Inhibitory Spectrum of α2-plasmin Inhibitor
α2-Plasmin inhibitor (α2PI) has been recently characterized as a fast-reacting inhibitor of plasmin in human plasma and appears to play an important role in the regulation of fibrinolysis in vivo. We have studied the effect of purified α2PI upon various proteases participating in human blood coagula...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1979-04, Vol.76 (4), p.2013-2017 |
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| container_issue | 4 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 76 |
| creator | Saito, Hidehiko Goldsmith, George H. Moroi, Masaaki Aoki, Nobuo |
| description | α2-Plasmin inhibitor (α2PI) has been recently characterized as a fast-reacting inhibitor of plasmin in human plasma and appears to play an important role in the regulation of fibrinolysis in vivo. We have studied the effect of purified α2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 μ g/ml), α2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. α2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). α2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhnace the inhibitory function of α2PI. These results suggest that, like other plasma protease inhibitors, α2PI possesses a broad in vitro spectrum of inhibitory properties. |
| doi_str_mv | 10.1073/pnas.76.4.2013 |
| format | Article |
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We have studied the effect of purified α2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 μ g/ml), α2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. α2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). α2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhnace the inhibitory function of α2PI. 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We have studied the effect of purified α2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 μ g/ml), α2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. α2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). α2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhnace the inhibitory function of α2PI. These results suggest that, like other plasma protease inhibitors, α2PI possesses a broad in vitro spectrum of inhibitory properties.</description><subject>Albumins</subject><subject>Antithrombins</subject><subject>Blood coagulation</subject><subject>Blood plasma</subject><subject>Clotting</subject><subject>Enzymes</subject><subject>Gels</subject><subject>Heparin</subject><subject>Sodium</subject><subject>Ungulates</subject><issn>0027-8424</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNo9jbtOwzAUQD2ARCldGZjyATjc3Gtf2yOqeFSqxNDu1Y1xRaImjeIw9LP4Eb6JSiCmsxydo9RtBWUFjh6GXnLpuDQlQkUXagaATnuD5kpd59wCQLAeZup-1X80dTMdx1OxGVKcxs-uOO6L7y_Uw0Fy1_TFv3KjLvdyyGnxx7naPj9tl696_fayWj6udevdpP17TGSDDyGwxUSE4kGSENbJR4himRI6thYw0FlmSIjsoK4MRi80V3e_2Tafp7thbDoZTzsObJh-AGovP0I</recordid><startdate>19790401</startdate><enddate>19790401</enddate><creator>Saito, Hidehiko</creator><creator>Goldsmith, George H.</creator><creator>Moroi, Masaaki</creator><creator>Aoki, Nobuo</creator><general>National Academy of Sciences of the United States of America</general><scope/></search><sort><creationdate>19790401</creationdate><title>Inhibitory Spectrum of α2-plasmin Inhibitor</title><author>Saito, Hidehiko ; Goldsmith, George H. ; Moroi, Masaaki ; Aoki, Nobuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j87t-8dce3598999652e332a80aea32be8c0ca563e276550293dce60e22670b142c8a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Albumins</topic><topic>Antithrombins</topic><topic>Blood coagulation</topic><topic>Blood plasma</topic><topic>Clotting</topic><topic>Enzymes</topic><topic>Gels</topic><topic>Heparin</topic><topic>Sodium</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saito, Hidehiko</creatorcontrib><creatorcontrib>Goldsmith, George H.</creatorcontrib><creatorcontrib>Moroi, Masaaki</creatorcontrib><creatorcontrib>Aoki, Nobuo</creatorcontrib><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saito, Hidehiko</au><au>Goldsmith, George H.</au><au>Moroi, Masaaki</au><au>Aoki, Nobuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibitory Spectrum of α2-plasmin Inhibitor</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1979-04-01</date><risdate>1979</risdate><volume>76</volume><issue>4</issue><spage>2013</spage><epage>2017</epage><pages>2013-2017</pages><issn>0027-8424</issn><abstract>α2-Plasmin inhibitor (α2PI) has been recently characterized as a fast-reacting inhibitor of plasmin in human plasma and appears to play an important role in the regulation of fibrinolysis in vivo. We have studied the effect of purified α2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 μ g/ml), α2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. α2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). α2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhnace the inhibitory function of α2PI. These results suggest that, like other plasma protease inhibitors, α2PI possesses a broad in vitro spectrum of inhibitory properties.</abstract><pub>National Academy of Sciences of the United States of America</pub><doi>10.1073/pnas.76.4.2013</doi><tpages>5</tpages></addata></record> |
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| language | eng |
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| source | PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Albumins Antithrombins Blood coagulation Blood plasma Clotting Enzymes Gels Heparin Sodium Ungulates |
| title | Inhibitory Spectrum of α2-plasmin Inhibitor |
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