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Daboxin P, a phospholipase A 2 of Indian Daboia russelii venom, modulates thrombin-mediated platelet aggregation
Daboxin P, reported earlier from the venom of Daboia russellii, disturbs the blood coagulation cascade by targeting factor X and factor Xa. The present study exhibits that Daboxin P also inhibits platelet aggregation induced by various agonists. The thrombin-induced platelet aggregation was inhibite...
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Published in: | Journal of biochemical and molecular toxicology 2023-11, Vol.37 (11), p.e23476 |
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container_title | Journal of biochemical and molecular toxicology |
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creator | Yasmin, Rafika Chanchal, Shankar Ashraf, Mohammad Zahid Doley, Robin |
description | Daboxin P, reported earlier from the venom of Daboia russellii, disturbs the blood coagulation cascade by targeting factor X and factor Xa. The present study exhibits that Daboxin P also inhibits platelet aggregation induced by various agonists. The thrombin-induced platelet aggregation was inhibited maximum whereas inhibition of collagen-induced platelet aggregation was found to be 50% and no inhibition of adenosine diphosphate (ADP) and arachidonic acid-induced aggregation was observed. Daboxin P dose-dependently inhibited the thrombin-induced platelet aggregation with Anti-Aggregation 50 (AD
) dose of 55.166 nM and also reduced the thrombin-mediated calcium influx. In-silico interaction studies suggested that Daboxin P binds to thrombin and blocks its interaction with its receptor on the platelet surface. Quenching of thrombin's emission spectrum by Daboxin P and electrophoretic profiles of pull-down assay further reveals the binding between Daboxin P and thrombin. Thus, the present study demonstrates that Daboxin P inhibits thrombin-induced platelet aggregation by binding to thrombin. |
doi_str_mv | 10.1002/jbt.23476 |
format | article |
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) dose of 55.166 nM and also reduced the thrombin-mediated calcium influx. In-silico interaction studies suggested that Daboxin P binds to thrombin and blocks its interaction with its receptor on the platelet surface. Quenching of thrombin's emission spectrum by Daboxin P and electrophoretic profiles of pull-down assay further reveals the binding between Daboxin P and thrombin. Thus, the present study demonstrates that Daboxin P inhibits thrombin-induced platelet aggregation by binding to thrombin.</description><identifier>ISSN: 1095-6670</identifier><identifier>EISSN: 1099-0461</identifier><identifier>DOI: 10.1002/jbt.23476</identifier><identifier>PMID: 37466159</identifier><language>eng</language><publisher>United States</publisher><ispartof>Journal of biochemical and molecular toxicology, 2023-11, Vol.37 (11), p.e23476</ispartof><rights>2023 Wiley Periodicals LLC.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c979-1de6270b4f98a5eb84f60fa9aabfb0b7f705c23ef5174c671c7dfa60767c538f3</citedby><cites>FETCH-LOGICAL-c979-1de6270b4f98a5eb84f60fa9aabfb0b7f705c23ef5174c671c7dfa60767c538f3</cites><orcidid>0000-0002-3229-028X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37466159$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yasmin, Rafika</creatorcontrib><creatorcontrib>Chanchal, Shankar</creatorcontrib><creatorcontrib>Ashraf, Mohammad Zahid</creatorcontrib><creatorcontrib>Doley, Robin</creatorcontrib><title>Daboxin P, a phospholipase A 2 of Indian Daboia russelii venom, modulates thrombin-mediated platelet aggregation</title><title>Journal of biochemical and molecular toxicology</title><addtitle>J Biochem Mol Toxicol</addtitle><description>Daboxin P, reported earlier from the venom of Daboia russellii, disturbs the blood coagulation cascade by targeting factor X and factor Xa. The present study exhibits that Daboxin P also inhibits platelet aggregation induced by various agonists. The thrombin-induced platelet aggregation was inhibited maximum whereas inhibition of collagen-induced platelet aggregation was found to be 50% and no inhibition of adenosine diphosphate (ADP) and arachidonic acid-induced aggregation was observed. Daboxin P dose-dependently inhibited the thrombin-induced platelet aggregation with Anti-Aggregation 50 (AD
) dose of 55.166 nM and also reduced the thrombin-mediated calcium influx. In-silico interaction studies suggested that Daboxin P binds to thrombin and blocks its interaction with its receptor on the platelet surface. Quenching of thrombin's emission spectrum by Daboxin P and electrophoretic profiles of pull-down assay further reveals the binding between Daboxin P and thrombin. Thus, the present study demonstrates that Daboxin P inhibits thrombin-induced platelet aggregation by binding to thrombin.</description><issn>1095-6670</issn><issn>1099-0461</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNo9kE1PwzAMhiMEYmNw4A-gXJFWcNomWY7T-Jo0CQ67V06bbJnapko6BP-ebgMOli29jy3rIeSWwQMDSB93un9Is1yKMzJmoFQCuWDnx5knQkgYkasYdwDAleSXZJTJXAjG1Zh0T6j9l2vpx5Qi7bY-DlW7DqOhc5pSb-myrRy29AA6pGEfo6mdo5-m9c2UNr7a19ibSPtt8I12bdKYYaE3Fe0OQW16iptNMBvsnW-vyYXFOpqb3z4h65fn9eItWb2_LhfzVVIqqRJWGZFK0LlVM-RGz3IrwKJC1FaDllYCL9PMWM5kXgrJSllZFCCFLHk2s9mE3J_OlsHHGIwtuuAaDN8Fg-IgrRikFUdpA3t3Yru9Hn7_J_8sZT9i1mkc</recordid><startdate>202311</startdate><enddate>202311</enddate><creator>Yasmin, Rafika</creator><creator>Chanchal, Shankar</creator><creator>Ashraf, Mohammad Zahid</creator><creator>Doley, Robin</creator><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-3229-028X</orcidid></search><sort><creationdate>202311</creationdate><title>Daboxin P, a phospholipase A 2 of Indian Daboia russelii venom, modulates thrombin-mediated platelet aggregation</title><author>Yasmin, Rafika ; Chanchal, Shankar ; Ashraf, Mohammad Zahid ; Doley, Robin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c979-1de6270b4f98a5eb84f60fa9aabfb0b7f705c23ef5174c671c7dfa60767c538f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yasmin, Rafika</creatorcontrib><creatorcontrib>Chanchal, Shankar</creatorcontrib><creatorcontrib>Ashraf, Mohammad Zahid</creatorcontrib><creatorcontrib>Doley, Robin</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Journal of biochemical and molecular toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yasmin, Rafika</au><au>Chanchal, Shankar</au><au>Ashraf, Mohammad Zahid</au><au>Doley, Robin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Daboxin P, a phospholipase A 2 of Indian Daboia russelii venom, modulates thrombin-mediated platelet aggregation</atitle><jtitle>Journal of biochemical and molecular toxicology</jtitle><addtitle>J Biochem Mol Toxicol</addtitle><date>2023-11</date><risdate>2023</risdate><volume>37</volume><issue>11</issue><spage>e23476</spage><pages>e23476-</pages><issn>1095-6670</issn><eissn>1099-0461</eissn><abstract>Daboxin P, reported earlier from the venom of Daboia russellii, disturbs the blood coagulation cascade by targeting factor X and factor Xa. The present study exhibits that Daboxin P also inhibits platelet aggregation induced by various agonists. The thrombin-induced platelet aggregation was inhibited maximum whereas inhibition of collagen-induced platelet aggregation was found to be 50% and no inhibition of adenosine diphosphate (ADP) and arachidonic acid-induced aggregation was observed. Daboxin P dose-dependently inhibited the thrombin-induced platelet aggregation with Anti-Aggregation 50 (AD
) dose of 55.166 nM and also reduced the thrombin-mediated calcium influx. In-silico interaction studies suggested that Daboxin P binds to thrombin and blocks its interaction with its receptor on the platelet surface. Quenching of thrombin's emission spectrum by Daboxin P and electrophoretic profiles of pull-down assay further reveals the binding between Daboxin P and thrombin. Thus, the present study demonstrates that Daboxin P inhibits thrombin-induced platelet aggregation by binding to thrombin.</abstract><cop>United States</cop><pmid>37466159</pmid><doi>10.1002/jbt.23476</doi><orcidid>https://orcid.org/0000-0002-3229-028X</orcidid></addata></record> |
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title | Daboxin P, a phospholipase A 2 of Indian Daboia russelii venom, modulates thrombin-mediated platelet aggregation |
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