Complex-dependent inhibition of factor VIIa by antithrombin III and heparin
The regulation of the factor VIIa-tissue factor complex is essential for control of the hemostatic response. However, the role of the inhibitor antithrombin III in the regulation of factor VIIa has remained in question. The inhibition of factor VIIa activity by antithrombin III and heparin in the pr...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-01, Vol.268 (2), p.767-770 |
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| container_title | The Journal of biological chemistry |
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| creator | LAWSON, J. H BUTENAS, S RIBARIK, N MANN, K. G |
| description | The regulation of the factor VIIa-tissue factor complex is essential for control of the hemostatic response. However, the
role of the inhibitor antithrombin III in the regulation of factor VIIa has remained in question. The inhibition of factor
VIIa activity by antithrombin III and heparin in the presence and absence of tissue factor was evaluated using the fluorescent
substrate m-LGR-nds. Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in
the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1. In the presence of tissue factor, the rate constant for this reaction
increases to 5.6 x 10(3) M-1 s-1. A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent
molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A heterogeneous mixture
of factor VIIa products with molecular weights between 50,000 and 80,000, most likely representing proteolytically degraded
factor VIIa-antithrombin III complexes, was also observed. |
| doi_str_mv | 10.1016/S0021-9258(18)53998-3 |
| format | Article |
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role of the inhibitor antithrombin III in the regulation of factor VIIa has remained in question. The inhibition of factor
VIIa activity by antithrombin III and heparin in the presence and absence of tissue factor was evaluated using the fluorescent
substrate m-LGR-nds. Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in
the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1. In the presence of tissue factor, the rate constant for this reaction
increases to 5.6 x 10(3) M-1 s-1. A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent
molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A heterogeneous mixture
of factor VIIa products with molecular weights between 50,000 and 80,000, most likely representing proteolytically degraded
factor VIIa-antithrombin III complexes, was also observed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)53998-3</identifier><identifier>PMID: 8419351</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>antithrombin III ; Antithrombin III - pharmacology ; Biological and medical sciences ; Blood coagulation. Blood cells ; coagulation factor VIIa ; Coagulation factors ; Factor VIIa - antagonists & inhibitors ; Fundamental and applied biological sciences. Psychology ; heparin ; Heparin - pharmacology ; Humans ; Immunoblotting ; inhibition ; Kinetics ; man ; Mathematics ; Molecular and cellular biology ; Recombinant Proteins - antagonists & inhibitors ; Thromboplastin - metabolism</subject><ispartof>The Journal of biological chemistry, 1993-01, Vol.268 (2), p.767-770</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-1a81e7228f37998c58b95c7bcbff844384338f98252d114dd876d63c254fd7ef3</citedby><cites>FETCH-LOGICAL-c437t-1a81e7228f37998c58b95c7bcbff844384338f98252d114dd876d63c254fd7ef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4568202$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8419351$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LAWSON, J. H</creatorcontrib><creatorcontrib>BUTENAS, S</creatorcontrib><creatorcontrib>RIBARIK, N</creatorcontrib><creatorcontrib>MANN, K. G</creatorcontrib><title>Complex-dependent inhibition of factor VIIa by antithrombin III and heparin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The regulation of the factor VIIa-tissue factor complex is essential for control of the hemostatic response. However, the
role of the inhibitor antithrombin III in the regulation of factor VIIa has remained in question. The inhibition of factor
VIIa activity by antithrombin III and heparin in the presence and absence of tissue factor was evaluated using the fluorescent
substrate m-LGR-nds. Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in
the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1. In the presence of tissue factor, the rate constant for this reaction
increases to 5.6 x 10(3) M-1 s-1. A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent
molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A heterogeneous mixture
of factor VIIa products with molecular weights between 50,000 and 80,000, most likely representing proteolytically degraded
factor VIIa-antithrombin III complexes, was also observed.</description><subject>antithrombin III</subject><subject>Antithrombin III - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>coagulation factor VIIa</subject><subject>Coagulation factors</subject><subject>Factor VIIa - antagonists & inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>heparin</subject><subject>Heparin - pharmacology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>inhibition</subject><subject>Kinetics</subject><subject>man</subject><subject>Mathematics</subject><subject>Molecular and cellular biology</subject><subject>Recombinant Proteins - antagonists & inhibitors</subject><subject>Thromboplastin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtr3DAQgEVoSDZpf0LAgRLag1vrZY2PYUlT00AOfdCbkPWIFWzJkbwk-ff1Zpe9di4DM988-BC6wNUXXOH668-qIrhsCIdPGD5z2jRQ0iO0whXQknL89x1aHZBTdJbzY7UEa_AJOgGGm4VZoR_rOE6DfSmNnWwwNsyFD73v_OxjKKIrnNJzTMWftlVF91qoMPu5T3HsfCjatl0KpujtpJIP79GxU0O2H_b5HP3-dvNr_b28u79t19d3pWZUzCVWgK0gBBwVy9OaQ9dwLTrdOQeMUWCUgmuAcGIwZsaAqE1NNeHMGWEdPUdXu71Tik8bm2c5-qztMKhg4yZLwTnjAPS_IK4Z8JrxBeQ7UKeYc7JOTsmPKr1KXMmtbflmW25VSgzyzbbcHrjYH9h0ozWHqb3epf9x31dZq8ElFbTPB4zxGkhFFuxyh_X-oX_2ycrOR93bUZIaJJGiFvQfLw6ROQ</recordid><startdate>19930115</startdate><enddate>19930115</enddate><creator>LAWSON, J. H</creator><creator>BUTENAS, S</creator><creator>RIBARIK, N</creator><creator>MANN, K. G</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930115</creationdate><title>Complex-dependent inhibition of factor VIIa by antithrombin III and heparin</title><author>LAWSON, J. H ; BUTENAS, S ; RIBARIK, N ; MANN, K. G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-1a81e7228f37998c58b95c7bcbff844384338f98252d114dd876d63c254fd7ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>antithrombin III</topic><topic>Antithrombin III - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>coagulation factor VIIa</topic><topic>Coagulation factors</topic><topic>Factor VIIa - antagonists & inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>heparin</topic><topic>Heparin - pharmacology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>inhibition</topic><topic>Kinetics</topic><topic>man</topic><topic>Mathematics</topic><topic>Molecular and cellular biology</topic><topic>Recombinant Proteins - antagonists & inhibitors</topic><topic>Thromboplastin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LAWSON, J. H</creatorcontrib><creatorcontrib>BUTENAS, S</creatorcontrib><creatorcontrib>RIBARIK, N</creatorcontrib><creatorcontrib>MANN, K. G</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LAWSON, J. H</au><au>BUTENAS, S</au><au>RIBARIK, N</au><au>MANN, K. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complex-dependent inhibition of factor VIIa by antithrombin III and heparin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-01-15</date><risdate>1993</risdate><volume>268</volume><issue>2</issue><spage>767</spage><epage>770</epage><pages>767-770</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The regulation of the factor VIIa-tissue factor complex is essential for control of the hemostatic response. However, the
role of the inhibitor antithrombin III in the regulation of factor VIIa has remained in question. The inhibition of factor
VIIa activity by antithrombin III and heparin in the presence and absence of tissue factor was evaluated using the fluorescent
substrate m-LGR-nds. Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in
the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1. In the presence of tissue factor, the rate constant for this reaction
increases to 5.6 x 10(3) M-1 s-1. A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent
molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A heterogeneous mixture
of factor VIIa products with molecular weights between 50,000 and 80,000, most likely representing proteolytically degraded
factor VIIa-antithrombin III complexes, was also observed.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8419351</pmid><doi>10.1016/S0021-9258(18)53998-3</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | antithrombin III Antithrombin III - pharmacology Biological and medical sciences Blood coagulation. Blood cells coagulation factor VIIa Coagulation factors Factor VIIa - antagonists & inhibitors Fundamental and applied biological sciences. Psychology heparin Heparin - pharmacology Humans Immunoblotting inhibition Kinetics man Mathematics Molecular and cellular biology Recombinant Proteins - antagonists & inhibitors Thromboplastin - metabolism |
| title | Complex-dependent inhibition of factor VIIa by antithrombin III and heparin |
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