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Gregory E Rice - One of the best experts on this subject based on the ideXlab platform.

  • contribution of type ii pla2 to prostaglandin formation a study using a type ii pla2 specific inhibitor sb 203347
    Prostaglandins & Other Lipid Mediators, 1999
    Co-Authors: Melinda J Munns, Roger G King, Gregory E Rice
    Abstract:

    Arachidonic acid (AA) mobilization by phospholipase A2 (PLA2) and subsequent prostaglandin synthesis is considered to be a Pivotal Event in inflammation. The purpose of this study was to assess the efficacy of a Type II PLA2 specific inhibitor, SB 203347, in reducing prostaglandin production in Type II PLA2-transfected Chinese hamster ovary (CHO) cells and in human placenta. In both experimental models uilised, Type II PLA2 represents the principal isozyme contributing to total PLA2 enzymatic activity. PLA2 enzymatic activity released into cell culture media and placental explant media was quantified by radiolabelled substrate assay [14C-phosphatidylethanolamine (PE)]. Immunoreactive prostaglandin F2α (PGF2α) concentrations were determined by radioimmunoassay. SB 203347 (at 0.1–10 μM final concentration) inhibited PLA2 enzymatic activity released by Zn++-activated CHO cells by up to 60% (P < 0.0001). The concentration of PGF2α present in culture media was concomitantly reduced by up to 90% (P < 0.0001). Similar results were observed for human placental explants. Treatment of human placental explants with SB 203347 (1 μM final concentration) significantly reduced PLA2 enzymatic activity recovered in media after 24 h incubation (P < 0.0001; n = 10). Incubation media PGF2α concentrations were also reduced by 60% (P < 0.00001). The addition of endogenous arachidonic acid (30 μM final concentration) significantly attenuated SB 203347-inhibition of PGF2α release (P < 0.01). The data obtained in this study are consistent with the hypothesis that Type II PLA2 contributes to the liberation of arachidonic acid for prostanoid formation in human placenta and in cells that abundantly express this isozyme.

Melinda J Munns - One of the best experts on this subject based on the ideXlab platform.

  • contribution of type ii pla2 to prostaglandin formation a study using a type ii pla2 specific inhibitor sb 203347
    Prostaglandins & Other Lipid Mediators, 1999
    Co-Authors: Melinda J Munns, Roger G King, Gregory E Rice
    Abstract:

    Arachidonic acid (AA) mobilization by phospholipase A2 (PLA2) and subsequent prostaglandin synthesis is considered to be a Pivotal Event in inflammation. The purpose of this study was to assess the efficacy of a Type II PLA2 specific inhibitor, SB 203347, in reducing prostaglandin production in Type II PLA2-transfected Chinese hamster ovary (CHO) cells and in human placenta. In both experimental models uilised, Type II PLA2 represents the principal isozyme contributing to total PLA2 enzymatic activity. PLA2 enzymatic activity released into cell culture media and placental explant media was quantified by radiolabelled substrate assay [14C-phosphatidylethanolamine (PE)]. Immunoreactive prostaglandin F2α (PGF2α) concentrations were determined by radioimmunoassay. SB 203347 (at 0.1–10 μM final concentration) inhibited PLA2 enzymatic activity released by Zn++-activated CHO cells by up to 60% (P < 0.0001). The concentration of PGF2α present in culture media was concomitantly reduced by up to 90% (P < 0.0001). Similar results were observed for human placental explants. Treatment of human placental explants with SB 203347 (1 μM final concentration) significantly reduced PLA2 enzymatic activity recovered in media after 24 h incubation (P < 0.0001; n = 10). Incubation media PGF2α concentrations were also reduced by 60% (P < 0.00001). The addition of endogenous arachidonic acid (30 μM final concentration) significantly attenuated SB 203347-inhibition of PGF2α release (P < 0.01). The data obtained in this study are consistent with the hypothesis that Type II PLA2 contributes to the liberation of arachidonic acid for prostanoid formation in human placenta and in cells that abundantly express this isozyme.

Roger G King - One of the best experts on this subject based on the ideXlab platform.

  • contribution of type ii pla2 to prostaglandin formation a study using a type ii pla2 specific inhibitor sb 203347
    Prostaglandins & Other Lipid Mediators, 1999
    Co-Authors: Melinda J Munns, Roger G King, Gregory E Rice
    Abstract:

    Arachidonic acid (AA) mobilization by phospholipase A2 (PLA2) and subsequent prostaglandin synthesis is considered to be a Pivotal Event in inflammation. The purpose of this study was to assess the efficacy of a Type II PLA2 specific inhibitor, SB 203347, in reducing prostaglandin production in Type II PLA2-transfected Chinese hamster ovary (CHO) cells and in human placenta. In both experimental models uilised, Type II PLA2 represents the principal isozyme contributing to total PLA2 enzymatic activity. PLA2 enzymatic activity released into cell culture media and placental explant media was quantified by radiolabelled substrate assay [14C-phosphatidylethanolamine (PE)]. Immunoreactive prostaglandin F2α (PGF2α) concentrations were determined by radioimmunoassay. SB 203347 (at 0.1–10 μM final concentration) inhibited PLA2 enzymatic activity released by Zn++-activated CHO cells by up to 60% (P < 0.0001). The concentration of PGF2α present in culture media was concomitantly reduced by up to 90% (P < 0.0001). Similar results were observed for human placental explants. Treatment of human placental explants with SB 203347 (1 μM final concentration) significantly reduced PLA2 enzymatic activity recovered in media after 24 h incubation (P < 0.0001; n = 10). Incubation media PGF2α concentrations were also reduced by 60% (P < 0.00001). The addition of endogenous arachidonic acid (30 μM final concentration) significantly attenuated SB 203347-inhibition of PGF2α release (P < 0.01). The data obtained in this study are consistent with the hypothesis that Type II PLA2 contributes to the liberation of arachidonic acid for prostanoid formation in human placenta and in cells that abundantly express this isozyme.

Franco Dallegri - One of the best experts on this subject based on the ideXlab platform.

  • is the carotid plaque rupture a Pivotal Event in stroke pathogenesis update on the role of the intraplaque inflammatory processes
    Current Vascular Pharmacology, 2015
    Co-Authors: Aldo Pende, Franco Dallegri
    Abstract:

    Abstract Stroke, a leading cause of death or disability worldwide, is frequently dependent on the rupture of carotid atherosclerotic plaques. It is therefore extremely important to study the mechanisms of formation, progression and Eventually rupture of the plaques. Vulnerability of the plaque, the intrinsic tendency to lose its integrity and consequently to induce a dramatic atherothrombotic or embolic Event, is still an elusive concept because many players are involved and the clinical picture is frequently the sum of different contrasting (pro-inflammatory and anti-inflammatory) phenomena. This review will discuss recent advancements in the comprehension of this topic. In particular inflammatory activation at the level of the carotid plaque will be described in the attempt to underline the main factors for the formation, the chronic persistence and the risk of rupture. Since these topics can be studied in humans only with plaque samples obtained following endarterectomy, research has tried to evaluate the role of different biomarkers which could be useful for the definition of the vulnerability of a carotid plaque, or, with more clinical relevance, of a patient; some recent results from our group will be discussed. A significant help for clinical decisions may also come from imaging tools, both well established ultrasound and more sophisticated options, such as magnetic resonance and positron emission tomography. This large amount of scientific information should allow the development of new therapeutic approaches for the effective prEvention of cerebrovascular Events.

Brendan Bell - One of the best experts on this subject based on the ideXlab platform.

  • Alternative Splicing of TAF6: Downstream Transcriptome Impacts and Upstream RNA Splice Control Elements
    PLoS ONE, 2014
    Co-Authors: Catherine Kamtchueng, Marie-eve Stébenne, Aurélie Delannoy, Emmanuelle Wilhelm, Hélène Léger, Arndt G. Benecke, Brendan Bell
    Abstract:

    The TAF6δ pathway of apoptosis can dictate life versus death decisions independently of the status of p53 tumor suppressor. TAF6δ is an inducible pro-apoptotic subunit of the general RNA polymerase II (Pol II) transcription factor TFIID. Alternative splice site choice of TAF6δ has been shown to be a Pivotal Event in triggering death via the TAF6δ pathway, yet nothing is currently known about the mechanisms that promote TAF6δ splicing. Furthermore the transcriptome impact of the gain of function of TAF6δ versus the loss of function of the major TAF6α splice form remains undefined. Here we employ comparative microarray analysis to show that TAF6δ drives a transcriptome profile distinct from that resulting from depletion of TAF6α. To define the cis-acting RNA elements responsible for TAF6δ alternative splicing we performed a mutational analysis of a TAF6 minigene system. The data point to several new RNA elements that can modulate TAF6δ and also reveal a role for RNA secondary structure in the selection of TAF6δ.