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Article: Characterization of factor VIII related protein synthesized by human endothelial cell: A study of structure and function

TitleCharacterization of factor VIII related protein synthesized by human endothelial cell: A study of structure and function
Authors
Issue Date1982
PublisherSchattauer GmbH. The Journal's web site is located at http://www.thrombosis-online.com
Citation
Thrombosis And Haemostasis, 1982, v. 48 n. 2, p. 177-181 How to Cite?
AbstractCrossed immunoelectrophoresis showed that factor VIII related protein (VIII R) synthesized in the human endothelial cell (EC-VIII R) had faster electrophoretic mobility than that secreted into the culture medium (MED-VIII R). Sodium dodecyl sulphate agarose gel electrophoresis followed by radioimmunofixation showed that EC-VIII R consisted of molecules varying from 0.26 x 106 to 3.76 x 106 daltons while MED-VIII R had molecules ranging from 0.93 x 106 to greater than 10 x 106 daltons, similar to that present in plasma. The smallest VIII R molecule present in normal plasma or spent culture medium (0.93 x 106 daltons) corresponded to a tetramer of subunits of 0.22-0.24 x 106 daltons. Only molecular forms greater than 3.76 x 106 daltons possessed ristocetin cofactor activity. Sonication (15 μ amplitude for 30 secs) effectively broke the non-covalent bonds of the VIII R multimers resulting in smaller molecules. Thus endothelial cells in culture synthesized VIII R subunits and assembled them into the higher multimeric forms on secretion. Different types of von Willebrand disease could result from defects of either of the two processes.
Persistent Identifierhttp://hdl.handle.net/10722/161670
ISSN
2015 Impact Factor: 5.255
2015 SCImago Journal Rankings: 2.089
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Ven_US
dc.contributor.authorChan, TKen_US
dc.date.accessioned2012-09-05T05:13:44Z-
dc.date.available2012-09-05T05:13:44Z-
dc.date.issued1982en_US
dc.identifier.citationThrombosis And Haemostasis, 1982, v. 48 n. 2, p. 177-181en_US
dc.identifier.issn0340-6245en_US
dc.identifier.urihttp://hdl.handle.net/10722/161670-
dc.description.abstractCrossed immunoelectrophoresis showed that factor VIII related protein (VIII R) synthesized in the human endothelial cell (EC-VIII R) had faster electrophoretic mobility than that secreted into the culture medium (MED-VIII R). Sodium dodecyl sulphate agarose gel electrophoresis followed by radioimmunofixation showed that EC-VIII R consisted of molecules varying from 0.26 x 106 to 3.76 x 106 daltons while MED-VIII R had molecules ranging from 0.93 x 106 to greater than 10 x 106 daltons, similar to that present in plasma. The smallest VIII R molecule present in normal plasma or spent culture medium (0.93 x 106 daltons) corresponded to a tetramer of subunits of 0.22-0.24 x 106 daltons. Only molecular forms greater than 3.76 x 106 daltons possessed ristocetin cofactor activity. Sonication (15 μ amplitude for 30 secs) effectively broke the non-covalent bonds of the VIII R multimers resulting in smaller molecules. Thus endothelial cells in culture synthesized VIII R subunits and assembled them into the higher multimeric forms on secretion. Different types of von Willebrand disease could result from defects of either of the two processes.en_US
dc.languageengen_US
dc.publisherSchattauer GmbH. The Journal's web site is located at http://www.thrombosis-online.comen_US
dc.relation.ispartofThrombosis and Haemostasisen_US
dc.subject.meshAntigens - Analysisen_US
dc.subject.meshCryoglobulins - Analysisen_US
dc.subject.meshEndothelium - Cytology - Metabolismen_US
dc.subject.meshFactor Viii - Analysis - Biosynthesis - Immunologyen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoelectrophoresis, Two-Dimensionalen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshRistocetin - Metabolismen_US
dc.subject.meshSonicationen_US
dc.subject.meshVon Willebrand Factoren_US
dc.titleCharacterization of factor VIII related protein synthesized by human endothelial cell: A study of structure and functionen_US
dc.typeArticleen_US
dc.identifier.emailChan, V:vnychana@hkucc.hku.hken_US
dc.identifier.authorityChan, V=rp00320en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid6817445-
dc.identifier.scopuseid_2-s2.0-0020419545en_US
dc.identifier.volume48en_US
dc.identifier.issue2en_US
dc.identifier.spage177en_US
dc.identifier.epage181en_US
dc.identifier.isiWOS:A1982PR13700015-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridChan, V=7202654865en_US
dc.identifier.scopusauthoridChan, TK=7402687762en_US

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