Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity
Ancrod is a purified fraction of venom from the Malayan pit viper Calloselasma rhodostoma, containing a serine protease that cleaves fibrinopeptides A from fibrinogen. We report on a study that involved intravenous and subcutaneous application of ancrod in healthy subjects in which it was shown that...
Gespeichert in:
| Veröffentlicht in: | Annals of the New York Academy of Sciences 2001-01, Vol.936 (1), p.210-214 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 214 |
|---|---|
| container_issue | 1 |
| container_start_page | 210 |
| container_title | Annals of the New York Academy of Sciences |
| container_volume | 936 |
| creator | Dempfle, C E Argiriou, S Alesci, S Kucher, K Müller-Peltzer, H Rübsamen, K Heene, D L |
| description | Ancrod is a purified fraction of venom from the Malayan pit viper Calloselasma rhodostoma, containing a serine protease that cleaves fibrinopeptides A from fibrinogen. We report on a study that involved intravenous and subcutaneous application of ancrod in healthy subjects in which it was shown that ancrod induces the formation of desAA-fibrin complexes that are partially crosslinked by factor XIII proenzyme, and act as cofactor in tPA induced plasminogen activation. The plasmin generated degrades fibrin, as well as fibrinogen, leading to the appearance of large amounts of fibrinogen and fibrin degradation products in the circulation, including fragment D-dimer. At low concentrations of ancrod, formation of desAA-fibrin is preceded by production of desA-profibrin, lacking only one fibrinopeptide A. |
| doi_str_mv | 10.1111/j.1749-6632.2001.tb03507.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71018044</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71018044</sourcerecordid><originalsourceid>FETCH-LOGICAL-c258t-650d61280f7d2e8a0fa3d6fe5236869ed358ce9ce4db6cfc56371c7726bf5bfd3</originalsourceid><addsrcrecordid>eNptUcFOAyEQJUZja_UXDPHgbVdYdmHrzZhWm5h40cQbYWFQmu5uBWran_CbZdNGL3IYyMx7w8x7CF1RktN0bpY5FeU045wVeUEIzWNDWEVEvj1C49_SMRoTIkRWTws2QmchLBO0qEtxikaUlpyUgo_R99w13nXY9r5V0fUdVp3Ba99H6Fe74AI2m1R_T2nte4OjBxVb6GKOZ1_OQKdh4GIDIbvLEs_-1y9--L5tUtp1BtaQQhexVTom5ttiscDp6b5c3J2jE6tWAS4O9wS9zmcv94_Z0_PD4v7uKdNFVceMV8TwtAyxwhRQK2IVM9xCVTBe8ykYVtUaphpK03BtdcWZoFqIgje2aqxhE3S975sm_txAiLJ1QcNqpTroN0EKSmhNyjIBb_fAtH0IHqxce9cqv5OUyMENuZSD5HKQXA5uyIMbcpvIl4dfNk0L5o96kJ_9AM54i0M</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71018044</pqid></control><display><type>article</type><title>Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><creator>Dempfle, C E ; Argiriou, S ; Alesci, S ; Kucher, K ; Müller-Peltzer, H ; Rübsamen, K ; Heene, D L</creator><creatorcontrib>Dempfle, C E ; Argiriou, S ; Alesci, S ; Kucher, K ; Müller-Peltzer, H ; Rübsamen, K ; Heene, D L</creatorcontrib><description>Ancrod is a purified fraction of venom from the Malayan pit viper Calloselasma rhodostoma, containing a serine protease that cleaves fibrinopeptides A from fibrinogen. We report on a study that involved intravenous and subcutaneous application of ancrod in healthy subjects in which it was shown that ancrod induces the formation of desAA-fibrin complexes that are partially crosslinked by factor XIII proenzyme, and act as cofactor in tPA induced plasminogen activation. The plasmin generated degrades fibrin, as well as fibrinogen, leading to the appearance of large amounts of fibrinogen and fibrin degradation products in the circulation, including fragment D-dimer. At low concentrations of ancrod, formation of desAA-fibrin is preceded by production of desA-profibrin, lacking only one fibrinopeptide A.</description><identifier>ISSN: 0077-8923</identifier><identifier>EISSN: 1749-6632</identifier><identifier>DOI: 10.1111/j.1749-6632.2001.tb03507.x</identifier><identifier>PMID: 11460476</identifier><language>eng</language><publisher>United States</publisher><subject>Ancrod - pharmacology ; Factor XIII - metabolism ; Fibrin - biosynthesis ; Fibrin - metabolism ; Humans ; Hydrolysis ; Thrombin - metabolism</subject><ispartof>Annals of the New York Academy of Sciences, 2001-01, Vol.936 (1), p.210-214</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c258t-650d61280f7d2e8a0fa3d6fe5236869ed358ce9ce4db6cfc56371c7726bf5bfd3</cites></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/11460476$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dempfle, C E</creatorcontrib><creatorcontrib>Argiriou, S</creatorcontrib><creatorcontrib>Alesci, S</creatorcontrib><creatorcontrib>Kucher, K</creatorcontrib><creatorcontrib>Müller-Peltzer, H</creatorcontrib><creatorcontrib>Rübsamen, K</creatorcontrib><creatorcontrib>Heene, D L</creatorcontrib><title>Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity</title><title>Annals of the New York Academy of Sciences</title><addtitle>Ann N Y Acad Sci</addtitle><description>Ancrod is a purified fraction of venom from the Malayan pit viper Calloselasma rhodostoma, containing a serine protease that cleaves fibrinopeptides A from fibrinogen. We report on a study that involved intravenous and subcutaneous application of ancrod in healthy subjects in which it was shown that ancrod induces the formation of desAA-fibrin complexes that are partially crosslinked by factor XIII proenzyme, and act as cofactor in tPA induced plasminogen activation. The plasmin generated degrades fibrin, as well as fibrinogen, leading to the appearance of large amounts of fibrinogen and fibrin degradation products in the circulation, including fragment D-dimer. At low concentrations of ancrod, formation of desAA-fibrin is preceded by production of desA-profibrin, lacking only one fibrinopeptide A.</description><subject>Ancrod - pharmacology</subject><subject>Factor XIII - metabolism</subject><subject>Fibrin - biosynthesis</subject><subject>Fibrin - metabolism</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Thrombin - metabolism</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUcFOAyEQJUZja_UXDPHgbVdYdmHrzZhWm5h40cQbYWFQmu5uBWran_CbZdNGL3IYyMx7w8x7CF1RktN0bpY5FeU045wVeUEIzWNDWEVEvj1C49_SMRoTIkRWTws2QmchLBO0qEtxikaUlpyUgo_R99w13nXY9r5V0fUdVp3Ba99H6Fe74AI2m1R_T2nte4OjBxVb6GKOZ1_OQKdh4GIDIbvLEs_-1y9--L5tUtp1BtaQQhexVTom5ttiscDp6b5c3J2jE6tWAS4O9wS9zmcv94_Z0_PD4v7uKdNFVceMV8TwtAyxwhRQK2IVM9xCVTBe8ykYVtUaphpK03BtdcWZoFqIgje2aqxhE3S975sm_txAiLJ1QcNqpTroN0EKSmhNyjIBb_fAtH0IHqxce9cqv5OUyMENuZSD5HKQXA5uyIMbcpvIl4dfNk0L5o96kJ_9AM54i0M</recordid><startdate>20010101</startdate><enddate>20010101</enddate><creator>Dempfle, C E</creator><creator>Argiriou, S</creator><creator>Alesci, S</creator><creator>Kucher, K</creator><creator>Müller-Peltzer, H</creator><creator>Rübsamen, K</creator><creator>Heene, D L</creator><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>20010101</creationdate><title>Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity</title><author>Dempfle, C E ; Argiriou, S ; Alesci, S ; Kucher, K ; Müller-Peltzer, H ; Rübsamen, K ; Heene, D L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c258t-650d61280f7d2e8a0fa3d6fe5236869ed358ce9ce4db6cfc56371c7726bf5bfd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Ancrod - pharmacology</topic><topic>Factor XIII - metabolism</topic><topic>Fibrin - biosynthesis</topic><topic>Fibrin - metabolism</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Thrombin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dempfle, C E</creatorcontrib><creatorcontrib>Argiriou, S</creatorcontrib><creatorcontrib>Alesci, S</creatorcontrib><creatorcontrib>Kucher, K</creatorcontrib><creatorcontrib>Müller-Peltzer, H</creatorcontrib><creatorcontrib>Rübsamen, K</creatorcontrib><creatorcontrib>Heene, D L</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>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dempfle, C E</au><au>Argiriou, S</au><au>Alesci, S</au><au>Kucher, K</au><au>Müller-Peltzer, H</au><au>Rübsamen, K</au><au>Heene, D L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>2001-01-01</date><risdate>2001</risdate><volume>936</volume><issue>1</issue><spage>210</spage><epage>214</epage><pages>210-214</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>Ancrod is a purified fraction of venom from the Malayan pit viper Calloselasma rhodostoma, containing a serine protease that cleaves fibrinopeptides A from fibrinogen. We report on a study that involved intravenous and subcutaneous application of ancrod in healthy subjects in which it was shown that ancrod induces the formation of desAA-fibrin complexes that are partially crosslinked by factor XIII proenzyme, and act as cofactor in tPA induced plasminogen activation. The plasmin generated degrades fibrin, as well as fibrinogen, leading to the appearance of large amounts of fibrinogen and fibrin degradation products in the circulation, including fragment D-dimer. At low concentrations of ancrod, formation of desAA-fibrin is preceded by production of desA-profibrin, lacking only one fibrinopeptide A.</abstract><cop>United States</cop><pmid>11460476</pmid><doi>10.1111/j.1749-6632.2001.tb03507.x</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0077-8923 |
| ispartof | Annals of the New York Academy of Sciences, 2001-01, Vol.936 (1), p.210-214 |
| issn | 0077-8923 1749-6632 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71018044 |
| source | MEDLINE; Access via Wiley Online Library |
| subjects | Ancrod - pharmacology Factor XIII - metabolism Fibrin - biosynthesis Fibrin - metabolism Humans Hydrolysis Thrombin - metabolism |
| title | Fibrin formation and proteolysis during ancrod treatment. Evidence for des-A-profibrin formation and thrombin independent factor XIII activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T15%3A58%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Fibrin%20formation%20and%20proteolysis%20during%20ancrod%20treatment.%20Evidence%20for%20des-A-profibrin%20formation%20and%20thrombin%20independent%20factor%20XIII%20activity&rft.jtitle=Annals%20of%20the%20New%20York%20Academy%20of%20Sciences&rft.au=Dempfle,%20C%20E&rft.date=2001-01-01&rft.volume=936&rft.issue=1&rft.spage=210&rft.epage=214&rft.pages=210-214&rft.issn=0077-8923&rft.eissn=1749-6632&rft_id=info:doi/10.1111/j.1749-6632.2001.tb03507.x&rft_dat=%3Cproquest_cross%3E71018044%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71018044&rft_id=info:pmid/11460476&rfr_iscdi=true |