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  • 1
    Digitale Medien
    Digitale Medien
    Induction of High-Affinity Interleukin 2 Receptors on Human T Lymphocytes (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 30 (1989), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The relationship between free cytoplasmic calcium, activation of protein kinase C (PKC) and expression of high-affinity interleukin 2 receptors (HA-IL-2R) on human T lymphocytes was studied. Induction of HA-IL-2R by phytohaemagglutinin (PHA) was associated with an increase in free cytoplasmic calcium and a transient increase in membrane-associated PKC. However, whereas addition of EGTA inhibited induction of receptors by PHA, addition of the PKC-inhibitor H7 did not. 12-o-tetradecanoyl-phorbol-13-acetate (PMA) and 1-oleoyl-2-acetyl-racglycerol (OAG) were both found to activate and translocate PKC. However, only PMA induced expression of HA-IL-2R. Not surprisingly, the effect of PMA was independent of extracellular calcium, but was inhibited by H7. Furthermore, a correlation between the number of HA-IL-2R and free cytoplasmic calcium upon stimulation with ionomycin was observed. Associated with the rise in intracellular calcium, the ionophore caused a slight increase in membrane-associat4ed PKC. Also, addition of 117 inhibited expression of HA-IL-2R. Finally, OAG and ionomycin acted synergistically on expression of HA-IL-2R. In conclusion, induction of HA-IL-2R requires at least two different signals and neither activation of PKC nor an increase in free cytoplasmic calcium is sufficient. However, these two signals may act synergistically. There is evidence for both a PKC- and calcium-independent pathway.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01213.x
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  • 2
    Digitale Medien
    Digitale Medien
    Translocation of Protein Kinase C to Subcellular Fractions of Human Neutrophils (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 29 (1989), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The subcellular localization of protein kinase C in unstimulated human neutrophils and neutrophils stimulated by phorbol-myristate-acetate (PMA), 1-oleoyl-2-acetyl-rac-glycerol (OAG), and ionomycin was investigated in subcellular tractions obtained by nitrogen cavitation and Percoll density gradient centrifugation. Protein kinase C was found to he localized mainly in the cytosol in unstimulated cells, whereas significant translocation to fractions containing the plasma membrane was observed after stimulation by PMA, OAG, and ionomycin. At the same time, phospholipid-insensitive protein kinase activity appeared in the cytosol and the plasma membrane fractions. To determine whether binding of protein kinase C occurred to the plasma membrane or to intracellular membranes that had translocated to the plasma membrane, we investigated the ability of isolated azurophil, specific and secretory granules, and plasma membrane vesicles to bind protein kinase C in response to addition of PMA and OAG. Only fractions containing plasma membranes and secretory granules were able to bind protein kinase C. The observation explains the selective activation of plasma membrane structures by protein kinase C.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01140.x
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  • 3
    Digitale Medien
    Digitale Medien
    Modulation of High-Affinity Interleukin 2 Receptors on Activated Human T Lymphocytes by Activators of Protein Kinase C (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 28 (1988), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Phorbol myristate acetate (PMA) and 1-oleoyl-2-acetyl-rac-glycerol (OAG) are shown to induce a rapid (within 30 min) down-regulation of the capacity of activated human T lymphocytes to bind interleukin 2. This was associated with a manifold increase in membrane-associated protein kinase C, whereas no change in free cytoplasmic calcium was observed. In contrast, a 10-fold increase in free cytoplasmic calcium by ionomycin had no effect on interleukin 2 binding or sub-cellular distribution of protein kinase C. The reduction of interleukin 2 binding was caused by a decreased number of high-affinity interleukin 2 receptors, whereas the affinity of the remaining receptors was unchanged. However, PMA and OAG had no effect on the rate of initialization of the interleukin receptor. These data suggest that activation of protein kinase C. but not an increase in free cytoplasmic calcium, leads to a rapid decrease in the number of high-affinity interleukin 2 receptors on activated human T lymphocytes. However, the mechanism and biological importance of this phenomenon have to be further elucidated.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1988.tb02428.x
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  • 4
    Digitale Medien
    Digitale Medien
    Effect of auranofin on eicosanoids and protein kinase C in human neutrophils (1989)
    Springer
    Inflammation research 28 (1989), S. 121-129 
    Details
    ISSN: 1420-908X
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Auranofin (AF), a lipophilic chrysotherapeutic agent, was investigated for its effect on the formation of lipoxygenase products and the activity of protein kinase C in human neutrophils. We have previously shown that inhibition of LTB4 formation by 5-lipoxygenase (5-LO) inhibitors is intimately associated with a marked increased in 15-HETE in excess of arachidonic acid. The calcium- and phospholipiddependent protein kinase, protein kinase C, is activated in FMLP- and A23187-stimulated neutrophils, is hypothesized to stimulate superoxide generation, and plays an essential role in eicosanoid production. AF dose-dependently inhibited the generation of leukotriene B4 (LTB4) in FMLP-stimulated neutrophils, the ID50 was approximately 4.5 μg/ml. Unlike known 5-LO inhibitors, AF did not enhance the production of 15-HETE. In neutrophils stimulated with the calcium ionophore, A23187, AF did not inhibit the generation of LTB4 nor did AF change the 15-HETE levels. AF inhibited superoxide generation in FMLP-stimulated neutrophils dose-dependently, but did not change the activation of protein kinase C in the cells. We therefore conclude, that AF inhibition of LTB4 production in neutrophils is different from 5-lipoxygenase inhibitors and is elicited at a step distal to protein kinase C activation.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02022992
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