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https://www.readbyqxmd.com/read/29757137/reversal-of-apixaban-induced-alterations-in-haemostasis-by-different-coagulation-factor-concentrates-in-patients-after-hip-or-knee-replacement-surgery
#1
Katrin Schmidt, Kerstin Krüger, Elisabeth Langer, Martin Schmutzler, Elke Johnen, Klaus D Wernecke, Christian Von Heymann, Mareike K Körber
BACKGROUND: Apixaban is a direct oral anticoagulant (DOAC) with a specific inhibition of activated factor X (FXa). In case of bleeding or need of urgent surgery a direct antidote is not yet available. Off-label application of non-specific haemostatic agents, such as prothrombin complex concentrate (PCC) and recombinant FVIIa (rFVIIa), has been reported to reverse the effects of apixaban in in vitro and animal studies. The aim of this study is to measure the reversal potential of PCC and rFVIIa in patients with prophylactic apixaban concentrations...
May 11, 2018: Blood Transfusion, Trasfusione del Sangue
https://www.readbyqxmd.com/read/29734527/evolutionary-conservation-of-the-allosteric-activation-of-factor-viia-by-tissue-factor-in-lamprey-reply
#2
D L Beeler, W C Aird, M A Grant
We have read with interest the letter by Olsen and colleagues in response to our recent article [1]. Therein, we reported the cloning of full-length tissue factor (Tf) and factor VIIa (FVIIa) cDNAs from lamprey Petromyzon marinus, and characterization of structural features in the proteins. Using constructed models of lamprey (Pm) tissue factor soluble extracellular-domain (sTF) and factor VIIa (sTF/FVIIa) complex, we assessed the conservation of allosteric TF-mediated stabilization of the FVIIa heavy chain (FVIIa-hc)...
May 7, 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29733494/evolutionary-conservation-of-the-allosteric-activation-of-factor-viia-by-tissue-factor-in-lamprey-comment
#3
J J Madsen, E Persson, O H Olsen
We read with great interest the article on allostery in a protease from the blood coagulation cascade by Beeler et al.(1) in a recent issue of Journal of Thrombosis and Haemostasis. Herein, the authors conclude that the allosteric activation of coagulation factor VIIa (FVIIa) by tissue factor (TF) in lamprey (l-) appears indistinguishable from, and conserved compared to, that in human (h-); meaning that l-FVIIa is assumed to be catalytically incompetent unless allosterically activated by l-TF. The lamprey, an ancient jawless eel-like vertebrate, is a fascinating creature and studying its coagulation system can certainly lead to insights into molecular mechanisms of coagulation as well as evolutionary adaptations over hundreds of millions of years (reviewed in (2))...
May 7, 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29669778/factor-viia-induces-anti-inflammatory-signaling-via-epcr-and-par1
#4
Vijay Kondreddy, Jue Wang, Shiva Keshava, Charles T Esmon, L Vijaya Mohan Rao, Usha R Pendurthi
Recent studies show that endothelial cell protein C receptor (EPCR) interacts with diverse ligands, in addition to its known ligands protein C and activated protein C (APC). We showed in earlier studies that procoagulant clotting factor VIIa (FVIIa) binds EPCR and down-regulates EPCR-mediated anticoagulation and induces endothelial barrier protective effect. Here, we investigated the effect of FVIIa interaction with EPCR on endothelial cell inflammation and LPS-induced inflammatory responses in vivo. Treatment of endothelial cells with FVIIa suppressed TNFα- and LPS-induced expression of cellular adhesion molecules and adherence of monocytes to endothelial cells...
April 18, 2018: Blood
https://www.readbyqxmd.com/read/29645406/modified-clot-waveform-analysis-to-measure-plasma-coagulation-potential-in-the-presence-of-the-anti-factor-ixa-factor-x-bispecific-antibody-emicizumab
#5
Keiji Nogami, Tomoko Matsumoto, Yuka Tabuchi, Tetsuhiro Soeda, Nobuo Arai, Takehisa Kitazawa, Midori Shima
BACKGROUND: Emicizumab is an anti-factor (F)IXa/FX bispecific antibody that mimics FVIIIa cofactor function. Emicizumab does not require activation by thrombin and its effect on shortening activated partial prothrombin time (aPTT) is much greater relative to FVIII. The aPTT has limited utility, therefore, in hemophilia A patients (HA-pts) treated with emicizumab. AIM: To evaluate the global coagulation potential of emicizumab. METHODS: Clot waveform analysis (CWA) with prothrombin time (PT)/aPTT-mixed reagents was used to define hemostatic monitoring protocols in HA-pts...
April 12, 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29621998/a-factor-xia-activatable-hirudin-albumin-fusion-protein-reduces-thrombosis-in-mice-without-promoting-blood-loss
#6
William P Sheffield, Louise J Eltringham-Smith, Varsha Bhakta
BACKGROUND: Hirudin is a potent thrombin inhibitor but its antithrombotic properties are offset by bleeding side-effects. Because hirudin's N-terminus must engage thrombin's active site for effective inhibition, fusing a cleavable peptide at this site may improve hirudin's risk/benefit ratio as a therapeutic agent. Previously we engineered a plasmin cleavage site (C) between human serum albumin (HSA) and hirudin variant 3 (HV3) in fusion protein HSACHV3. Because coagulation factor XI (FXI) is more involved in thrombosis than hemostasis, we hypothesized that making HV3 activity FXIa-dependent would also improve HV3's potential therapeutic profile...
April 5, 2018: BMC Biotechnology
https://www.readbyqxmd.com/read/29611182/factor-f-viii-viia-enhances-global-haemostatic-function-in-the-co-presence-of-bypassing-agents-and-fviii-among-patients-with-haemophilia-a-with-inhibitor
#7
Keiji Nogami, Tomoko Matsumoto, Koji Yada, Kenichi Ogiwara, Shoko Furukawa, Yasuaki Shida, Masahiro Takeyama, Midori Shima
Bypassing therapy is essential for the haemostatic management of patients with haemophilia A with inhibitor (PWHA-inh), but the therapeutic effects are inconsistent. We previously reported that activated prothrombin complex concentrates (aPCC) activated factor (F)VIIIin vitro, and was mediated mainly by the activated FVII (FVIIa) contained in aPCC. We have extended those studies to assess global coagulation in whole blood from 18 PWHA-inh in the co-presence of aPCC and FVIII using Ca2+ -triggered rotational thromboelastometry...
April 2, 2018: British Journal of Haematology
https://www.readbyqxmd.com/read/29563336/enzymatically-oxidized-phospholipids-restore-thrombin-generation-in-coagulation-factor-deficiencies
#8
David A Slatter, Charles L Percy, Keith Allen-Redpath, Joshua M Gajsiewicz, Nick J Brooks, Aled Clayton, Victoria J Tyrrell, Marcela Rosas, Sarah N Lauder, Andrew Watson, Maria Dul, Yoel Garcia-Diaz, Maceler Aldrovandi, Meike Heurich, Judith Hall, James H Morrissey, Sebastien Lacroix-Desmazes, Sandrine Delignat, P Vincent Jenkins, Peter W Collins, Valerie B O'Donnell
Hemostatic defects are treated using coagulation factors; however, clot formation also requires a procoagulant phospholipid (PL) surface. Here, we show that innate immune cell-derived enzymatically oxidized phospholipids (eoxPL) termed hydroxyeicosatetraenoic acid-phospholipids (HETE-PLs) restore hemostasis in human and murine conditions of pathological bleeding. HETE-PLs abolished blood loss in murine hemophilia A and enhanced coagulation in factor VIII- (FVIII-), FIX-, and FX-deficient human plasma . HETE-PLs were decreased in platelets from patients after cardiopulmonary bypass (CPB)...
March 22, 2018: JCI Insight
https://www.readbyqxmd.com/read/29537116/in-vitro-characterization-of-mod-5014-a-novel-long-acting-carboxy-terminal-peptide-ctp-modified-activated-fvii
#9
A Bar-Ilan, T Livnat, M Hoffmann, L Binder, M Zakar, R Guy, Y Felikman, L Moschcovich, B Shenkman, D Monroe, O Hershkovitz, G Kenet, G Hart
INTRODUCTION: Recombinant FVIIa (rFVIIa) is an effective treatment for haemophilia through frequent administration. However, the short half-life of rFVIIa decreases its prophylactic ability to reduce bleeding. Carboxy-terminal peptide (CTP)-modified FVIIa (MOD-5014) is a long-acting rFVIIa developed for on-demand treatment of haemophilia using either an intravenous or subcutaneous injection with the aim of less frequent administrations, as well as for prophylactic use. AIM: The comprehensive evaluation of the activity MOD-5014 vs commercially available rhFVIIa, as well as their interaction with cofactors and inhibitors...
March 14, 2018: Haemophilia: the Official Journal of the World Federation of Hemophilia
https://www.readbyqxmd.com/read/29532595/factor-xa-and-viia-inhibition-by-tissue-factor-pathway-inhibitor-is-prevented-by-a-monoclonal-antibody-to-its-kunitz-1-domain
#10
Cecilia Augustsson, Anders Svensson, Birgitte Kjaer, Tzu-Yuan Chao, Xia Wenjuan, Berit Olsen Krogh, Jens Breinholt, Jes Thorn Clausen, Ida Hilden, Helle Heibroch Petersen, Lars Christian Petersen
BACKGROUND: Initiation of coagulation is induced by binding of activated factor VII (FVIIa) to tissue factor (TF) and activation of factor X (FX) in a process regulated by tissue factor pathway inhibitor (TFPI). TFPI contains three Kunitz-type protease inhibitor domains (K1-K3) of which K1 and K2 block the active sites of FVIIa and FXa respectively. OBJECTIVE: To produce a monoclonal antibody (mAb) directed towards K1, to characterize the binding epitope, and to study its effect on TFPI inhibition...
March 12, 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29437578/tissue-factor-an-essential-mediator-of-hemostasis-and-trigger-of-thrombosis
#11
REVIEW
Steven P Grover, Nigel Mackman
Tissue factor (TF) is the high-affinity receptor and cofactor for factor (F)VII/VIIa. The TF-FVIIa complex is the primary initiator of blood coagulation and plays an essential role in hemostasis. TF is expressed on perivascular cells and epithelial cells at organ and body surfaces where it forms a hemostatic barrier. TF also provides additional hemostatic protection to vital organs, such as the brain, lung, and heart. Under pathological conditions, TF can trigger both arterial and venous thrombosis. For instance, atherosclerotic plaques contain high levels of TF on macrophage foam cells and microvesicles that drives thrombus formation after plaque rupture...
April 2018: Arteriosclerosis, Thrombosis, and Vascular Biology
https://www.readbyqxmd.com/read/29418058/evolutionary-conservation-of-the-allosteric-activation-of-factor-viia-by-tissue-factor-in-lamprey
#12
D L Beeler, W C Aird, M A Grant
Essentials Tissue factor (TF) enhances factor VIIa (FVIIa) activity through structural and dynamic changes. We analyzed conservation of TF-activated FVIIa allosteric networks in extant vertebrate lamprey. Lamprey Tf/FVIIa molecular dynamics show conserved Tf-induced structural/dynamic FVIIa changes. Lamprey Tf activation of FVIIa allosteric networks follows molecular pathways similar to human. SUMMARY: Background Previous studies have provided insight into the molecular basis of human tissue factor (TF) activation of activated factor VII (FVIIa)...
April 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29351237/bioengineering-of-rfviia-biopharmaceutical-and-structure-characterization-for-biosimilarity-assessment
#13
Othman Montacir, Houda Montacir, Murat Eravci, Andreas Springer, Stephan Hinderlich, Fereidoun Mahboudi, Amirhossein Saadati, Maria Kristina Parr
Eptacog alfa (NovoSeven® ) is a vitamin K-dependent recombinant Factor VIIa produced by genetic engineering from baby hamster kidney (BHK) cells as a single peptide chain of 406 residues. After activation, it consists of a light chain (LC) of 152 amino and a heavy chain (HC) of 254 amino acids. Recombinant FVIIa undergoes many post-translational modifications (PTMs). The first ten glutamic acids of the N-terminal moiety are γ-carboxylated, Asn145 and Asn322 are N-glycosylated, and Ser52 and Ser60 are O-glycosylated...
January 19, 2018: Bioengineering
https://www.readbyqxmd.com/read/29304529/passivating-injured-endothelium-with-kinexins-in-thrombolytic-therapy
#14
Yunn-Hwa Ma, Chao-Wei Huang, Chih-Jen Wen, Yi-Ching Lu, Shiaw-Pyng Wey, Tze-Chein Wun
Without conjunctive administration of an anticoagulant, endothelial injury-induced thrombosis is resistant to thrombolysis and prone to re-thrombosis. We hypothesized that co-delivery of recombinant tissue plasminogen activator (rtPA) with annexin V-containing anticoagulants that specifically target the injured endothelium may passivate the thrombogenic elements of the vascular injury site and enhance rtPA-induced thrombolysis. In this study, the effects of conjunctive administration of Kinexins (Kunitz inhibitor-annexin V fusion proteins) with rtPA on thrombolysis were determined in vitro and in vivo ...
January 2018: Thrombosis and Haemostasis
https://www.readbyqxmd.com/read/29246902/identification-of-the-integrin-binding-site-on-coagulation-factor-viia-required-for-proangiogenic-par2-signaling
#15
Andrea S Rothmeier, Enbo Liu, Sagarika Chakrabarty, Jennifer Disse, Barbara M Mueller, Henrik Østergaard, Wolfram Ruf
The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1...
February 8, 2018: Blood
https://www.readbyqxmd.com/read/29204261/recombinant-human-factor-viia-rfviia-in-hemophilia-mode-of-action-and-evidence-to-date
#16
REVIEW
Muriel Giansily-Blaizot, Jean-François Schved
Recombinant activated factor VII (rFVIIa) is a bypassing agent widely used both in the treatment and prevention of hemorrhagic complications due to hemophilia with inhibitor. In such cases, antihemophilic factors cannot be used. The normal physiology of factor VII/ factor VIIa (FVII/FVIIa) in the hemostatic process requires the presence of tissue factor (TF) that links to FVII leading to a FVIIa-TF complex which activates both factor X and factor IX. The therapeutic use of rFVIIa requires high amount of FVIIa...
December 2017: Therapeutic Advances in Hematology
https://www.readbyqxmd.com/read/29126301/coagulation-testing-in-the-core-laboratory
#17
REVIEW
William E Winter, Sherri D Flax, Neil S Harris
Primary hemostasis begins with endothelial injury. VWF, produced by endothelial cells, binds to platelets and links them to subendothelial collagen. Platelet-derived ADP and thromboxane activate non-adhered platelets via their GPIIb/IIIa receptors, allowing these platelets to participate in platelet aggregation. Secondary hemostasis is initiated with the binding of factor VII to extravascular tissue factor (TF). Factors II, VII, IX and X are vitamin K-dependent factors. The role of vitamin K is to assist in the addition of gamma carboxylate groups to glutamic acids in the "GLA" domains of these factors...
November 8, 2017: Laboratory Medicine
https://www.readbyqxmd.com/read/29112333/associations-of-activated-coagulation-factor-vii-and-factor-viia-antithrombin-levels-with-genome-wide-polymorphisms-and-cardiovascular-disease-risk
#18
N C Olson, L M Raffield, L A Lange, E M Lange, W T Longstreth, G Chauhan, S Debette, S Seshadri, A P Reiner, R P Tracy
ESSENTIALS: Essentials A fraction of coagulation factor VII circulates in blood as an activated protease (FVIIa). We evaluated FVIIa and FVIIa-antithrombin (FVIIa-AT) levels in the Cardiovascular Health Study. Polymorphisms in the F7 and PROCR loci were associated with FVIIa and FVIIa-AT levels. FVIIa may be an ischemic stroke risk factor in older adults and FVIIa-AT may assess mortality risk. SUMMARY: Background A fraction of coagulation factor (F) VII circulates as an active protease (FVIIa)...
January 2018: Journal of Thrombosis and Haemostasis: JTH
https://www.readbyqxmd.com/read/29111325/inhibition-of-tissue-factor-signaling-in-breast-tumour-xenografts-induces-widespread-changes-in-the-microrna-expression-profile
#19
Esterina D'Asti, G Mark Anderson, Janusz Rak
Tissue factor (TF) is a transmembrane receptor for coagulation factor VII/VIIa and is frequently overexpressed by cancer cells. The TF/VIIa complex acts as the main initiator of the clotting cascade in blood and a trigger of intracellular signaling that changes gene expression and the cellular phenotype. However, pathways mediating these changes are still poorly characterized and especially the impact of TF signals on regulatory microRNA (miR) networks in cancer remains unknown. We show that the monoclonal antibody that selectively neutralises the signaling (but not coagulant) function of human TF (CNTO 2559) inhibits progression of MDA-MB-231 breast cancer xenografts in mice and prolongs animal survival...
December 16, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29109275/engineering-of-a-membrane-triggered-activity-switch-in-coagulation-factor-viia
#20
Anders L Nielsen, Anders B Sorensen, Heidi L Holmberg, Prafull S Gandhi, Johan Karlsson, Jens Buchardt, Kasper Lamberth, Mads Kjelgaard-Hansen, Carsten Dan Ley, Brit B Sørensen, Wolfram Ruf, Ole H Olsen, Henrik Østergaard
Recombinant factor VIIa (FVIIa) variants with increased activity offer the promise to improve the treatment of bleeding episodes in patients with inhibitor-complicated hemophilia. Here, an approach was adopted to enhance the activity of FVIIa by selectively optimizing substrate turnover at the membrane surface. Under physiological conditions, endogenous FVIIa engages its cell-localized cofactor tissue factor (TF), which stimulates activity through membrane-dependent substrate recognition and allosteric effects...
November 21, 2017: Proceedings of the National Academy of Sciences of the United States of America
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