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Article: Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1

TitleRedox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1
Authors
KeywordsPlatelet adhesion
β2-glycoprotein I
Von Willebrand factor
Thioredoxin
Oxidoreductase
Issue Date2010
Citation
Journal of Thrombosis and Haemostasis, 2010, v. 8, n. 8, p. 1754-1762 How to Cite?
AbstractBackground: β 2 -Glycoprotein I (β 2 GPI) is an abundant plasma protein that is closely linked to blood clotting, as it interacts with various protein and cellular components of the coagulation system. However, the role of β 2 GPI in thrombus formation is unknown. We have recently shown that β 2 GPI is susceptible to reduction by the thiol oxidoreductases thioredoxin-1 and protein disulfide isomerase, and that reduction of β 2 GPI can take place on the platelet surface. Methods: β 2 GPI, reduced by thioredoxin-1, was labeled with the selective sulfhydryl probe N a -(3-maleimidylpropionyl)biocytin and subjected to mass spectrometry to identify the specific cysteines involved in the thiol exchange reaction. Binding assays were used to examine the affinity of reduced β 2 GPI for von Willebrand factor (VWF) and the effect of reduced β2GPI on glycoprotein (GP)Ibα binding to VWF. Platelet adhesion to ristocetin-activated VWF was studied in the presence of reduced β 2 GPI. Results: We demonstrate that the Cys288-Cys326 disulfide in domain V of β 2 GPI is the predominant disulfide reduced by thioredoxin-1. Reduced β 2 GPI in vitro displays increased binding to VWF that is dependent on disulfide bond formation. β 2 GPI reduced by thioredoxin-1, in comparison with non-reduced β 2 GPI, leads to increased binding of GPIbα to VWF and increased platelet adhesion to activated VWF. Conclusions: Given the importance of thiol oxidoreductases in thrombus formation, we provide preliminary evidence that the thiol-dependent interaction of β 2 GPI with VWF may contribute to the redox regulation of platelet adhesion. © 2010 International Society on Thrombosis and Haemostasis.
Persistent Identifierhttp://hdl.handle.net/10722/250951
ISSN
2021 Impact Factor: 16.036
2020 SCImago Journal Rankings: 1.947
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorPassam, F. H.-
dc.contributor.authorRahgozar, S.-
dc.contributor.authorQi, M.-
dc.contributor.authorRaftery, M. J.-
dc.contributor.authorWong, J. W.H.-
dc.contributor.authorTanaka, K.-
dc.contributor.authorIoannou, Y.-
dc.contributor.authorZhang, J. Y.-
dc.contributor.authorGemmell, R.-
dc.contributor.authorQi, J. C.-
dc.contributor.authorGiannakopoulos, B.-
dc.contributor.authorHughes, W. E.-
dc.contributor.authorHogg, P. J.-
dc.contributor.authorKrilis, S. A.-
dc.date.accessioned2018-02-01T01:54:10Z-
dc.date.available2018-02-01T01:54:10Z-
dc.date.issued2010-
dc.identifier.citationJournal of Thrombosis and Haemostasis, 2010, v. 8, n. 8, p. 1754-1762-
dc.identifier.issn1538-7933-
dc.identifier.urihttp://hdl.handle.net/10722/250951-
dc.description.abstractBackground: β 2 -Glycoprotein I (β 2 GPI) is an abundant plasma protein that is closely linked to blood clotting, as it interacts with various protein and cellular components of the coagulation system. However, the role of β 2 GPI in thrombus formation is unknown. We have recently shown that β 2 GPI is susceptible to reduction by the thiol oxidoreductases thioredoxin-1 and protein disulfide isomerase, and that reduction of β 2 GPI can take place on the platelet surface. Methods: β 2 GPI, reduced by thioredoxin-1, was labeled with the selective sulfhydryl probe N a -(3-maleimidylpropionyl)biocytin and subjected to mass spectrometry to identify the specific cysteines involved in the thiol exchange reaction. Binding assays were used to examine the affinity of reduced β 2 GPI for von Willebrand factor (VWF) and the effect of reduced β2GPI on glycoprotein (GP)Ibα binding to VWF. Platelet adhesion to ristocetin-activated VWF was studied in the presence of reduced β 2 GPI. Results: We demonstrate that the Cys288-Cys326 disulfide in domain V of β 2 GPI is the predominant disulfide reduced by thioredoxin-1. Reduced β 2 GPI in vitro displays increased binding to VWF that is dependent on disulfide bond formation. β 2 GPI reduced by thioredoxin-1, in comparison with non-reduced β 2 GPI, leads to increased binding of GPIbα to VWF and increased platelet adhesion to activated VWF. Conclusions: Given the importance of thiol oxidoreductases in thrombus formation, we provide preliminary evidence that the thiol-dependent interaction of β 2 GPI with VWF may contribute to the redox regulation of platelet adhesion. © 2010 International Society on Thrombosis and Haemostasis.-
dc.languageeng-
dc.relation.ispartofJournal of Thrombosis and Haemostasis-
dc.subjectPlatelet adhesion-
dc.subjectβ2-glycoprotein I-
dc.subjectVon Willebrand factor-
dc.subjectThioredoxin-
dc.subjectOxidoreductase-
dc.titleRedox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1538-7836.2010.03944.x-
dc.identifier.pmid20979592-
dc.identifier.scopuseid_2-s2.0-77956918612-
dc.identifier.volume8-
dc.identifier.issue8-
dc.identifier.spage1754-
dc.identifier.epage1762-
dc.identifier.eissn1538-7836-
dc.identifier.isiWOS:000280646300014-
dc.identifier.issnl1538-7836-

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