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dc.contributor.authorGeirsson, A
dc.contributor.authorHalldorsson, H
dc.contributor.authorMagnusdottir, K
dc.contributor.authorKjeld, M
dc.contributor.authorThorgeirsson, G
dc.date.accessioned2010-03-04T13:09:08Z
dc.date.available2010-03-04T13:09:08Z
dc.date.issued1998-10-01
dc.date.submitted2010-03-04
dc.identifier.citationJ. Cell. Physiol. 1998, 177(1):103-8en
dc.identifier.issn0021-9541
dc.identifier.pmid9731750
dc.identifier.doi10.1002/(SICI)1097-4652(199810)177:1<103::AID-JCP11>3.0.CO;2-E
dc.identifier.urihttp://hdl.handle.net/2336/93640
dc.descriptionTo access publisher full text version of this article. Please click on the hyperlink in Additional Links fielden
dc.description.abstractLeukotriene C4 is an arachidonic acid metabolite and an important mediator of inflammation and anaphylaxis that is known to induce production of prostacyclin in endothelial cells. The goal of this study was to examine the signal transduction mechanisms activated by leukotriene C4 stimulation. Formation of inositol phosphates was measured to determine the activation of phospholipase C and pertussis toxin was used to explore the role of G-proteins. Additionally, we evaluated the role of protein kinase C in these events, especially whether there was an interaction between pertussis toxin mediated effects and the activity of protein kinase C. Leukotriene C4 induced a dose- and time-dependent formation of inositol phosphates and prostacyclin. The response to leukotriene C4 was greater than the response to leukotriene D4 even after treatment with L-serine borate complex, suggesting the presence of a specific leukotriene C4 receptor. Exposure to pertussis toxin potentiated, time-dependently, the leukotriene C4 induced formation of inositol phosphates and prostacyclin through a mechanism which was altered by manipulation of protein kinase C activity. The exact mechanism is not clear but our results are consistent with a postulated dual mechanism of phospholipase C control, in which leukotriene C4 induced stimulation is attenuated by a pertussis toxin sensitive G-protein.
dc.language.isoenen
dc.publisherWiley-Lissen
dc.relation.urlhttp://dx.doi.org/10.1002/(SICI)1097-4652(199810)177:1<103::AID-JCP11>3.0.CO;2-Een
dc.subject.meshBoratesen
dc.subject.meshCells, Cultureden
dc.subject.meshEndothelium, Vascularen
dc.subject.meshEpoprostenolen
dc.subject.meshHumansen
dc.subject.meshInositol Phosphatesen
dc.subject.meshLeukotriene C4en
dc.subject.meshLeukotriene D4en
dc.subject.meshPertussis Toxinen
dc.subject.meshProtein Kinase Cen
dc.subject.meshReceptors, Leukotrieneen
dc.subject.meshSerineen
dc.subject.meshUmbilical Veinsen
dc.subject.meshVirulence Factors, Bordetellaen
dc.titlePotentiating effects of pertussis toxin on leukotriene C4 induced formation of inositol phosphate and prostacyclin in human umbilical vein endothelial cells.en
dc.typeArticleen
dc.contributor.departmentDepartment of Pharmacology, University of Iceland, Reykjavik.en
dc.identifier.journalJournal of cellular physiologyen
html.description.abstractLeukotriene C4 is an arachidonic acid metabolite and an important mediator of inflammation and anaphylaxis that is known to induce production of prostacyclin in endothelial cells. The goal of this study was to examine the signal transduction mechanisms activated by leukotriene C4 stimulation. Formation of inositol phosphates was measured to determine the activation of phospholipase C and pertussis toxin was used to explore the role of G-proteins. Additionally, we evaluated the role of protein kinase C in these events, especially whether there was an interaction between pertussis toxin mediated effects and the activity of protein kinase C. Leukotriene C4 induced a dose- and time-dependent formation of inositol phosphates and prostacyclin. The response to leukotriene C4 was greater than the response to leukotriene D4 even after treatment with L-serine borate complex, suggesting the presence of a specific leukotriene C4 receptor. Exposure to pertussis toxin potentiated, time-dependently, the leukotriene C4 induced formation of inositol phosphates and prostacyclin through a mechanism which was altered by manipulation of protein kinase C activity. The exact mechanism is not clear but our results are consistent with a postulated dual mechanism of phospholipase C control, in which leukotriene C4 induced stimulation is attenuated by a pertussis toxin sensitive G-protein.


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