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7. Blood Coagulation and Beyond: Position Paper from the Fourth Maastricht Consensus Conference on Thrombosis

Author

Akbulut, Asim Cengiz, additional, Arisz, Ryanne A., additional, Baaten, Constance C. F. M. J., additional, Baidildinova, Gaukhar, additional, Barakzie, Aarazo, additional, Bauersachs, Rupert, additional, ten Berg, Jur, additional, van den Broek, Wout W. A., additional, de Boer, H. C., additional, Bonifay, Amandine, additional, Bröker, Vanessa, additional, Buka, Richard J., additional, ten Cate, Hugo, additional, ten Cate-Hoek, Arina J., additional, Cointe, S., additional, De Luca, Ciro, additional, De Simone, Ilaria, additional, Diaz, Rocio Vacik, additional, Dignat-George, Françoise, additional, Freson, Kathleen, additional, Gazzaniga, Giulia, additional, van Gorp, Eric C. M., additional, Habibi, Anxhela, additional, Henskens, Yvonne M. C., additional, Iding, Aaron F. J., additional, Khan, Abdullah, additional, Koenderink, Gijsje H., additional, Konkoth, Akhil, additional, Lacroix, Romaric, additional, Lahiri, Trisha, additional, Lam, Wilbur, additional, Lamerton, Rachel E., additional, Lorusso, Roberto, additional, Luo, Qi, additional, Maas, Coen, additional, McCarty, Owen J. T., additional, van der Meijden, Paola E. J., additional, Meijers, Joost C. M., additional, Mohapatra, Adarsh K., additional, Nevo, Neta, additional, Robles, Alejandro Pallares, additional, Poncelet, Philippe, additional, Reinhardt, Christoph, additional, Ruf, Wolfram, additional, Saraswat, Ronald, additional, Schönichen, Claudia, additional, Schutgens, Roger, additional, Simioni, Paolo, additional, Spada, Stefano, additional, Spronk, Henri M. H., additional, Tazhibayeva, Karlygash, additional, Thachil, Jecko, additional, Vallier, L., additional, Veninga, Alicia, additional, Verhamme, Peter, additional, Visser, Chantal, additional, Watson, Steve P., additional, Wenzel, Philip, additional, Willems, Ruth A. L., additional, Willers, Anne, additional, Zhang, Pengyu, additional, Zifkos, Konstantinos, additional, and van Zonneveld, Anton Jan, additional

Published
2023
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9. Structures of factor XI and prekallikrein bound to domain 6 of high–molecular weight kininogen reveal alternate domain 6 conformations and exosites

Author

Li, Chan, Barroeta, Awital Bar, Wong, Szu Shen, Kim, Hyo Jung, Pathak, Monika, Dreveny, Ingrid, Meijers, Joost C. M., Emsley, Jonas, Experimental Vascular Medicine, Vascular Medicine, ACS - Pulmonary hypertension & thrombosis, and ACS - Amsterdam Cardiovascular Sciences

Subjects
factor IX, factor XII, kininogens, prekallikrein, Hematology, factor XI
Abstract

Background: High–molecular weight kininogen (HK) circulates in plasma as a complex with zymogen prekallikrein (PK). HK is both a substrate and a cofactor for activated plasma kallikrein, and the principal exosite interactions occur between PK N-terminal apple domains and the C-terminal D6 domain of HK. Objectives: To determine the structure of the complex formed between PK apple domains and an HKD6 fragment and compare this with the coagulation factor XI (FXI)-HK complex. Methods: We produced recombinant FXI and PK heavy chains (HCs) spanning all 4 apple domains. We cocrystallized PKHC (and subsequently FXIHC) with a 31-amino acid synthetic peptide spanning HK residues Ser565-Lys595 and determined the crystal structure. We also analyzed the full-length FXI-HK complex in solution using hydrogen deuterium exchange mass spectrometry. Results: The 2.3Å PKHC-HK peptide crystal structure revealed that the HKD6 sequence WIPDIQ (Trp569-Gln574) binds to the apple 1 domain and HK FNPISDFPDT (Phe582-Thr591) binds to the apple 2 domain with a flexible intervening sequence resulting in a bent double conformation. A second 3.2Å FXIHC-HK peptide crystal structure revealed a similar interaction with the apple 2 domain but an alternate, straightened conformation of the HK peptide where residues LSFN (Leu579-Asn583) interacts with a unique pocket formed between the apple 2 and 3 domains. HDX-MS of full length FXI-HK complex in solution confirmed interactions with both apple 2 and apple 3. Conclusions: The alternate conformations and exosite binding of the HKD6 peptide likely reflects the diverging relationship of HK to the functions of PK and FXI.

Published
2023

13. Correction to:Coagulation in gout: is there a link with disease activity? (Clinical Rheumatology, (2022), 41, 6, (1809-1815), 10.1007/s10067-022-06047-9)

Author

Vedder, Daisy, Gerritsen, Martijn, Meijers, Joost C. M., Nurmohamed, Michael T., Elderly care medicine, Rheumatology, ACS - Atherosclerosis & ischemic syndromes, AII - Inflammatory diseases, Experimental Vascular Medicine, Vascular Medicine, and ACS - Pulmonary hypertension & thrombosis

Abstract

In the original version of the above article, The figures and legends used were incorrect. The correct figures are presented as follows (Figs.1, 2, 3, and 4): The original article has been corrected.

Published
2022

16. Nanobodies against factor XI apple 3 domain inhibit binding of factor IX and reveal a novel binding site for high molecular weight kininogen

Author

Poli Van Creveldkliniek Medisch, Circulatory Health, Bar Barroeta, Awital, Marquart, J Arnoud, Bakhtiari, Kamran, Meijer, Alexander B, Urbanus, Rolf T, Meijers, Joost C M, Poli Van Creveldkliniek Medisch, Circulatory Health, Bar Barroeta, Awital, Marquart, J Arnoud, Bakhtiari, Kamran, Meijer, Alexander B, Urbanus, Rolf T, and Meijers, Joost C M

Published
2022

17. VhH anti-thrombomodulin clone 1 inhibits TAFI activation and enhances fibrinolysis in human whole blood under flow

Author

CDL Nanomedicine, Poli Van Creveldkliniek Medisch, Centraal Diagnostisch Laboratorium, CDL Contact activatie, Circulatory Health, CDL Research analisten, Cancer, CDL Cluster Onderzoek en Onderwijs, van Moorsel, Marc V A, Poolen, Geke, Koekman, Cornelis A, Verhoef, Sandra, de Maat, Steven, Barendrecht, Arjan, van Kleef, Nadine D, Meijers, Joost C M, Schiffelers, Raymond, Maas, Coen, Urbanus, Rolf T, CDL Nanomedicine, Poli Van Creveldkliniek Medisch, Centraal Diagnostisch Laboratorium, CDL Contact activatie, Circulatory Health, CDL Research analisten, Cancer, CDL Cluster Onderzoek en Onderwijs, van Moorsel, Marc V A, Poolen, Geke, Koekman, Cornelis A, Verhoef, Sandra, de Maat, Steven, Barendrecht, Arjan, van Kleef, Nadine D, Meijers, Joost C M, Schiffelers, Raymond, Maas, Coen, and Urbanus, Rolf T

Published
2022

29. Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein

Author

Renné, Thomas, Gailani, David, Meijers, Joost C. M., Müller-Esterl, Werner, Renné, Thomas, Gailani, David, Meijers, Joost C. M., and Müller-Esterl, Werner

Abstract

Factor XI (FXI), the zymogen of the blood coagulation protease FXIa, and the structurally homologous protein plasma prekallikrein circulate in plasma in noncovalent complexes with H-kininogen (HK). HK binds to the heavy chains of FXI and of prekallikrein. Each chain contains four apple domains (F1-F4 for FXI and P1-P4 for prekallikrein). Previous studies indicated that the HK-binding site on FXI is located in F1, whereas the major HK-binding site on prekallikrein is in P2. To determine the contribution of each FXI apple domain to HK-FXI complex formation, we examined binding of recombinant single apple domain-tissue plasminogen activator fusion proteins to HK. The order of affinity from highest to lowest is F2 F4 > F1 F3. Monoclonal antibodies against F2 are superior to F4 or F1 antibodies as inhibitors of HK binding to FXI. Antibody alphaP2, raised against prekallikrein, cross-reacts with FXI F2 and inhibits FXI-HK binding with an IC(50) of 8 nm. HK binding to a platelet-specific FXI variant lacking the N-terminal half of F2 is reduced > 5-fold compared with full-length FXI. A chimeric FXI molecule in which F2 is replaced by P2 is cleaved within P2 during activation by factor XIIa, resulting in greatly reduced HK binding capacity. In contrast, wild-type FXI is not cleaved within F2, and its binding capacity for HK is unaffected by factor XIIa. Our data show that HK binding to FXI involves multiple apple domains, with F2 being most important. The findings demonstrate a similarity in mechanism for FXI and prekallikrein binding to HK.

Published
2021

34. Nanobodies against factor XI apple 3 domain inhibit binding of factor IX and reveal a novel binding site for high molecular weight kininogen

Author

Bar Barroeta, Awital, Marquart, J. Arnoud, Bakhtiari, Kamran, Meijer, Alexander B., Urbanus, Rolf T., and Meijers, Joost C. M.

Abstract

Factor XI (FXI) is a promising target for novel anticoagulants because it shows a strong relation to thromboembolic diseases, while fulfilling a mostly supportive role in hemostasis. Anticoagulants targeting FXI could therefore reduce the risk for thrombosis, without increasing the chance of bleeding side effects. To generate nanobodies that can interfere with FXIa mediated activation of factor IX (FIX). Nanobodies were selected for binding to the apple 3 domain of FXI and their effects on FXI and coagulation were measured in purified protein systems as well as in plasma‐based coagulation assays. Additionally, the binding epitope of selected nanobodies was assessed by hydrogen–deuterium exchange mass spectrometry. We have identified five nanobodies that inhibit FIX activation by FXI by competing with the FIX binding site on FXI. Interestingly, a sixth nanobody was found to target a different binding epitope in the apple 3 domain, resulting in competition with the FXI–high molecular weight kininogen (HK) interaction. We have characterized a nanobody targeting the FXI apple 3 domain that elucidates the binding orientation of HK on FXI. Moreover, we have produced five nanobodies that can inhibit the FXI–FIX interaction.

Published
2022
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35. Complement C5 Contributes to Brain Injury After Subarachnoid Hemorrhage

Author

van Dijk, Bart J, Meijers, Joost C M, Kloek, Anne T, Knaup, Veronique L, Rinkel, Gabriel J E, Morgan, B Paul, van der Kamp, Marije J, Osuka, Koji, Aronica, Eleonora, Ruigrok, Ynte M, van de Beek, Diederik, Brouwer, Matthijs, Pekna, Marcela, Hol, Elly M, Vergouwen, Mervyn D I, van Dijk, Bart J, Meijers, Joost C M, Kloek, Anne T, Knaup, Veronique L, Rinkel, Gabriel J E, Morgan, B Paul, van der Kamp, Marije J, Osuka, Koji, Aronica, Eleonora, Ruigrok, Ynte M, van de Beek, Diederik, Brouwer, Matthijs, Pekna, Marcela, Hol, Elly M, and Vergouwen, Mervyn D I

Abstract

Previous studies showed that complement activation is associated with poor functional outcome after aneurysmal subarachnoid hemorrhage (SAH). We investigated whether complement activation is underlying brain injury after aneurysmal SAH (n = 7) and if it is an appropriate treatment target. We investigated complement expression in brain tissue of aneurysmal SAH patients (n = 930) and studied the role of common genetic variants in C3 and C5 genes in outcome. We analyzed plasma levels (n = 229) to identify the functionality of a single nucleotide polymorphism (SNP) associated with outcome. The time course of C5a levels was measured in plasma (n = 31) and CSF (n = 10). In an SAH mouse model, we studied the extent of microglia activation and cell death in wild-type mice, mice lacking the C5a receptor, and in mice treated with C5-specific antibodies (n = 15 per group). Brain sections from aneurysmal SAH patients showed increased presence of complement components C1q and C3/C3b/iC3B compared to controls. The complement component 5 (C5) SNP correlated with C5a plasma levels and poor disease outcome. Serial measurements in CSF revealed that C5a was > 1400-fold increased 1 day after aneurysmal SAH and then gradually decreased. C5a in plasma was 2-fold increased at days 3-10 after aneurysmal SAH. In the SAH mouse model, we observed a ≈ 40% reduction in both microglia activation and cell death in mice lacking the C5a receptor, and in mice treated with C5-specific antibodies. These data show that C5 contributes to brain injury after experimental SAH, and support further study of C5-specific antibodies as novel treatment option to reduce brain injury and improve prognosis after aneurysmal SAH.

Published
2020

36. Complement C5 Contributes to Brain Injury After Subarachnoid Hemorrhage

Author

TN groep Hol, Brain, Neurologie, Circulatory Health, Pathologie, ZL Cerebrovasculaire Ziekten Medisch, Cancer, van Dijk, Bart J, Meijers, Joost C M, Kloek, Anne T, Knaup, Veronique L, Rinkel, Gabriel J E, Morgan, B Paul, van der Kamp, Marije J, Osuka, Koji, Aronica, Eleonora, Ruigrok, Ynte M, van de Beek, Diederik, Brouwer, Matthijs, Pekna, Marcela, Hol, Elly M, Vergouwen, Mervyn D I, TN groep Hol, Brain, Neurologie, Circulatory Health, Pathologie, ZL Cerebrovasculaire Ziekten Medisch, Cancer, van Dijk, Bart J, Meijers, Joost C M, Kloek, Anne T, Knaup, Veronique L, Rinkel, Gabriel J E, Morgan, B Paul, van der Kamp, Marije J, Osuka, Koji, Aronica, Eleonora, Ruigrok, Ynte M, van de Beek, Diederik, Brouwer, Matthijs, Pekna, Marcela, Hol, Elly M, and Vergouwen, Mervyn D I

Published
2020

37. Hydrogen-deuterium exchange mass spectrometry highlights conformational changes induced by factor XI activation and binding of factor IX to factor XIa

Author

Bar Barroeta, Awital, van Galen, Josse, Stroo, Ingrid, Marquart, J Arnoud, Meijer, Alexander B, Meijers, Joost C M, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Graduate School, Vascular Medicine, ACS - Pulmonary hypertension & thrombosis, Afd Biomol.Mass Spect. and Proteomics, and Biomolecular Mass Spectrometry and Proteomics

Subjects
Models, Molecular, Hydrogen Deuterium Exchange-Mass Spectrometry, 030204 cardiovascular system & hematology, Mass spectrometry, Article, 03 medical and health sciences, Structure-Activity Relationship, 0302 clinical medicine, Zymogen, medicine, Humans, Protein Interaction Domains and Motifs, Binding site, factor XIa, Factor IX, mass spectrometry, factor IX, Chemistry, Prekallikrein, Hematology, Protein superfamily, factor XI, Enzyme Activation, HEK293 Cells, Coagulation, Biophysics, hemostasis, bacteria, Hydrogen–deuterium exchange, medicine.drug, Protein Binding
Abstract

Background Factor XI (FXI) is a zymogen in the coagulation pathway that, once activated, promotes haemostasis by activating factor IX (FIX). Substitution studies using apple domains of the homologous protein prekallikrein have identified that FIX binds to the apple 3 domain of FXI. However, the molecular changes upon activation of FXI or binding of FIX to FXIa have remained largely unresolved. Objectives This study aimed to gain more insight in the FXI activation mechanism by identifying the molecular differences between FXI and FXIa, and in the conformational changes in FXIa induced by binding of FIX. Methods Hydrogen-deuterium exchange mass spectrometry was performed on FXI, FXIa, and FXIa in complex with FIX. Results Both activation and binding to FIX induced conformational changes at the interface between the catalytic domain and the apple domains of FXI(a)-more specifically at the loops connecting the apple domains. Moreover, introduction of FIX uniquely induced a reduction of deuterium uptake in the beginning of the apple 3 domain. Conclusions We propose that the conformational changes of the catalytic domain upon activation increase the accessibility to the apple 3 domain to enable FIX binding. Moreover, our HDX MS results support the location of the proposed FIX binding site at the beginning of the apple 3 domain and suggest a mediating role in FIX binding for both loops adjacent to the apple 3 domain.

Published
2019

44. Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor

Author

Marx, Pauline F., Dawson, Philip, Bouma, Bonno N., and Meijers, Joost C. M.

Subjects
Biochemistry -- Research, Thrombin -- Physiological aspects, Fibrinolysis -- Physiological aspects, Chemical inhibitors -- Physiological aspects, Plasmin -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the thrombin-activatable fibrinolysis inhibitor. The effect of plasmin on the activity regulation of this inhibitor has been investigated and the details are discussed.

Published
2002

47. MiR-223-3p and miR-122-5p as circulating biomarkers for plaque instability

Author

Singh, Sandeep, primary, de Ronde, Maurice W J, additional, Kok, Maayke G M, additional, Beijk, Marcel AM, additional, De Winter, Robbert J, additional, van der Wal, Allard C, additional, Sondermeijer, Brigitte M, additional, Meijers, Joost C M, additional, Creemers, Esther E, additional, and Pinto-Sietsma, Sara-Joan, additional

Published
2020
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48. C4b-binding protein protects coagulation factor Va from inactivation by activated protein C

Author

Poel, Robbert H. L. van de, Meijers, Joost C. M., Rosing, Jan, Tans, Guido, and Bouma, Bonno N.

Subjects
Biochemistry -- Research, Carrier proteins -- Research, Coagulation -- Analysis, Protein C -- Research, Biological sciences, Chemistry
Abstract

Research has been conducted on the activated protein C-mediated inactivation of factor Va. The effect of the C4b-binding protein on this factor in the absence and presence of protein S has been investigated.

Published
2000

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