{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T21:56:48Z","timestamp":1787003808570,"version":"build-2736575974"},"reference-count":41,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2009,1,29]],"date-time":"2009-01-29T00:00:00Z","timestamp":1233187200000},"content-version":"vor","delay-in-days":2919,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bpspubs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["British J Pharmacology"],"published-print":{"date-parts":[[2001,2]]},"abstract":"<jats:p>\n                    <jats:list list-type=\"explicit-label\">\n                      <jats:list-item>\n                        <jats:p>\n                          Agkistin, purified from the snake venom of Formosan\n                          <jats:italic>Agkistrodon acutus<\/jats:italic>\n                          , belongs to the family of C\u2010type lectin GPIb binding proteins. It is a heterodimeric molecule, consisting of \u03b1\u2010 (16.5\u2003kDa) and \u03b2\u2010 (15.5\u2003kDa) subunits with a molecular mass of 32,512 Daltons examined by SDS\u2003\u2013\u2003PAGE and mass spectrometry.\n                        <\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:p>\n                          <jats:italic>In vitro<\/jats:italic>\n                          , agkistin concentration\u2010dependently inhibited ristocetin\u2010induced human platelet agglutination and aggregation in the presence of vWF. It also inhibited TXA\n                          <jats:sub>2<\/jats:sub>\n                          formation and prolonged the latent period in triggering aggregation by a low concentration of thrombin (0.03\u2003u\u2003ml\n                          <jats:sup>\u22121<\/jats:sup>\n                          ).\n                        <\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:p>\n                          <jats:sup>125<\/jats:sup>\n                          I\u2010agkistin specifically bound to unactivated human platelets in a saturable manner with a K\n                          <jats:sub>D<\/jats:sub>\n                          value of 223\u00b110.6\u2003n\n                          <jats:sc>M<\/jats:sc>\n                          . This binding reaction was rapid and reversible. Monoclonal antibodies, AP1 and 6D1 raised against platelet GPIb, almost completely blocked\n                          <jats:sup>125<\/jats:sup>\n                          I\u2010agkistin binding to platelets. However, monoclonal antibody 7E3 raised against GPIIb\/IIIa complex, trigramin, a GPIIb\/IIIa antagonist, ADP and EDTA did not affect\n                          <jats:sup>125<\/jats:sup>\n                          I\u2010agkistin binding reaction.\n                        <\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:p>\n                          Agkistin (250\u2003\u03bcg\u2003kg\n                          <jats:sup>\u22121<\/jats:sup>\n                          ) significantly prolonged the bleeding time and induced transient thrombocytopenia of mice when given intravenously. Furthermore, it markedly inhibited platelet plug formation in irradiated mesenteric venules of fluorescein\u2010treated mice\n                          <jats:italic>in vivo<\/jats:italic>\n                          .\n                        <\/jats:p>\n                      <\/jats:list-item>\n                      <jats:list-item>\n                        <jats:p>\n                          In conclusion, agkistin inhibits ristocetin induced platelet aggregation mainly through its specific binding to platelet GPIb, thereby blocking the interaction between GPIb and vWF. In addition, agkistin exhibits antithrombotic activity\n                          <jats:italic>in vivo<\/jats:italic>\n                          .\n                        <\/jats:p>\n                      <\/jats:list-item>\n                    <\/jats:list>\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>British Journal of Pharmacology<\/jats:italic>\n                    (2001)\n                    <jats:bold>132<\/jats:bold>\n                    , 843\u2013850; doi:\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" xlink:href=\"10.1038\/sj.bjp.0703865\">10.1038\/sj.bjp.0703865<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1038\/sj.bjp.0703865","type":"journal-article","created":{"date-parts":[[2005,1,28]],"date-time":"2005-01-28T16:10:46Z","timestamp":1106928646000},"page":"843-850","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Pharmacological characterization and antithrombotic effect of agkistin, a platelet glycoprotein Ib antagonist"],"prefix":"10.1111","volume":"132","author":[{"given":"Chia\u2010Hsin","family":"Yeh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei\u2010Chi","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui\u2010Chin","family":"Peng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tur\u2010Fu","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1,29]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1161\/01.ATV.20.5.1347"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0049-3848(94)90051-5"},{"key":"e_1_2_7_4_1","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1182\/blood.V91.5.1582","article-title":"Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib agonist from venom of Crotalus atrox","volume":"91","author":"CHANG M.C.","year":"1998","journal-title":"Blood"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1995.1684"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1055\/s-2007-1000387"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI108778"},{"key":"e_1_2_7_8_1","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1182\/blood.V61.1.99.99","article-title":"Studies with a murine monoclonal antibody that abolishes ristocetin\u2010induced binding of von Willebrand factor to platelet: additional evidence in support of GPIb as a platelet receptor for von Willebrand factor","volume":"61","author":"COLLER B.S.","year":"1983","journal-title":"Blood"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI111931"},{"key":"e_1_2_7_10_1","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1055\/s-0038-1657230","article-title":"Bleeding time in rats: A comparison of different experimental conditions","volume":"48","author":"DEJANA E.","year":"1982","journal-title":"Thromb. 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