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- Publisher Website: 10.1111/j.1538-7836.2010.03944.x
- Scopus: eid_2-s2.0-77956918612
- PMID: 20979592
- WOS: WOS:000280646300014
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Article: Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1
Title | Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1 |
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Authors | |
Keywords | Platelet adhesion β2-glycoprotein I Von Willebrand factor Thioredoxin Oxidoreductase |
Issue Date | 2010 |
Citation | Journal of Thrombosis and Haemostasis, 2010, v. 8, n. 8, p. 1754-1762 How to Cite? |
Abstract | Background: 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 Identifier | http://hdl.handle.net/10722/250951 |
ISSN | 2023 Impact Factor: 5.5 2023 SCImago Journal Rankings: 2.128 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Passam, F. H. | - |
dc.contributor.author | Rahgozar, S. | - |
dc.contributor.author | Qi, M. | - |
dc.contributor.author | Raftery, M. J. | - |
dc.contributor.author | Wong, J. W.H. | - |
dc.contributor.author | Tanaka, K. | - |
dc.contributor.author | Ioannou, Y. | - |
dc.contributor.author | Zhang, J. Y. | - |
dc.contributor.author | Gemmell, R. | - |
dc.contributor.author | Qi, J. C. | - |
dc.contributor.author | Giannakopoulos, B. | - |
dc.contributor.author | Hughes, W. E. | - |
dc.contributor.author | Hogg, P. J. | - |
dc.contributor.author | Krilis, S. A. | - |
dc.date.accessioned | 2018-02-01T01:54:10Z | - |
dc.date.available | 2018-02-01T01:54:10Z | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Journal of Thrombosis and Haemostasis, 2010, v. 8, n. 8, p. 1754-1762 | - |
dc.identifier.issn | 1538-7933 | - |
dc.identifier.uri | http://hdl.handle.net/10722/250951 | - |
dc.description.abstract | Background: 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.language | eng | - |
dc.relation.ispartof | Journal of Thrombosis and Haemostasis | - |
dc.subject | Platelet adhesion | - |
dc.subject | β2-glycoprotein I | - |
dc.subject | Von Willebrand factor | - |
dc.subject | Thioredoxin | - |
dc.subject | Oxidoreductase | - |
dc.title | Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1 | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1111/j.1538-7836.2010.03944.x | - |
dc.identifier.pmid | 20979592 | - |
dc.identifier.scopus | eid_2-s2.0-77956918612 | - |
dc.identifier.volume | 8 | - |
dc.identifier.issue | 8 | - |
dc.identifier.spage | 1754 | - |
dc.identifier.epage | 1762 | - |
dc.identifier.eissn | 1538-7836 | - |
dc.identifier.isi | WOS:000280646300014 | - |
dc.identifier.issnl | 1538-7836 | - |