic Acid; Solubility; Sulfhydryl Compounds; Sulfonamides

1988