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  • 1
    Electronic Resource
    Electronic Resource
    S35b, a new phenylsulfonylfuroxan compound, inhibits thrombin-induced synthesis of platelet-activating factor and prostacyclin in human endothelial cells (1993)
    Springer
    Inflammation research 40 (1993), S. 157-165 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Endothelial cells (EC) produce platelet activating factor (PAF) and prostacyclin (PGI2) in response to inflammatory agents such as thrombin. Upon cell stimulation a calcium-dependent phospholipase A2 (PLA2) is activated which hydrolyzes a membrane phospholipid to yield 1-0-alkyl-2-lyso-sn-glycero-3-phospho-choline (lyso-PAF) and free arachidonic acid. Lyso-PAF is in turn converted into PAF by a specific acetyltransferase and arachidonic acid is metabolized via cyclic endoperoxides to PGI2. In the present study we report that S35b (4-methyl-3-phenylsulfonylfuroxan), an new phenyl-sulfonylfuroxan compound with potent antiaggregatory effect, inhibits thrombin-induced PAF synthesis and acetyltransferase activation as well as PGI2 production in human umbilical vein endothelial cells (HUVEC) in a concentration dependent way. Additionally, we show that S35b stimulates the production of cyclic GMP (cGMP) in HUVEC in a concentration- and time-dependent manner. At high concentration, S35b potentiates the cAMP increase induced by iloprost or forskolin without having a significant influence on cAMP level itself. Potentiation of cAMP increase during agonist-induced EC stimulation seems not to be important for the effect of S35b on cellular function as the compound is active in inhibiting PAF production when endothelial cells are pretreated with indomethacin to block PGI2 synthesis. The increase of cGMP evoked by S35b may account for the effect on endothelial cell function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01984055
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Correlation between nitric oxide synthase activity and reduced glutathione level in human and murine endothelial cells (1996)
    Springer
    Amino acids 10 (1996), S. 277-281 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; Nitric oxide ; Endothelial cells ; Glutathione ; Polyomavirus ; N-(2-Mercaptopropionyl)-glycine ; 1-Chloro-2,4-dinitrobenzene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The synthesis of nitric oxide (NO), detected as citrulline production, in human (HUVEC) and murine (tEnd.1) endothelial cells correlated with intracellular GSH. tEnd.1, which exhibited an intracellular GSH level 2.5-fold higher than HUVEC, showed a citrulline production (basally and after ionomycin stimulation) 5–8 times higher than human cells. Ionomycinelicited citrulline synthesis in tEnd.1 cells increased 2.4-fold after loading with GSH, and decreased dose-dependently after GSH depletion. Cell loading with N-(2-mercaptopropionyl)-glycine neither significantly increased citrulline production nor relieved the effect of GSH depletion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00807330
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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