Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide
Summary We have addressed the role of Rho-kinase in the different steps of thrombin receptor agonist peptide (TRAP) -induced platelet activation. Interestingly, under physiological conditions, incubation of platelets with increasing concentrations of the specific Rho-kinase inhibitor Y-27632 resulte...
Gespeichert in:
| Veröffentlicht in: | Thrombosis and haemostasis 2001-03, Vol.85 (3), p.514-20 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 20 |
|---|---|
| container_issue | 3 |
| container_start_page | 514 |
| container_title | Thrombosis and haemostasis |
| container_volume | 85 |
| creator | Missy, K. Plantavid, M. Pacaud, P. Viala, C. Chap, H. Payrastre, B. |
| description | Summary
We have addressed the role of Rho-kinase in the different steps of thrombin receptor agonist peptide (TRAP) -induced platelet activation. Interestingly, under physiological conditions, incubation of platelets with increasing concentrations of the specific Rho-kinase inhibitor Y-27632 resulted in a dose-dependent reversion of the aggregation induced by 10 μM TRAP, without affecting serotonin secretion. Addition of Y-27632 after three minutes of TRAP stimulation, when the maximal aggregation was reached, resulted in a rapid disaggregation of platelets. Accordingly, the early peak of myosin light chain (MLC) phosphorylation induced by TRAP was not affected by Y-27632 but its sustained phosphorylation, observed during the irreversible phase of aggregation, was dependent of Rho-kinase activity. The rapid decrease in MLC phosphorylation upon Y-27632 treatment correlated well with the specific disappearance of myosin heavy chain from the cytoskeleton and preceded platelet disaggregation. Finally, we provide evidence that secreted ADP, known to play a key role in TRAP-induced irreversible phase of aggregation, was involved in the sustained MLC phosphorylation through Rho-kinase and could be replaced by epinephrine. |
| doi_str_mv | 10.1055/s-0037-1615614 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_thiem</sourceid><recordid>TN_cdi_thieme_journals_10_1055_s_0037_1615614</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77057007</sourcerecordid><originalsourceid>FETCH-LOGICAL-c547t-a61498dfde6662caade7a2da442e80581238618c86aeab9de879cca20104cf123</originalsourceid><addsrcrecordid>eNqtkV-L1DAUxYso7jj66qMEBN-6Jv2Tto_DsurAisOq4Fu4k95Os7ZJzU1H5kv4mc3sDCsIvvkUkvO755JzkuSl4JeCl-VbSjnPq1RIUUpRPEoWWSmrVNbNt8fJgucFT2VWlBfJM6I7zoUsmvJpciFEzqs6KxbJr9vepd-NBUK2Jra2ezfssWXGstAj-zxTAGPjw6Z3NPXOHwYIxlnmOvbx4ChyYNt7du097tGT2Q7INhHDAQNb7XYed6eZtW1nHb22B7ZZ3Qq20sHso2R3bINTMC0-T550MBC-OJ_L5Ou76y9XH9KbT-_XV6ubVJdFFVKIf23qtmtRSplpgBYryFooigxrXtYiy2spal1LQNg2LdZVozVkXPBCd1FdJm9OvpN3P2akoEZDGocBLLqZVFXxsuK8iuDlCdTeEXns1OTNCP6gBFfHBhSpYwPq3EAceHV2nrcjtn_wc-QReH0GgDQMnQerDT1wTSbzaLhM0hMVeoMjqjs3exsT-fdafeJJ9xACzOgfLEPv3biNXZGKXakecHSx1uNdOxvQhih43Zs9KkM0o6IJtYFBjWBn0t5MQWXVfRrmP26pZf33BkW9-6n6MA75b_-A7to</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77057007</pqid></control><display><type>article</type><title>Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide</title><source>MEDLINE</source><source>Thieme Connect Journals</source><creator>Missy, K. ; Plantavid, M. ; Pacaud, P. ; Viala, C. ; Chap, H. ; Payrastre, B.</creator><creatorcontrib>Missy, K. ; Plantavid, M. ; Pacaud, P. ; Viala, C. ; Chap, H. ; Payrastre, B.</creatorcontrib><description>Summary
We have addressed the role of Rho-kinase in the different steps of thrombin receptor agonist peptide (TRAP) -induced platelet activation. Interestingly, under physiological conditions, incubation of platelets with increasing concentrations of the specific Rho-kinase inhibitor Y-27632 resulted in a dose-dependent reversion of the aggregation induced by 10 μM TRAP, without affecting serotonin secretion. Addition of Y-27632 after three minutes of TRAP stimulation, when the maximal aggregation was reached, resulted in a rapid disaggregation of platelets. Accordingly, the early peak of myosin light chain (MLC) phosphorylation induced by TRAP was not affected by Y-27632 but its sustained phosphorylation, observed during the irreversible phase of aggregation, was dependent of Rho-kinase activity. The rapid decrease in MLC phosphorylation upon Y-27632 treatment correlated well with the specific disappearance of myosin heavy chain from the cytoskeleton and preceded platelet disaggregation. Finally, we provide evidence that secreted ADP, known to play a key role in TRAP-induced irreversible phase of aggregation, was involved in the sustained MLC phosphorylation through Rho-kinase and could be replaced by epinephrine.</description><identifier>ISSN: 0340-6245</identifier><identifier>EISSN: 2567-689X</identifier><identifier>DOI: 10.1055/s-0037-1615614</identifier><identifier>PMID: 11307824</identifier><identifier>CODEN: THHADQ</identifier><language>eng</language><publisher>Stuttgart: Schattauer Verlag für Medizin und Naturwissenschaften</publisher><subject>Adenosine Diphosphate - pharmacology ; Adenosine Diphosphate - secretion ; Amides - pharmacology ; Biological and medical sciences ; Blood coagulation. Blood cells ; Blood Platelets - cytology ; Blood Platelets - drug effects ; Cytoskeleton - drug effects ; Cytoskeleton - metabolism ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; Humans ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Molecular and cellular biology ; Myosins - drug effects ; Myosins - metabolism ; Peptide Fragments - pharmacology ; Phosphorylation ; Platelet ; Platelet Aggregation - drug effects ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Serine-Threonine Kinases - physiology ; Pyridines - pharmacology ; Review Article ; rho-Associated Kinases</subject><ispartof>Thrombosis and haemostasis, 2001-03, Vol.85 (3), p.514-20</ispartof><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c547t-a61498dfde6662caade7a2da442e80581238618c86aeab9de879cca20104cf123</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-0037-1615614.pdf$$EPDF$$P50$$Gthieme$$H</linktopdf><linktohtml>$$Uhttps://www.thieme-connect.de/products/ejournals/html/10.1055/s-0037-1615614$$EHTML$$P50$$Gthieme$$H</linktohtml><link.rule.ids>314,780,784,3017,3018,27924,27925,54559,54560</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=926300$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11307824$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Missy, K.</creatorcontrib><creatorcontrib>Plantavid, M.</creatorcontrib><creatorcontrib>Pacaud, P.</creatorcontrib><creatorcontrib>Viala, C.</creatorcontrib><creatorcontrib>Chap, H.</creatorcontrib><creatorcontrib>Payrastre, B.</creatorcontrib><title>Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide</title><title>Thrombosis and haemostasis</title><addtitle>Thromb Haemost</addtitle><description>Summary
We have addressed the role of Rho-kinase in the different steps of thrombin receptor agonist peptide (TRAP) -induced platelet activation. Interestingly, under physiological conditions, incubation of platelets with increasing concentrations of the specific Rho-kinase inhibitor Y-27632 resulted in a dose-dependent reversion of the aggregation induced by 10 μM TRAP, without affecting serotonin secretion. Addition of Y-27632 after three minutes of TRAP stimulation, when the maximal aggregation was reached, resulted in a rapid disaggregation of platelets. Accordingly, the early peak of myosin light chain (MLC) phosphorylation induced by TRAP was not affected by Y-27632 but its sustained phosphorylation, observed during the irreversible phase of aggregation, was dependent of Rho-kinase activity. The rapid decrease in MLC phosphorylation upon Y-27632 treatment correlated well with the specific disappearance of myosin heavy chain from the cytoskeleton and preceded platelet disaggregation. Finally, we provide evidence that secreted ADP, known to play a key role in TRAP-induced irreversible phase of aggregation, was involved in the sustained MLC phosphorylation through Rho-kinase and could be replaced by epinephrine.</description><subject>Adenosine Diphosphate - pharmacology</subject><subject>Adenosine Diphosphate - secretion</subject><subject>Amides - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Blood Platelets - cytology</subject><subject>Blood Platelets - drug effects</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Myosins - drug effects</subject><subject>Myosins - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>Phosphorylation</subject><subject>Platelet</subject><subject>Platelet Aggregation - drug effects</subject><subject>Protein-Serine-Threonine Kinases - antagonists & inhibitors</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Serine-Threonine Kinases - physiology</subject><subject>Pyridines - pharmacology</subject><subject>Review Article</subject><subject>rho-Associated Kinases</subject><issn>0340-6245</issn><issn>2567-689X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqtkV-L1DAUxYso7jj66qMEBN-6Jv2Tto_DsurAisOq4Fu4k95Os7ZJzU1H5kv4mc3sDCsIvvkUkvO755JzkuSl4JeCl-VbSjnPq1RIUUpRPEoWWSmrVNbNt8fJgucFT2VWlBfJM6I7zoUsmvJpciFEzqs6KxbJr9vepd-NBUK2Jra2ezfssWXGstAj-zxTAGPjw6Z3NPXOHwYIxlnmOvbx4ChyYNt7du097tGT2Q7INhHDAQNb7XYed6eZtW1nHb22B7ZZ3Qq20sHso2R3bINTMC0-T550MBC-OJ_L5Ou76y9XH9KbT-_XV6ubVJdFFVKIf23qtmtRSplpgBYryFooigxrXtYiy2spal1LQNg2LdZVozVkXPBCd1FdJm9OvpN3P2akoEZDGocBLLqZVFXxsuK8iuDlCdTeEXns1OTNCP6gBFfHBhSpYwPq3EAceHV2nrcjtn_wc-QReH0GgDQMnQerDT1wTSbzaLhM0hMVeoMjqjs3exsT-fdafeJJ9xACzOgfLEPv3biNXZGKXakecHSx1uNdOxvQhih43Zs9KkM0o6IJtYFBjWBn0t5MQWXVfRrmP26pZf33BkW9-6n6MA75b_-A7to</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>Missy, K.</creator><creator>Plantavid, M.</creator><creator>Pacaud, P.</creator><creator>Viala, C.</creator><creator>Chap, H.</creator><creator>Payrastre, B.</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>20010301</creationdate><title>Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide</title><author>Missy, K. ; Plantavid, M. ; Pacaud, P. ; Viala, C. ; Chap, H. ; Payrastre, B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c547t-a61498dfde6662caade7a2da442e80581238618c86aeab9de879cca20104cf123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adenosine Diphosphate - pharmacology</topic><topic>Adenosine Diphosphate - secretion</topic><topic>Amides - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Blood Platelets - cytology</topic><topic>Blood Platelets - drug effects</topic><topic>Cytoskeleton - drug effects</topic><topic>Cytoskeleton - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Myosins - drug effects</topic><topic>Myosins - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>Phosphorylation</topic><topic>Platelet</topic><topic>Platelet Aggregation - drug effects</topic><topic>Protein-Serine-Threonine Kinases - antagonists & inhibitors</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases - physiology</topic><topic>Pyridines - pharmacology</topic><topic>Review Article</topic><topic>rho-Associated Kinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Missy, K.</creatorcontrib><creatorcontrib>Plantavid, M.</creatorcontrib><creatorcontrib>Pacaud, P.</creatorcontrib><creatorcontrib>Viala, C.</creatorcontrib><creatorcontrib>Chap, H.</creatorcontrib><creatorcontrib>Payrastre, B.</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>Missy, K.</au><au>Plantavid, M.</au><au>Pacaud, P.</au><au>Viala, C.</au><au>Chap, H.</au><au>Payrastre, B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide</atitle><jtitle>Thrombosis and haemostasis</jtitle><addtitle>Thromb Haemost</addtitle><date>2001-03-01</date><risdate>2001</risdate><volume>85</volume><issue>3</issue><spage>514</spage><epage>20</epage><pages>514-20</pages><issn>0340-6245</issn><eissn>2567-689X</eissn><coden>THHADQ</coden><abstract>Summary
We have addressed the role of Rho-kinase in the different steps of thrombin receptor agonist peptide (TRAP) -induced platelet activation. Interestingly, under physiological conditions, incubation of platelets with increasing concentrations of the specific Rho-kinase inhibitor Y-27632 resulted in a dose-dependent reversion of the aggregation induced by 10 μM TRAP, without affecting serotonin secretion. Addition of Y-27632 after three minutes of TRAP stimulation, when the maximal aggregation was reached, resulted in a rapid disaggregation of platelets. Accordingly, the early peak of myosin light chain (MLC) phosphorylation induced by TRAP was not affected by Y-27632 but its sustained phosphorylation, observed during the irreversible phase of aggregation, was dependent of Rho-kinase activity. The rapid decrease in MLC phosphorylation upon Y-27632 treatment correlated well with the specific disappearance of myosin heavy chain from the cytoskeleton and preceded platelet disaggregation. Finally, we provide evidence that secreted ADP, known to play a key role in TRAP-induced irreversible phase of aggregation, was involved in the sustained MLC phosphorylation through Rho-kinase and could be replaced by epinephrine.</abstract><cop>Stuttgart</cop><pub>Schattauer Verlag für Medizin und Naturwissenschaften</pub><pmid>11307824</pmid><doi>10.1055/s-0037-1615614</doi><tpages>-493</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0340-6245 |
| ispartof | Thrombosis and haemostasis, 2001-03, Vol.85 (3), p.514-20 |
| issn | 0340-6245 2567-689X |
| language | eng |
| recordid | cdi_thieme_journals_10_1055_s_0037_1615614 |
| source | MEDLINE; Thieme Connect Journals |
| subjects | Adenosine Diphosphate - pharmacology Adenosine Diphosphate - secretion Amides - pharmacology Biological and medical sciences Blood coagulation. Blood cells Blood Platelets - cytology Blood Platelets - drug effects Cytoskeleton - drug effects Cytoskeleton - metabolism Enzyme Inhibitors - pharmacology Fundamental and applied biological sciences. Psychology Humans Intracellular Signaling Peptides and Proteins Kinetics Molecular and cellular biology Myosins - drug effects Myosins - metabolism Peptide Fragments - pharmacology Phosphorylation Platelet Platelet Aggregation - drug effects Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - metabolism Protein-Serine-Threonine Kinases - physiology Pyridines - pharmacology Review Article rho-Associated Kinases |
| title | Rho-kinase Is Involved in the Sustained Phosphorylation of Myosin and the Irreversible Platelet Aggregation Induced by PAR1 Activating Peptide |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T08%3A52%3A23IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_thiem&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Rho-kinase%20Is%20Involved%20in%20the%20Sustained%20Phosphorylation%20of%20Myosin%20and%20the%20Irreversible%20Platelet%20Aggregation%20Induced%20by%20PAR1%20Activating%20Peptide&rft.jtitle=Thrombosis%20and%20haemostasis&rft.au=Missy,%20K.&rft.date=2001-03-01&rft.volume=85&rft.issue=3&rft.spage=514&rft.epage=20&rft.pages=514-20&rft.issn=0340-6245&rft.eissn=2567-689X&rft.coden=THHADQ&rft_id=info:doi/10.1055/s-0037-1615614&rft_dat=%3Cproquest_thiem%3E77057007%3C/proquest_thiem%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77057007&rft_id=info:pmid/11307824&rfr_iscdi=true |