Endothelial desquamating activity of rat synthetic fibrinopeptide b and its analogues “in vivo” : Identification of responsible sequence
The endothelial desquamating activity of the synthetic rat fibrinopeptide B (ATTDSDKVDLSIAR-OH), and its analogues was studied “in vivo” after intravenous administration to rats. Rat fibrinopeptide B (FPB) caused a significant increase in the count of circulating endothelial cell carcasses at the do...
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| Veröffentlicht in: | Thrombosis research 1994-05, Vol.74 (4), p.409-418 |
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| creator | Šimák, Jan Holada, Karel Zábrodský, Vladimir Komalik, František |
| description | The endothelial desquamating activity of the synthetic rat fibrinopeptide B (ATTDSDKVDLSIAR-OH), and its analogues was studied “in vivo” after intravenous administration to rats. Rat fibrinopeptide B (FPB) caused a significant increase in the count of circulating endothelial cell carcasses at the dose of 100 nmol/kg. Maximal effect reaching about 270% of the normal value was achieved with the dose of 600 nmol/kg in 30 min. after the injection. No significant thrombocytopenia, no hemolysis and no other life-threatening complications were observed. The same endothelial desquamating effect was achieved with N-terminal FPB(1–7) peptide ATTDSDK-OH, but very low activity exhibited the two FPB mutant peptides: ATDSDKVDLSIAR-OH and ATTNSNK-OH. Our results indicate that N-terminal sequence (1–7) consisting of N-terminal “pig tail” (ATT), acid region (DSD) and basic aminoacid (K) is responsible for endothelial desquamating activity of rat FPB. Similar corresponding sequences may be reconized in FPB of different species. The conservation of this common “active site” sequence is less apparent in primates. |
| doi_str_mv | 10.1016/0049-3848(94)90156-2 |
| format | Article |
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Rat fibrinopeptide B (FPB) caused a significant increase in the count of circulating endothelial cell carcasses at the dose of 100 nmol/kg. Maximal effect reaching about 270% of the normal value was achieved with the dose of 600 nmol/kg in 30 min. after the injection. No significant thrombocytopenia, no hemolysis and no other life-threatening complications were observed. The same endothelial desquamating effect was achieved with N-terminal FPB(1–7) peptide ATTDSDK-OH, but very low activity exhibited the two FPB mutant peptides: ATDSDKVDLSIAR-OH and ATTNSNK-OH. Our results indicate that N-terminal sequence (1–7) consisting of N-terminal “pig tail” (ATT), acid region (DSD) and basic aminoacid (K) is responsible for endothelial desquamating activity of rat FPB. Similar corresponding sequences may be reconized in FPB of different species. The conservation of this common “active site” sequence is less apparent in primates.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/0049-3848(94)90156-2</identifier><identifier>PMID: 8085242</identifier><identifier>CODEN: THBRAA</identifier><language>eng</language><publisher>New York, NY: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites - physiology ; Biological and medical sciences ; Blood and lymphatic vessels ; Cardiology. Vascular system ; endothelial cells ; Endothelium, Vascular - drug effects ; Female ; fibrinogen ; fibrinopeptide B ; Fibrinopeptide B - chemistry ; Fibrinopeptide B - pharmacology ; Keratolytic Agents - chemistry ; Keratolytic Agents - pharmacology ; Medical sciences ; Miscellaneous ; Molecular Sequence Data ; Rats ; Rats, Wistar ; Sequence Homology, Amino Acid ; Species Specificity ; thrombin ; vessel wall</subject><ispartof>Thrombosis research, 1994-05, Vol.74 (4), p.409-418</ispartof><rights>1994</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c335t-4a56244a5a6b607e9d52bee2512df72f9adf3dc1f0fd49647660f93a98450fdb3</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(94)90156-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4236888$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8085242$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Šimák, Jan</creatorcontrib><creatorcontrib>Holada, Karel</creatorcontrib><creatorcontrib>Zábrodský, Vladimir</creatorcontrib><creatorcontrib>Komalik, František</creatorcontrib><title>Endothelial desquamating activity of rat synthetic fibrinopeptide b and its analogues “in vivo” : Identification of responsible sequence</title><title>Thrombosis research</title><addtitle>Thromb Res</addtitle><description>The endothelial desquamating activity of the synthetic rat fibrinopeptide B (ATTDSDKVDLSIAR-OH), and its analogues was studied “in vivo” after intravenous administration to rats. Rat fibrinopeptide B (FPB) caused a significant increase in the count of circulating endothelial cell carcasses at the dose of 100 nmol/kg. Maximal effect reaching about 270% of the normal value was achieved with the dose of 600 nmol/kg in 30 min. after the injection. No significant thrombocytopenia, no hemolysis and no other life-threatening complications were observed. The same endothelial desquamating effect was achieved with N-terminal FPB(1–7) peptide ATTDSDK-OH, but very low activity exhibited the two FPB mutant peptides: ATDSDKVDLSIAR-OH and ATTNSNK-OH. Our results indicate that N-terminal sequence (1–7) consisting of N-terminal “pig tail” (ATT), acid region (DSD) and basic aminoacid (K) is responsible for endothelial desquamating activity of rat FPB. Similar corresponding sequences may be reconized in FPB of different species. The conservation of this common “active site” sequence is less apparent in primates.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites - physiology</subject><subject>Biological and medical sciences</subject><subject>Blood and lymphatic vessels</subject><subject>Cardiology. Vascular system</subject><subject>endothelial cells</subject><subject>Endothelium, Vascular - drug effects</subject><subject>Female</subject><subject>fibrinogen</subject><subject>fibrinopeptide B</subject><subject>Fibrinopeptide B - chemistry</subject><subject>Fibrinopeptide B - pharmacology</subject><subject>Keratolytic Agents - chemistry</subject><subject>Keratolytic Agents - pharmacology</subject><subject>Medical sciences</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>thrombin</subject><subject>vessel wall</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1uFDEQRi0ECkPgBiB5gRAsGmy3-8dZIKEoQKRIbGBtue1yKNRjd9rukWaXA3CE5HI5CZ7MaJZsXJLr1WfrFSGvOfvIGW8_MSZVVfeyf6_kB8V401biCVnxvlOVkJ14SlZH5Dl5kdIfxnjHVXNCTnrWN0KKFfl7EVzMv2FEM1IH6WYxa5MxXFNjM24wb2n0dDaZpm0oXEZLPQ4zhjjBlNEBHagJjmJOpZoxXi-Q6MPtHQa6wU18uL2nZ_TSQcjo0ZbsGB4jIU0xJBxGoAluFggWXpJn3owJXh3qKfn19eLn-ffq6se3y_MvV5Wt6yZX0jStkOU07dCyDpRrxAAgGi6c74RXxvnaWe6Zd1K1smtb5lVtVC-bcjXUp-TdPneaY3k5Zb3GZGEcTYC4JN21HesUVwWUe9DOMaUZvJ5mXJt5qznTuyXonWG9M6yV1I9L0KKMvTnkL8Ma3HHoYL303x76Jlkz-tkEi-mIFaLt-75gn_cYFBcbhFkniztPDmewWbuI___HP_TTp_8</recordid><startdate>19940515</startdate><enddate>19940515</enddate><creator>Šimák, Jan</creator><creator>Holada, Karel</creator><creator>Zábrodský, Vladimir</creator><creator>Komalik, František</creator><general>Elsevier Ltd</general><general>Elsevier Science</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>19940515</creationdate><title>Endothelial desquamating activity of rat synthetic fibrinopeptide b and its analogues “in vivo” : Identification of responsible sequence</title><author>Šimák, Jan ; Holada, Karel ; Zábrodský, Vladimir ; Komalik, František</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-4a56244a5a6b607e9d52bee2512df72f9adf3dc1f0fd49647660f93a98450fdb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites - physiology</topic><topic>Biological and medical sciences</topic><topic>Blood and lymphatic vessels</topic><topic>Cardiology. Vascular system</topic><topic>endothelial cells</topic><topic>Endothelium, Vascular - drug effects</topic><topic>Female</topic><topic>fibrinogen</topic><topic>fibrinopeptide B</topic><topic>Fibrinopeptide B - chemistry</topic><topic>Fibrinopeptide B - pharmacology</topic><topic>Keratolytic Agents - chemistry</topic><topic>Keratolytic Agents - pharmacology</topic><topic>Medical sciences</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>thrombin</topic><topic>vessel wall</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Šimák, Jan</creatorcontrib><creatorcontrib>Holada, Karel</creatorcontrib><creatorcontrib>Zábrodský, Vladimir</creatorcontrib><creatorcontrib>Komalik, František</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 research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Šimák, Jan</au><au>Holada, Karel</au><au>Zábrodský, Vladimir</au><au>Komalik, František</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endothelial desquamating activity of rat synthetic fibrinopeptide b and its analogues “in vivo” : Identification of responsible sequence</atitle><jtitle>Thrombosis research</jtitle><addtitle>Thromb Res</addtitle><date>1994-05-15</date><risdate>1994</risdate><volume>74</volume><issue>4</issue><spage>409</spage><epage>418</epage><pages>409-418</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><coden>THBRAA</coden><abstract>The endothelial desquamating activity of the synthetic rat fibrinopeptide B (ATTDSDKVDLSIAR-OH), and its analogues was studied “in vivo” after intravenous administration to rats. Rat fibrinopeptide B (FPB) caused a significant increase in the count of circulating endothelial cell carcasses at the dose of 100 nmol/kg. Maximal effect reaching about 270% of the normal value was achieved with the dose of 600 nmol/kg in 30 min. after the injection. No significant thrombocytopenia, no hemolysis and no other life-threatening complications were observed. The same endothelial desquamating effect was achieved with N-terminal FPB(1–7) peptide ATTDSDK-OH, but very low activity exhibited the two FPB mutant peptides: ATDSDKVDLSIAR-OH and ATTNSNK-OH. Our results indicate that N-terminal sequence (1–7) consisting of N-terminal “pig tail” (ATT), acid region (DSD) and basic aminoacid (K) is responsible for endothelial desquamating activity of rat FPB. Similar corresponding sequences may be reconized in FPB of different species. The conservation of this common “active site” sequence is less apparent in primates.</abstract><cop>New York, NY</cop><pub>Elsevier Ltd</pub><pmid>8085242</pmid><doi>10.1016/0049-3848(94)90156-2</doi><tpages>10</tpages></addata></record> |
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| ispartof | Thrombosis research, 1994-05, Vol.74 (4), p.409-418 |
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| subjects | Amino Acid Sequence Animals Binding Sites - physiology Biological and medical sciences Blood and lymphatic vessels Cardiology. Vascular system endothelial cells Endothelium, Vascular - drug effects Female fibrinogen fibrinopeptide B Fibrinopeptide B - chemistry Fibrinopeptide B - pharmacology Keratolytic Agents - chemistry Keratolytic Agents - pharmacology Medical sciences Miscellaneous Molecular Sequence Data Rats Rats, Wistar Sequence Homology, Amino Acid Species Specificity thrombin vessel wall |
| title | Endothelial desquamating activity of rat synthetic fibrinopeptide b and its analogues “in vivo” : Identification of responsible sequence |
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