Endocytosis of Fibrinogen Into Megakaryocyte and Platelet α-Granules Is Mediated by αIIbβ3 (Glycoprotein Ilb-IIIa)
Recently, we showed that platelet α-granule fibrinogen is derived entirely from endocytic uptake and not from megakaryocyte synthesis, as previously thought. In this present report, we identify the receptor that mediates endocytosis. We have found that barbourin, a unique disintegrin that is a speci...
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| Veröffentlicht in: | Blood 1993-07, Vol.82 (1), p.135-138 |
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| creator | Handagama, Prem Scarborough, Robert M. Shuman, Marc A. Bainton, Dorothy F. |
| description | Recently, we showed that platelet α-granule fibrinogen is derived entirely from endocytic uptake and not from megakaryocyte synthesis, as previously thought. In this present report, we identify the receptor that mediates endocytosis. We have found that barbourin, a unique disintegrin that is a specific antagonist of αIIbβ3, inhibits the endocytic uptake of fibrinogen into α-granules. Continuous intravenous infusion of barbourin (200 µg/h) into guinea pigs blocked collagen-induced platelet aggregation as well as endocytosis of biotinylated fibrinogen into megakaryocytes; however, endocytosis of biotinylated albumin by megakaryocytes was not affected. Thus, we have shown that endocytosis of fibrinogen into megakaryocyte and platelet α-granules is receptor-mediated, and that αIIbβ3 is the primary receptor. |
| doi_str_mv | 10.1182/blood.V82.1.135.bloodjournal821135 |
| format | Article |
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In this present report, we identify the receptor that mediates endocytosis. We have found that barbourin, a unique disintegrin that is a specific antagonist of αIIbβ3, inhibits the endocytic uptake of fibrinogen into α-granules. Continuous intravenous infusion of barbourin (200 µg/h) into guinea pigs blocked collagen-induced platelet aggregation as well as endocytosis of biotinylated fibrinogen into megakaryocytes; however, endocytosis of biotinylated albumin by megakaryocytes was not affected. Thus, we have shown that endocytosis of fibrinogen into megakaryocyte and platelet α-granules is receptor-mediated, and that αIIbβ3 is the primary receptor.</description><identifier>ISSN: 0006-4971</identifier><identifier>EISSN: 1528-0020</identifier><identifier>DOI: 10.1182/blood.V82.1.135.bloodjournal821135</identifier><language>eng</language><publisher>Washington, DC: Elsevier Inc</publisher><subject>Biological and medical sciences ; Blood coagulation. 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In this present report, we identify the receptor that mediates endocytosis. We have found that barbourin, a unique disintegrin that is a specific antagonist of αIIbβ3, inhibits the endocytic uptake of fibrinogen into α-granules. Continuous intravenous infusion of barbourin (200 µg/h) into guinea pigs blocked collagen-induced platelet aggregation as well as endocytosis of biotinylated fibrinogen into megakaryocytes; however, endocytosis of biotinylated albumin by megakaryocytes was not affected. Thus, we have shown that endocytosis of fibrinogen into megakaryocyte and platelet α-granules is receptor-mediated, and that αIIbβ3 is the primary receptor.</description><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Fundamental and applied biological sciences. 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Blood cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Molecular and cellular biology</topic><topic>Platelet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Handagama, Prem</creatorcontrib><creatorcontrib>Scarborough, Robert M.</creatorcontrib><creatorcontrib>Shuman, Marc A.</creatorcontrib><creatorcontrib>Bainton, Dorothy F.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><jtitle>Blood</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Handagama, Prem</au><au>Scarborough, Robert M.</au><au>Shuman, Marc A.</au><au>Bainton, Dorothy F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endocytosis of Fibrinogen Into Megakaryocyte and Platelet α-Granules Is Mediated by αIIbβ3 (Glycoprotein Ilb-IIIa)</atitle><jtitle>Blood</jtitle><date>1993-07-01</date><risdate>1993</risdate><volume>82</volume><issue>1</issue><spage>135</spage><epage>138</epage><pages>135-138</pages><issn>0006-4971</issn><eissn>1528-0020</eissn><abstract>Recently, we showed that platelet α-granule fibrinogen is derived entirely from endocytic uptake and not from megakaryocyte synthesis, as previously thought. In this present report, we identify the receptor that mediates endocytosis. We have found that barbourin, a unique disintegrin that is a specific antagonist of αIIbβ3, inhibits the endocytic uptake of fibrinogen into α-granules. Continuous intravenous infusion of barbourin (200 µg/h) into guinea pigs blocked collagen-induced platelet aggregation as well as endocytosis of biotinylated fibrinogen into megakaryocytes; however, endocytosis of biotinylated albumin by megakaryocytes was not affected. Thus, we have shown that endocytosis of fibrinogen into megakaryocyte and platelet α-granules is receptor-mediated, and that αIIbβ3 is the primary receptor.</abstract><cop>Washington, DC</cop><pub>Elsevier Inc</pub><doi>10.1182/blood.V82.1.135.bloodjournal821135</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Blood, 1993-07, Vol.82 (1), p.135-138 |
| issn | 0006-4971 1528-0020 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_4849116 |
| source | EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Blood coagulation. Blood cells Fundamental and applied biological sciences. Psychology Molecular and cellular biology Platelet |
| title | Endocytosis of Fibrinogen Into Megakaryocyte and Platelet α-Granules Is Mediated by αIIbβ3 (Glycoprotein Ilb-IIIa) |
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