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Article: Endothelium-derived relaxing factor inhibits thrombin-induced platelet aggregation by inhibiting platelet phospholipase C

TitleEndothelium-derived relaxing factor inhibits thrombin-induced platelet aggregation by inhibiting platelet phospholipase C
Authors
Issue Date1992
PublisherAmerican Society of Hematology. The Journal's web site is located at http://bloodjournal.hematologylibrary.org/
Citation
Blood, 1992, v. 79 n. 1, p. 110-116 How to Cite?
AbstractEndothelium-derived relaxing factor (EDRF) inhibits platelet function, but the mechanism underlying this inhibitory effect is not known. To examine this, cultured acetylsalicylic acid (ASA)-treated endothelial cells (EC) from bovine aorta (BAEC) or from human umbilical vein (HUVEC) were incubated with washed, ASA-treated human platelets. Incubation of platelets with either BAEC or HUVEC resulted in inhibition of thrombin-induced platelet aggregation that was dependent on the number of EC added. This effect was potentiated by superoxide dismutase and reversed by treating EC with N(G)-nitro-L-arginine or by treating platelets with methylene blue, indicating that the inhibition of platelet aggregation was due to the release of EDRF by EC. EC significantly blocked the thrombin stimulated breakdown of phosphatidylinositol- 4,5,-bisphosphate (PIP2) and the production of phosphatidic acid in [32P]orthophosphate-labeled platelets and of inositol trisphosphate in [3H]myoinositol-labeled platelets. In addition, the thrombin-mediated activation of protein kinase C (PKC) and phosphorylation of myosin light chain were inhibited in the presence of EC. Finally, thrombin stimulated an increase in cytosolic ionized calcium concentration ([Ca2+]i) in fura2-loaded platelets that was abolished by concentrations of EC which also blocked thrombin-induced aggregation. These data indicate that EDRF blocks thrombin-induced platelet aggregation by inhibiting the activation of PIP2-specific phospholipase C and thereby suppressing the consequent activation of PKC and the mobilization of [Ca2+]i.
Persistent Identifierhttp://hdl.handle.net/10722/171056
ISSN
2015 Impact Factor: 11.841
2015 SCImago Journal Rankings: 6.395
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorDurante, Wen_US
dc.contributor.authorKroll, MHen_US
dc.contributor.authorVanhoutte, PMen_US
dc.contributor.authorSchafer, AIen_US
dc.date.accessioned2012-10-30T06:12:01Z-
dc.date.available2012-10-30T06:12:01Z-
dc.date.issued1992en_US
dc.identifier.citationBlood, 1992, v. 79 n. 1, p. 110-116en_US
dc.identifier.issn0006-4971en_US
dc.identifier.urihttp://hdl.handle.net/10722/171056-
dc.description.abstractEndothelium-derived relaxing factor (EDRF) inhibits platelet function, but the mechanism underlying this inhibitory effect is not known. To examine this, cultured acetylsalicylic acid (ASA)-treated endothelial cells (EC) from bovine aorta (BAEC) or from human umbilical vein (HUVEC) were incubated with washed, ASA-treated human platelets. Incubation of platelets with either BAEC or HUVEC resulted in inhibition of thrombin-induced platelet aggregation that was dependent on the number of EC added. This effect was potentiated by superoxide dismutase and reversed by treating EC with N(G)-nitro-L-arginine or by treating platelets with methylene blue, indicating that the inhibition of platelet aggregation was due to the release of EDRF by EC. EC significantly blocked the thrombin stimulated breakdown of phosphatidylinositol- 4,5,-bisphosphate (PIP2) and the production of phosphatidic acid in [32P]orthophosphate-labeled platelets and of inositol trisphosphate in [3H]myoinositol-labeled platelets. In addition, the thrombin-mediated activation of protein kinase C (PKC) and phosphorylation of myosin light chain were inhibited in the presence of EC. Finally, thrombin stimulated an increase in cytosolic ionized calcium concentration ([Ca2+]i) in fura2-loaded platelets that was abolished by concentrations of EC which also blocked thrombin-induced aggregation. These data indicate that EDRF blocks thrombin-induced platelet aggregation by inhibiting the activation of PIP2-specific phospholipase C and thereby suppressing the consequent activation of PKC and the mobilization of [Ca2+]i.en_US
dc.languageengen_US
dc.publisherAmerican Society of Hematology. The Journal's web site is located at http://bloodjournal.hematologylibrary.org/en_US
dc.relation.ispartofBlooden_US
dc.subject.meshAnimalsen_US
dc.subject.meshAortaen_US
dc.subject.meshArginine - Analogs & Derivatives - Pharmacologyen_US
dc.subject.meshAspirin - Pharmacologyen_US
dc.subject.meshBlood Platelets - Drug Effects - Enzymologyen_US
dc.subject.meshCalcium - Blooden_US
dc.subject.meshCattleen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshEndothelium, Vascular - Drug Effects - Physiologyen_US
dc.subject.meshHumansen_US
dc.subject.meshNitric Oxide - Pharmacology - Secretionen_US
dc.subject.meshNitroarginineen_US
dc.subject.meshPhosphatidylinositols - Blooden_US
dc.subject.meshPlatelet Aggregation - Drug Effectsen_US
dc.subject.meshPlatelet Aggregation Inhibitors - Pharmacologyen_US
dc.subject.meshSuperoxide Dismutase - Pharmacologyen_US
dc.subject.meshThrombin - Pharmacologyen_US
dc.subject.meshType C Phospholipases - Antagonists & Inhibitorsen_US
dc.subject.meshUmbilical Veinsen_US
dc.titleEndothelium-derived relaxing factor inhibits thrombin-induced platelet aggregation by inhibiting platelet phospholipase Cen_US
dc.typeArticleen_US
dc.identifier.emailVanhoutte, PM:vanhoutt@hku.hken_US
dc.identifier.authorityVanhoutte, PM=rp00238en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid1309423-
dc.identifier.scopuseid_2-s2.0-0026593432en_US
dc.identifier.volume79en_US
dc.identifier.issue1en_US
dc.identifier.spage110en_US
dc.identifier.epage116en_US
dc.identifier.isiWOS:A1992GX61400014-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDurante, W=7006946922en_US
dc.identifier.scopusauthoridKroll, MH=7102187905en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US
dc.identifier.scopusauthoridSchafer, AI=7202243976en_US

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