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    Activation of NF-kappa B transcription factor in human neutrophils by sulphatides and L-selectin cross-linking

    Turutin, Denis V, Kubareva, Elena A, Pushkareva, Marina A, Ullrich, Volker, Sud'Ina, Galina F
    FEBS letters, 11 February 2003, Vol.536(1-3), pp.241-5 [Peer Reviewed Journal]
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    Title: Activation of NF-kappa B transcription factor in human neutrophils by sulphatides and L-selectin cross-linking
    Author: Turutin, Denis V; Kubareva, Elena A; Pushkareva, Marina A; Ullrich, Volker; Sud'Ina, Galina F
    Subject: Depsipeptides ; Galactosylceramides -- Pharmacology ; L-Selectin -- Physiology ; Nf-Kappa B -- Metabolism ; Neutrophils -- Immunology ; Sulfoglycosphingolipids -- Pharmacology
    Description: Sulphated galactocerebroside (sulphatide) has been established as a ligand for L-selectin and shown to trigger intracellular signals in human neutrophils. We have found that sulphatide activated transcription factor NF-kappa B in human neutrophils in a concentration-dependent manner whereas non-sulphated galactocerebroside did not demonstrate such an effect. The activation was inhibitable by pretreatment with primary monoclonal anti-L-selectin antibody (clone LAM1-116). Binding of the primary antibody to L-selectin was insufficient to induce NF-kappa B activation but cross-linking of L-selectin with a secondary antibody was effective. alpha-Chymotrypsin, the agent known to shed L-selectin, activated NF-kappa B by itself. The response to sulphatides was inhibited by jasplakinolide, an actin-polymerising agent known to downregulate surface expression of L-selectin, Fc gamma RIIIb, CD43 and CD44. Recently we have reported that sulphatide stimulated the attachment of human neutrophils to collagen...
    Is part of: FEBS letters, 11 February 2003, Vol.536(1-3), pp.241-5
    Identifier: 0014-5793 (ISSN); 12586371 Version (PMID)

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    Endothelium-leukocyte interactions under the influence of the superoxide-nitrogen monoxide system

    Galkina, Svetlana I, Dormeneva, Elena V, Bachschmid, Marcus, Pushkareva, Marina A, Sud'Ina, Galina F, Ullrich, Volker
    Medical science monitor : international medical journal of experimental and clinical research, September 2004, Vol.10(9), pp.BR307-16 [Peer Reviewed Journal]
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    Title: Endothelium-leukocyte interactions under the influence of the superoxide-nitrogen monoxide system
    Author: Galkina, Svetlana I; Dormeneva, Elena V; Bachschmid, Marcus; Pushkareva, Marina A; Sud'Ina, Galina F; Ullrich, Volker
    Subject: Cell Adhesion -- Physiology ; Endothelial Cells -- Metabolism ; Endothelium, Vascular -- Cytology ; Neutrophils -- Metabolism ; Nitric Oxide Donors -- Pharmacology ; Xanthine Oxidase -- Metabolism
    Description: The production of reactive oxygen and nitrogen species contributes to the development of vascular injury and inflammation. The present study was focused on neutrophil adhesion to monolayers of primary endothelial cells in the presence of NO donors, a superoxide anion producing system (hypoxanthine-xanthine oxidase, HX-XO) and peroxynitrite under static conditions. Phase contrast and scanning electron microscopy was used to study endothelial monolayer integrity. Neutrophil attachment to surfaces was quantified by myeloperoxidase assay in parallel with microscopic assessment of cell count. In the presence of HX-XO, the endothelial monolayer was destroyed and neutrophil adhesion to the endothelium and exposed subendothelial matrix was drastically increased. Neutrophil attachment was mainly CD18 integrins-mediated and depended on P-selectin, but not on the endothelial adhesion molecules E-selectin, ICAM-1 or PECAM-1. The endothelial monolayer damage caused by HX-XO was a result of superoxide-induced oxidative destruction, since tocopherol and superoxide dismutase protected the monolayer and reduced the number of attached PMNs. Together with the superoxide-producing system, nitric oxide donor diethylamine NONOate also protected the endothelium monolayer from disruption and reduced the number of PMNs attached. Additional exogenous peroxynitrite slightly enhanced neutrophil adhesion to endothelial cells, without monolayer injury. Superoxide anions induced endothelium injury and neutrophil attachment, but nitric oxide played a protective role.
    Is part of: Medical science monitor : international medical journal of experimental and clinical research, September 2004, Vol.10(9), pp.BR307-16
    Identifier: 1234-1010 (ISSN); 15328475 Version (PMID)

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    Cholesterol and its anionic derivatives inhibit 5-lipoxygenase activation in polymorphonuclear leukocytes and MonoMac6 cells

    Aleksandrov, Dmitry A, Zagryagskaya, Anna N, Pushkareva, Marina A, Bachschmid, Markus, Peters-Golden, Marc, Werz, Oliver, Steinhilber, Dieter, Sud'Ina, Galina F
    The FEBS journal, February 2006, Vol.273(3), pp.548-57 [Peer Reviewed Journal]
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    Title: Cholesterol and its anionic derivatives inhibit 5-lipoxygenase activation in polymorphonuclear leukocytes and MonoMac6 cells
    Author: Aleksandrov, Dmitry A; Zagryagskaya, Anna N; Pushkareva, Marina A; Bachschmid, Markus; Peters-Golden, Marc; Werz, Oliver; Steinhilber, Dieter; Sud'Ina, Galina F
    Subject: Lipoxygenase Inhibitors ; Arachidonate 5-Lipoxygenase -- Metabolism ; Cholesterol -- Analogs & Derivatives ; Neutrophils -- Metabolism
    Description: 5-Lipoxygenase (5-LO) is the key enzyme in the biosynthesis of leukotrienes (LTs), biological mediators of host defense reactions and of inflammatory diseases. While the role of membrane binding in the regulation of 5-LO activity is well established, the effects of lipids on cellular activity when added to the medium has not been characterized. Here, we show such a novel function of the most abundant sulfated sterol in human blood, cholesterol sulfate (CS), to suppress LT production in human polymorphonuclear leukocytes (PMNL) and Mono Mac6 cells. We synthesized another anionic lipid, cholesterol phosphate, which demonstrated a similar capacity in suppression of LT synthesis in PMNL. Cholesteryl acetate was without effect. Cholesterol increased the effect of CS on 5-LO product synthesis. CS and cholesterol also inhibited arachidonic acid (AA) release from PMNL. Addition of exogenous AA increased the threshold concentration of CS required to inhibit LT synthesis. The effect of cholesterol...
    Is part of: The FEBS journal, February 2006, Vol.273(3), pp.548-57
    Identifier: 1742-464X (ISSN); 16420478 Version (PMID)