INTERACTION OF A NEW DEPOLYMERIZED HOLOTHURIAN GLYCOSAMINOGLYCAN WITH PROTEINS IN HUMAN PLASMA
In a rat template bleeding model, depolymerized holothurian glycosaminoglycan (DHG) prolonged bleeding time at 30 mg/kg i.v. but unfractionated heparin (UFH) had the same effect at 1 mg/kg i.v., indicating that DHG is much less bleeding than UFH. To characterize this difference, we examined the affi...
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Veröffentlicht in: | Thrombosis research 1996-08, Vol.83 (3), p.253-264 |
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creator | Minamiguchi, Kazuhisa Nagase, Hideki Kitazato, Keiko T Kitazato, Kenji |
description | In a rat template bleeding model, depolymerized holothurian glycosaminoglycan (DHG) prolonged bleeding time at 30 mg/kg i.v. but unfractionated heparin (UFH) had the same effect at 1 mg/kg i.v., indicating that DHG is much less bleeding than UFH. To characterize this difference, we examined the affinity of DHG for plasma proteins by means of a glycosaminoglycan-conjugated cellulofine column in comparison with that of UFH. The DHG column strongly bound factor V, factor IX, protein S, histidine-rich glycoprotein, platelet factor 4 (PF4), β-thromboglobulin, von Willebrand factor, fibronectin, and heparin cofactor II, but did not bind fibrinogen, prothrombin, factor VII, protein C, antithrombin III (ATIII), plasminogen or α 2-plasmin inhibitor. The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH. One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma. |
doi_str_mv | 10.1016/0049-3848(96)00134-X |
format | Article |
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To characterize this difference, we examined the affinity of DHG for plasma proteins by means of a glycosaminoglycan-conjugated cellulofine column in comparison with that of UFH. The DHG column strongly bound factor V, factor IX, protein S, histidine-rich glycoprotein, platelet factor 4 (PF4), β-thromboglobulin, von Willebrand factor, fibronectin, and heparin cofactor II, but did not bind fibrinogen, prothrombin, factor VII, protein C, antithrombin III (ATIII), plasminogen or α 2-plasmin inhibitor. The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH. One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/0049-3848(96)00134-X</identifier><identifier>PMID: 8840467</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Animals ; anticoagulant ; Bleeding Time ; Blood Proteins - metabolism ; depolymerized holothurian glycosaminoglycan ; glycosaminoglycan ; Glycosaminoglycans - metabolism ; Glycosaminoglycans - pharmacology ; Hemorrhage - metabolism ; Humans ; Protein Binding ; Rats</subject><ispartof>Thrombosis research, 1996-08, Vol.83 (3), p.253-264</ispartof><rights>1996 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-aaa7459f4853df7ef0c67b948f519c43d1b36e0b3be64db97e0e24939d166d563</citedby><cites>FETCH-LOGICAL-c357t-aaa7459f4853df7ef0c67b948f519c43d1b36e0b3be64db97e0e24939d166d563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0049-3848(96)00134-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8840467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Minamiguchi, Kazuhisa</creatorcontrib><creatorcontrib>Nagase, Hideki</creatorcontrib><creatorcontrib>Kitazato, Keiko T</creatorcontrib><creatorcontrib>Kitazato, Kenji</creatorcontrib><title>INTERACTION OF A NEW DEPOLYMERIZED HOLOTHURIAN GLYCOSAMINOGLYCAN WITH PROTEINS IN HUMAN PLASMA</title><title>Thrombosis research</title><addtitle>Thromb Res</addtitle><description>In a rat template bleeding model, depolymerized holothurian glycosaminoglycan (DHG) prolonged bleeding time at 30 mg/kg i.v. but unfractionated heparin (UFH) had the same effect at 1 mg/kg i.v., indicating that DHG is much less bleeding than UFH. To characterize this difference, we examined the affinity of DHG for plasma proteins by means of a glycosaminoglycan-conjugated cellulofine column in comparison with that of UFH. The DHG column strongly bound factor V, factor IX, protein S, histidine-rich glycoprotein, platelet factor 4 (PF4), β-thromboglobulin, von Willebrand factor, fibronectin, and heparin cofactor II, but did not bind fibrinogen, prothrombin, factor VII, protein C, antithrombin III (ATIII), plasminogen or α 2-plasmin inhibitor. The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH. One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma.</description><subject>Animals</subject><subject>anticoagulant</subject><subject>Bleeding Time</subject><subject>Blood Proteins - metabolism</subject><subject>depolymerized holothurian glycosaminoglycan</subject><subject>glycosaminoglycan</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Glycosaminoglycans - pharmacology</subject><subject>Hemorrhage - metabolism</subject><subject>Humans</subject><subject>Protein Binding</subject><subject>Rats</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1LwzAUhoMoOj_-gUKuRC-qyZImzY1QZrWBrhlbh5sXhn6kUNmsNpvgvzdlw0uvztd73sN5ALjE6A4jzO4RosIjAQ1uBLtFCBPqLQ7AAAdceEPKh4dg8Cc5AafWvjsRx8I_BsdBQBFlfADeZJpF03CUSZVC9QRDmEYv8DGaqGQ5jqbyNXqEsUpUFs-nMkzhc7IcqVk4lqnqU9d5kVkMJ1OVRTKdQZnCeD527UkSzsbhOTiq85U1F_t4BuZPUTaKvUQ9y1GYeCXx-cbL85xTX9Q08ElVc1OjkvFC0KD2sSgpqXBBmEEFKQyjVSG4QWZIBREVZqzyGTkD1zvfz6792hq70evGlma1yj9Mu7WaB8RhIcQJ6U5Ydq21nan1Z9es8-5HY6R7rLpnpntmWvSFw6oXbu1q778t1qb6W9pzdPOH3dy4J78b02lbNuajNFXTmXKjq7b5_8AvJCB-3Q</recordid><startdate>19960801</startdate><enddate>19960801</enddate><creator>Minamiguchi, Kazuhisa</creator><creator>Nagase, Hideki</creator><creator>Kitazato, Keiko T</creator><creator>Kitazato, Kenji</creator><general>Elsevier Ltd</general><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>19960801</creationdate><title>INTERACTION OF A NEW DEPOLYMERIZED HOLOTHURIAN GLYCOSAMINOGLYCAN WITH PROTEINS IN HUMAN PLASMA</title><author>Minamiguchi, Kazuhisa ; Nagase, Hideki ; Kitazato, Keiko T ; Kitazato, Kenji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-aaa7459f4853df7ef0c67b948f519c43d1b36e0b3be64db97e0e24939d166d563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>anticoagulant</topic><topic>Bleeding Time</topic><topic>Blood Proteins - metabolism</topic><topic>depolymerized holothurian glycosaminoglycan</topic><topic>glycosaminoglycan</topic><topic>Glycosaminoglycans - metabolism</topic><topic>Glycosaminoglycans - pharmacology</topic><topic>Hemorrhage - metabolism</topic><topic>Humans</topic><topic>Protein Binding</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Minamiguchi, Kazuhisa</creatorcontrib><creatorcontrib>Nagase, Hideki</creatorcontrib><creatorcontrib>Kitazato, Keiko T</creatorcontrib><creatorcontrib>Kitazato, Kenji</creatorcontrib><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 research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Minamiguchi, Kazuhisa</au><au>Nagase, Hideki</au><au>Kitazato, Keiko T</au><au>Kitazato, Kenji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>INTERACTION OF A NEW DEPOLYMERIZED HOLOTHURIAN GLYCOSAMINOGLYCAN WITH PROTEINS IN HUMAN PLASMA</atitle><jtitle>Thrombosis research</jtitle><addtitle>Thromb Res</addtitle><date>1996-08-01</date><risdate>1996</risdate><volume>83</volume><issue>3</issue><spage>253</spage><epage>264</epage><pages>253-264</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><abstract>In a rat template bleeding model, depolymerized holothurian glycosaminoglycan (DHG) prolonged bleeding time at 30 mg/kg i.v. but unfractionated heparin (UFH) had the same effect at 1 mg/kg i.v., indicating that DHG is much less bleeding than UFH. To characterize this difference, we examined the affinity of DHG for plasma proteins by means of a glycosaminoglycan-conjugated cellulofine column in comparison with that of UFH. The DHG column strongly bound factor V, factor IX, protein S, histidine-rich glycoprotein, platelet factor 4 (PF4), β-thromboglobulin, von Willebrand factor, fibronectin, and heparin cofactor II, but did not bind fibrinogen, prothrombin, factor VII, protein C, antithrombin III (ATIII), plasminogen or α 2-plasmin inhibitor. The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH. One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>8840467</pmid><doi>10.1016/0049-3848(96)00134-X</doi><tpages>12</tpages></addata></record> |
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subjects | Animals anticoagulant Bleeding Time Blood Proteins - metabolism depolymerized holothurian glycosaminoglycan glycosaminoglycan Glycosaminoglycans - metabolism Glycosaminoglycans - pharmacology Hemorrhage - metabolism Humans Protein Binding Rats |
title | INTERACTION OF A NEW DEPOLYMERIZED HOLOTHURIAN GLYCOSAMINOGLYCAN WITH PROTEINS IN HUMAN PLASMA |
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