PPACK-thrombin is a noncompetitive inhibitor of α-thrombin binding to human platelets
Recent studies from our laboratory indicate that purified kininogens are noncompetitive inhibitors of human α-thrombin but not PPACK-thrombin, binding to human washed platelets. In order to understand the mechanism by which the kininogens inhibit α-thrombin binding, investigations were initiated to...
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| Veröffentlicht in: | Thrombosis research 1992-09, Vol.67 (5), p.479-489 |
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| creator | Schmaier, A.H. Meloni, F.J. Nawarawong, W. Jiang, Y.P. |
| description | Recent studies from our laboratory indicate that purified kininogens are noncompetitive inhibitors of human α-thrombin but not PPACK-thrombin, binding to human washed platelets. In order to understand the mechanism by which the kininogens inhibit α-thrombin binding, investigations were initiated to determine if α-thrombin and PPACK-thrombin bound to the same site on human platelets. Initial investigations reveal that α-thrombin is a more potent inhibitor of
125I-PPACK-thrombin binding than PPACK-thrombin. Further studies show that PPACK-thrombin is a noncompetitive inhibitor of
125I-α-thrombin binding to platelets. These studies suggest that human α-thrombin binds on the platelet surface to a different site or binds differently to the same site from PPACK-thrombin. These data indicate that the ability of the kininogens to block α-thrombin binding to platelets but not PPACK-thrombin binding results from these thrombins having either two different binding sites or one binding site on the platelet surface which they interact with differently. |
| doi_str_mv | 10.1016/0049-3848(92)90010-8 |
| format | Article |
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125I-PPACK-thrombin binding than PPACK-thrombin. Further studies show that PPACK-thrombin is a noncompetitive inhibitor of
125I-α-thrombin binding to platelets. These studies suggest that human α-thrombin binds on the platelet surface to a different site or binds differently to the same site from PPACK-thrombin. These data indicate that the ability of the kininogens to block α-thrombin binding to platelets but not PPACK-thrombin binding results from these thrombins having either two different binding sites or one binding site on the platelet surface which they interact with differently.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/0049-3848(92)90010-8</identifier><identifier>PMID: 1448784</identifier><identifier>CODEN: THBRAA</identifier><language>eng</language><publisher>OXFORD: Elsevier Ltd</publisher><subject>Amino Acid Chloromethyl Ketones - metabolism ; Binding Sites ; Biological and medical sciences ; Blood coagulation. Blood cells ; Blood Platelets - metabolism ; Cardiovascular System & Cardiology ; Fundamental and applied biological sciences. Psychology ; Hematology ; Humans ; kininogen ; Life Sciences & Biomedicine ; Models, Biological ; Molecular and cellular biology ; Peripheral Vascular Disease ; Platelet ; platelets ; PPACK-thrombin ; Protein Binding ; Science & Technology ; Thrombin - antagonists & inhibitors ; Thrombin - metabolism ; thrombin receptor ; α-thrombin</subject><ispartof>Thrombosis research, 1992-09, Vol.67 (5), p.479-489</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>10</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992JR70800001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c432t-730d9e590e9e7c8564d16f492b9fc2c2492d8deddde78b5d65aa99d5062183253</citedby><cites>FETCH-LOGICAL-c432t-730d9e590e9e7c8564d16f492b9fc2c2492d8deddde78b5d65aa99d5062183253</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(92)90010-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27197,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4452215$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1448784$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schmaier, A.H.</creatorcontrib><creatorcontrib>Meloni, F.J.</creatorcontrib><creatorcontrib>Nawarawong, W.</creatorcontrib><creatorcontrib>Jiang, Y.P.</creatorcontrib><title>PPACK-thrombin is a noncompetitive inhibitor of α-thrombin binding to human platelets</title><title>Thrombosis research</title><addtitle>THROMB RES</addtitle><addtitle>Thromb Res</addtitle><description>Recent studies from our laboratory indicate that purified kininogens are noncompetitive inhibitors of human α-thrombin but not PPACK-thrombin, binding to human washed platelets. In order to understand the mechanism by which the kininogens inhibit α-thrombin binding, investigations were initiated to determine if α-thrombin and PPACK-thrombin bound to the same site on human platelets. Initial investigations reveal that α-thrombin is a more potent inhibitor of
125I-PPACK-thrombin binding than PPACK-thrombin. Further studies show that PPACK-thrombin is a noncompetitive inhibitor of
125I-α-thrombin binding to platelets. These studies suggest that human α-thrombin binds on the platelet surface to a different site or binds differently to the same site from PPACK-thrombin. These data indicate that the ability of the kininogens to block α-thrombin binding to platelets but not PPACK-thrombin binding results from these thrombins having either two different binding sites or one binding site on the platelet surface which they interact with differently.</description><subject>Amino Acid Chloromethyl Ketones - metabolism</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Blood Platelets - metabolism</subject><subject>Cardiovascular System & Cardiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hematology</subject><subject>Humans</subject><subject>kininogen</subject><subject>Life Sciences & Biomedicine</subject><subject>Models, Biological</subject><subject>Molecular and cellular biology</subject><subject>Peripheral Vascular Disease</subject><subject>Platelet</subject><subject>platelets</subject><subject>PPACK-thrombin</subject><subject>Protein Binding</subject><subject>Science & Technology</subject><subject>Thrombin - antagonists & inhibitors</subject><subject>Thrombin - metabolism</subject><subject>thrombin receptor</subject><subject>α-thrombin</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkN-K1DAUh4Mo67j6Bgq9EFGkmqRJm9wIQ_H_gouotyFNTp1Im4xJuuJj-SI-kxk7zN6JgZAD5_sdTj6E7hP8jGDSPseYyboRTDyW9InEmOBa3EAbIjpZU9bRm2hzQm6jOyl9K0xHJD9DZ4Qx0Qm2QV8uL7f9-zrvYpgH5yuXKl354E2Y95BddldQOb9zg8shVmGsfv-6hsu1zn-tcqh2y6x9tZ90hglyuotujXpKcO_4nqPPr15-6t_UFx9ev-23F7VhDc1112ArgUsMEjojeMssaUcm6SBHQw0tlRUWrLXQiYHblmstpeW4pUQ0lDfn6NE6dx_D9wVSVrNLBqZJewhLUl3TSN5iWUC2giaGlCKMah_drONPRbA66FQHV-rgSkmq_upUosQeHOcvwwz2OrT6K_2Hx75ORk9j1N64dMIY45SSw5pPV-wHDGFMxoE3cKK2REr67mOHBS6HFFr8P927rLMLvg-LzyX6Yo1CkX7lIKpj3LoIJisb3L8__AesgLKj</recordid><startdate>19920901</startdate><enddate>19920901</enddate><creator>Schmaier, A.H.</creator><creator>Meloni, F.J.</creator><creator>Nawarawong, W.</creator><creator>Jiang, Y.P.</creator><general>Elsevier Ltd</general><general>Elsevier</general><general>Elsevier Science</general><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</scope><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>19920901</creationdate><title>PPACK-thrombin is a noncompetitive inhibitor of α-thrombin binding to human platelets</title><author>Schmaier, A.H. ; Meloni, F.J. ; Nawarawong, W. ; Jiang, Y.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c432t-730d9e590e9e7c8564d16f492b9fc2c2492d8deddde78b5d65aa99d5062183253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Chloromethyl Ketones - metabolism</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Blood Platelets - metabolism</topic><topic>Cardiovascular System & Cardiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hematology</topic><topic>Humans</topic><topic>kininogen</topic><topic>Life Sciences & Biomedicine</topic><topic>Models, Biological</topic><topic>Molecular and cellular biology</topic><topic>Peripheral Vascular Disease</topic><topic>Platelet</topic><topic>platelets</topic><topic>PPACK-thrombin</topic><topic>Protein Binding</topic><topic>Science & Technology</topic><topic>Thrombin - antagonists & inhibitors</topic><topic>Thrombin - metabolism</topic><topic>thrombin receptor</topic><topic>α-thrombin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schmaier, A.H.</creatorcontrib><creatorcontrib>Meloni, F.J.</creatorcontrib><creatorcontrib>Nawarawong, W.</creatorcontrib><creatorcontrib>Jiang, Y.P.</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</collection><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 research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schmaier, A.H.</au><au>Meloni, F.J.</au><au>Nawarawong, W.</au><au>Jiang, Y.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PPACK-thrombin is a noncompetitive inhibitor of α-thrombin binding to human platelets</atitle><jtitle>Thrombosis research</jtitle><stitle>THROMB RES</stitle><addtitle>Thromb Res</addtitle><date>1992-09-01</date><risdate>1992</risdate><volume>67</volume><issue>5</issue><spage>479</spage><epage>489</epage><pages>479-489</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><coden>THBRAA</coden><abstract>Recent studies from our laboratory indicate that purified kininogens are noncompetitive inhibitors of human α-thrombin but not PPACK-thrombin, binding to human washed platelets. In order to understand the mechanism by which the kininogens inhibit α-thrombin binding, investigations were initiated to determine if α-thrombin and PPACK-thrombin bound to the same site on human platelets. Initial investigations reveal that α-thrombin is a more potent inhibitor of
125I-PPACK-thrombin binding than PPACK-thrombin. Further studies show that PPACK-thrombin is a noncompetitive inhibitor of
125I-α-thrombin binding to platelets. These studies suggest that human α-thrombin binds on the platelet surface to a different site or binds differently to the same site from PPACK-thrombin. These data indicate that the ability of the kininogens to block α-thrombin binding to platelets but not PPACK-thrombin binding results from these thrombins having either two different binding sites or one binding site on the platelet surface which they interact with differently.</abstract><cop>OXFORD</cop><pub>Elsevier Ltd</pub><pmid>1448784</pmid><doi>10.1016/0049-3848(92)90010-8</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Thrombosis research, 1992-09, Vol.67 (5), p.479-489 |
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| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Chloromethyl Ketones - metabolism Binding Sites Biological and medical sciences Blood coagulation. Blood cells Blood Platelets - metabolism Cardiovascular System & Cardiology Fundamental and applied biological sciences. Psychology Hematology Humans kininogen Life Sciences & Biomedicine Models, Biological Molecular and cellular biology Peripheral Vascular Disease Platelet platelets PPACK-thrombin Protein Binding Science & Technology Thrombin - antagonists & inhibitors Thrombin - metabolism thrombin receptor α-thrombin |
| title | PPACK-thrombin is a noncompetitive inhibitor of α-thrombin binding to human platelets |
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