Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase
Summary P-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of prote...
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| Veröffentlicht in: | Thrombosis and haemostasis 2003-06, Vol.89 (6), p.1016-1023 |
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| container_title | Thrombosis and haemostasis |
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| creator | Libersan, Danielle Merhi, Yahye |
| description | Summary
P-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of protein kinase C (PKC) with chelerythrine reduced P-selectin expression by 66%, platelet/neutrophil binding, GPIIb/IIIa activation and aggregation (p |
| doi_str_mv | 10.1055/s-0037-1613403 |
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P-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of protein kinase C (PKC) with chelerythrine reduced P-selectin expression by 66%, platelet/neutrophil binding, GPIIb/IIIa activation and aggregation (p<0.05). Gö 6976, an inhibitor of the conventional PKCs (α and β), did not alter P-selectin expression. However, rottlerin inhibited by 50% its expression (p<0.05), but only at doses that interfere with the novel (є, η) and atypical (ζ) PKCs. Inhibition of protein tyrosine kinase (PTK) and phosphoinositide 3-kinase (PI3-K) did not significantly affect P-selectin expression. In conclusion, thrombin-induced P-selectin expression is PKC-sensitive, but PTK and PI3-K-insensitive. The novel є and η and atypical ζ, but not the conventional α and β and the novel θ PKCs, may be involved in this process.</description><identifier>ISSN: 0340-6245</identifier><identifier>EISSN: 2567-689X</identifier><identifier>DOI: 10.1055/s-0037-1613403</identifier><identifier>PMID: 12783114</identifier><identifier>CODEN: THHADQ</identifier><language>eng</language><publisher>Stuttgart: Schattauer Verlag für Medizin und Naturwissenschaften</publisher><subject>Biological and medical sciences ; Blood coagulation. Blood cells ; Blood Platelets - metabolism ; Blood Platelets - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Humans ; Isoenzymes - physiology ; Molecular and cellular biology ; P-Selectin - analysis ; P-Selectin - biosynthesis ; Phosphatidylinositol 3-Kinases ; Platelet ; Platelets and Blood Cells ; Protein Kinase C - physiology ; Protein-Tyrosine Kinases ; Secretory Vesicles - secretion ; Signal Transduction ; Thrombin</subject><ispartof>Thrombosis and haemostasis, 2003-06, Vol.89 (6), p.1016-1023</ispartof><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-484154e6d632dcb54dc5c18345d306f65e6a5c17ee8a6f1845aa890e33da8933</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.thieme-connect.de/products/ejournals/pdf/10.1055/s-0037-1613403.pdf$$EPDF$$P50$$Gthieme$$H</linktopdf><linktohtml>$$Uhttps://www.thieme-connect.de/products/ejournals/html/10.1055/s-0037-1613403$$EHTML$$P50$$Gthieme$$H</linktohtml><link.rule.ids>314,780,784,3008,3009,27915,27916,54550,54551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14855708$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12783114$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Libersan, Danielle</creatorcontrib><creatorcontrib>Merhi, Yahye</creatorcontrib><title>Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase</title><title>Thrombosis and haemostasis</title><addtitle>Thromb Haemost</addtitle><description>Summary
P-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of protein kinase C (PKC) with chelerythrine reduced P-selectin expression by 66%, platelet/neutrophil binding, GPIIb/IIIa activation and aggregation (p<0.05). Gö 6976, an inhibitor of the conventional PKCs (α and β), did not alter P-selectin expression. However, rottlerin inhibited by 50% its expression (p<0.05), but only at doses that interfere with the novel (є, η) and atypical (ζ) PKCs. Inhibition of protein tyrosine kinase (PTK) and phosphoinositide 3-kinase (PI3-K) did not significantly affect P-selectin expression. In conclusion, thrombin-induced P-selectin expression is PKC-sensitive, but PTK and PI3-K-insensitive. The novel є and η and atypical ζ, but not the conventional α and β and the novel θ PKCs, may be involved in this process.</description><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Blood Platelets - metabolism</subject><subject>Blood Platelets - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Isoenzymes - physiology</subject><subject>Molecular and cellular biology</subject><subject>P-Selectin - analysis</subject><subject>P-Selectin - biosynthesis</subject><subject>Phosphatidylinositol 3-Kinases</subject><subject>Platelet</subject><subject>Platelets and Blood Cells</subject><subject>Protein Kinase C - physiology</subject><subject>Protein-Tyrosine Kinases</subject><subject>Secretory Vesicles - secretion</subject><subject>Signal Transduction</subject><subject>Thrombin</subject><issn>0340-6245</issn><issn>2567-689X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqtkb1v1TAUxSMEoo_CyoiywISLHX8kYUNPfEmV6NCBzfJzbhSXxE59nUIX_nb8SGglJDYG68r3_HyPfVwUzxk9Y1TKN0go5TVhinFB-YNiV0lVE9W0Xx8WO5p7RFVCnhRPEK8oZUq08nFxwqq64YyJXfHzYjQJRkjlBcFcbXK-hB9zBEQX_NsywvXiIkzgU9mHWM4xJMjMN-cNQrl_XR6WVPqQ7pR0GwM6D3-Q46EhYF7OZyG5DkpOVvFp8ag3I8KzrZ4Wlx_eX-4_kfMvHz_v350TK0WbiGgEkwJUp3jV2YMUnZWWNVzIjlPVKwnK5EYN0BjVs0ZIY5qWAuddrpyfFq_WsfmO1wtg0pNDC-NoPIQFdc254uw3eLaCNr8BI_R6jm4y8VYzqo-Ba9THwPUWeD7wYpu8HCbo7vEt4Qy83ACD1ox9NN46vOdEI2VNm8yRlUuDy2nrq7BEnyP5t7FdebSDScksEO-GpiGG6ZCzRm18pwcDU8BkjnsbfMpfmYVoB3cD2iEuoHEG68yoJ-MXtNHNSXMhVHZx_9Glbqu_HTQO4bse0jTyX17q6bk</recordid><startdate>20030601</startdate><enddate>20030601</enddate><creator>Libersan, Danielle</creator><creator>Merhi, Yahye</creator><general>Schattauer Verlag für Medizin und Naturwissenschaften</general><general>Schattauer GmbH</general><general>Schattauer</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20030601</creationdate><title>Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase</title><author>Libersan, Danielle ; Merhi, Yahye</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-484154e6d632dcb54dc5c18345d306f65e6a5c17ee8a6f1845aa890e33da8933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Blood Platelets - metabolism</topic><topic>Blood Platelets - ultrastructure</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Isoenzymes - physiology</topic><topic>Molecular and cellular biology</topic><topic>P-Selectin - analysis</topic><topic>P-Selectin - biosynthesis</topic><topic>Phosphatidylinositol 3-Kinases</topic><topic>Platelet</topic><topic>Platelets and Blood Cells</topic><topic>Protein Kinase C - physiology</topic><topic>Protein-Tyrosine Kinases</topic><topic>Secretory Vesicles - secretion</topic><topic>Signal Transduction</topic><topic>Thrombin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Libersan, Danielle</creatorcontrib><creatorcontrib>Merhi, Yahye</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Thrombosis and haemostasis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Libersan, Danielle</au><au>Merhi, Yahye</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase</atitle><jtitle>Thrombosis and haemostasis</jtitle><addtitle>Thromb Haemost</addtitle><date>2003-06-01</date><risdate>2003</risdate><volume>89</volume><issue>6</issue><spage>1016</spage><epage>1023</epage><pages>1016-1023</pages><issn>0340-6245</issn><eissn>2567-689X</eissn><coden>THHADQ</coden><abstract>Summary
P-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of protein kinase C (PKC) with chelerythrine reduced P-selectin expression by 66%, platelet/neutrophil binding, GPIIb/IIIa activation and aggregation (p<0.05). Gö 6976, an inhibitor of the conventional PKCs (α and β), did not alter P-selectin expression. However, rottlerin inhibited by 50% its expression (p<0.05), but only at doses that interfere with the novel (є, η) and atypical (ζ) PKCs. Inhibition of protein tyrosine kinase (PTK) and phosphoinositide 3-kinase (PI3-K) did not significantly affect P-selectin expression. In conclusion, thrombin-induced P-selectin expression is PKC-sensitive, but PTK and PI3-K-insensitive. The novel є and η and atypical ζ, but not the conventional α and β and the novel θ PKCs, may be involved in this process.</abstract><cop>Stuttgart</cop><pub>Schattauer Verlag für Medizin und Naturwissenschaften</pub><pmid>12783114</pmid><doi>10.1055/s-0037-1613403</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Thieme Connect Journals |
| subjects | Biological and medical sciences Blood coagulation. Blood cells Blood Platelets - metabolism Blood Platelets - ultrastructure Fundamental and applied biological sciences. Psychology Humans Isoenzymes - physiology Molecular and cellular biology P-Selectin - analysis P-Selectin - biosynthesis Phosphatidylinositol 3-Kinases Platelet Platelets and Blood Cells Protein Kinase C - physiology Protein-Tyrosine Kinases Secretory Vesicles - secretion Signal Transduction Thrombin |
| title | Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase |
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