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Inhibition of the intrinsic factor X activating complex by protein S: evidence for a specific binding of protein S to factor VIII

Autor: SJ Koppelman, TM Hackeng, JJ Sixma, BN Bouma

Publikováno v: Blood. 86:1062-1071

Protein S is a vitamin K-dependent nonenzymatic anticoagulant protein that acts as a cofactor to activated protein C. Recently it was shown that protein S inhibits the prothrombinase reaction independent of activated protein C. In this study, we show

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6d6e9d47ec59ee468649a6c23e378653
https://doi.org/10.1182/blood.v86.3.1062.bloodjournal8631062

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Antiphospholipid antibodies directed against a combination of phospholipids with prothrombin, protein C, or protein S: an explanation for their pathogenic mechanism? [see comments]

Autor: JD Oosting, RH Derksen, IW Bobbink, TM Hackeng, BN Bouma, PG de Groot

Publikováno v: Blood. 81:2618-2625

Despite many studies on the pathophysiology of antiphospholipid antibodies (aPL), the mechanism by which aPL causes thrombosis has not been established. We have tried to elucidate the paradox between the prolongation of the clotting time of phospholi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f67c8027c41987b5b3f98a60e24b75cd
https://doi.org/10.1182/blood.v81.10.2618.bloodjournal81102618

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Synergistic inhibition of the intrinsic factor X activation by protein S and C4b-binding protein

Autor: SJ Koppelman, C van't Veer, JJ Sixma, BN Bouma

Publikováno v: Blood. 86(7)

The complement protein C4b-binding protein plays an important role in the regulation of the protein C anticoagulant pathway. C4b-binding protein can bind to protein S, thereby inhibiting the cofactor activity of protein S for activated protein C. In

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15f1b6053e7907acf8a641e870922403
https://pubmed.ncbi.nlm.nih.gov/7670108

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Increased prothrombin activation in protein S-deficient plasma under flow conditions on endothelial cell matrix: an independent anticoagulant function of protein S in plasma

Autor: van't Veer C, Tilman Hackeng, Biesbroeck D, Jj, Sixma, Bn, Bouma

Publikováno v: Europe PubMed Central

Protein S is a vitamin K-dependent nonenzymatic coagulation factor involved in the regulation of activated protein C (aPC). In this study, we report an aPC-independent anticoagulant function of protein S in plasma under flow conditions. Plasma, antic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::65f2aacd4cc6213c89e4bab6eafa5a50
https://pubmed.ncbi.nlm.nih.gov/7703488

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Construction and characterization of thrombin-resistant variants of recombinant human protein S

Autor: Gt, Chang, Aaldering L, Tilman Hackeng, Ph, Reitsma, Rm, Bertina, Bn, Bouma

Publikováno v: Europe PubMed Central

Protein S is a vitamin K-dependent plasma protein that functions as a cofactor of activated protein C (APC) in the inactivation of coagulation factors Va and VIIIa. Protein S, migrates as a doublet on reduced SDS polyacrylamide gel electrophoresis. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f7f70b7a66fd725373989fb6d38cedcf
https://pubmed.ncbi.nlm.nih.gov/7900076

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The localization of heparin-binding fragments on human C4b-binding protein

Autor: Hessing M, Ra, Vlooswijk, Tilman Hackeng, Kanters D, Bn, Bouma

Publikováno v: Europe PubMed Central

C4b-binding protein (C4BP) is a multimeric plasma protein, which regulates the classical pathway of the C system. C4BP interacts with C C4b on a domain located in a 48-kDa chymotryptic fragment. We now demonstrate that C4BP contains heparin-binding f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::43ad498b537cbdd28e6b133516377c03
https://pubmed.ncbi.nlm.nih.gov/2136880

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Elimination of Intravenously Administered Radiolabelled Antithrombin III and Heparin in Humans

Autor: E Holmer, B Nijmeyer, LO Andersson, JJ Sixma, BN Bouma, de Swart Ca

Publikováno v: Thrombosis and Haemostasis. 52:066-070

SummaryAntithrombin III was purified from normal plasma by DEAE- Sephadex chromatography and heparin affinity chromatography; the protein was subsequently radiolabelled with 125I. 125I-anti- thrombin III alone and 125I-antithrombin III in the presenc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1bf763c3570529d4beb4ac7244709e30
https://doi.org/10.1055/s-0038-1661139

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Elimination of high affinity heparin fractions and their anticoagulant and lipase activity

Autor: B Nijmeyer, JJ Sixma, CA de Swart, E Holmer, LO Andersson, L Verschoor, BN Bouma

Publikováno v: Blood. 63:836-842

High and low affinity heparin (HA and LA heparin) were prepared from commercial heparin by affinity chromatography to insolubilized antithrombin III. HA heparin was radiolabeled with 35S and subdivided by gel chromatography into high molecular weight

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ffb35b89d458a8717e68a738e2391f9
https://doi.org/10.1182/blood.v63.4.836.bloodjournal634836

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Immunologic studies on human factor VIII (anti-hemophilic factor A, AHF) components produced by low-ionic-strength dialysis

Autor: JJ Sixma, J. A. Van Mourik, BN Bouma, JM Hordijk-Hos, S. de Graaf

Publikováno v: Blood. 47:253-264

Since dialysis of human factor VIII against buffers of low ionic strength yielded two distinct components, and since the factor VIII fraction isolated from normal plasma showed von Willebrand factor activity as defined by the corrective effect on abn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::483718c9583b152a82f05f91192e1640
https://doi.org/10.1182/blood.v47.2.253.253

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Identification of monoclonal antibodies that inhibit the function of protein C inhibitor. Evidence for heparin-independent inhibition of activated protein C in plasma

Autor: JC Meijers, RA Vlooswijk, DH Kanters, M Hessing, BN Bouma

Publikováno v: Blood. 72(4)

Monoclonal antibodies specific for protein C inhibitor (PCI) partially blocked the inactivation of activated protein C (APC) in plasma, whereas in a purified system, the PCI activity could be completely blocked. The inactivation of APC in normal and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bccf2c0f45011cd2a5b602bf987159f
https://pubmed.ncbi.nlm.nih.gov/2844328

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