Search results for: Egon Persson

Items from 1 to 20 out of 32 results

article

FIXing postinfusion monitoring: Assay experiences with N9‐GP (nonacog beta pegol; Refixia^®; Rebinyn^®)

Mirella Ezban, Mette Brunsgaard Hermit, Egon Persson

N9‐GP (nonacog beta pegol; Refixia^®; Rebinyn^®, Novo Nordisk A/S, Bagsværd, Denmark) is a glycoPEGylated extended half‐life recombinant factor IX (rFIX) that exhibits efficacy and potency comparable to unmodified FIX molecules in non‐clinical models. Phase 3 clinical trials have confirmed the efficacy and tolerability of N9‐GP for the prevention and on‐demand treatment of bleeding episodes in patients...

article

Factor VII Tokushima (Cys22→Gly) is not γ-carboxylated due to a disrupted γ-carboxylase recognition site

Christian Dissing, Egon Persson

Thrombosis Research > 2017 > 158 > C > 108-112

•Sequencing and functional analysis show no γ-carboxylation of factor VII Tokushima.•Lack of γ-carboxylation explains <1% procoagulant activity of factor VII Tokushima.•The factor VII Tokushima mutation (C22G) disrupts a γ-carboxylase recognition site.•The γ-carboxylase recognition site is common to proteins homologous to factor VII.

article

More efficient reversal of dabigatran inhibition of coagulation by activated prothrombin complex concentrate or recombinant factor VIIa than by four-factor prothrombin complex concentrate

Tomas L. Lindahl, Maria Wallstedt, Kerstin M. Gustafsson, Egon Persson, more

Thrombosis Research > 2015 > 135 > 3 > 544-547

The number of patients on antithrombotic treatment due to atrial fibrillation and venous thromboembolism is increasing fast due to an aging population. A growing proportion will be treated with novel oral anticoagulants, the first in clinical use was the direct oral thrombin inhibitor dabigatran (Pradaxa®). A small percentage of the patients on dabigatran will experience serious bleeding or be in...

article

The length of the linker between the epidermal growth factor‐like domains in factor VIIa is critical for a productive interaction with tissue factor

Egon Persson, Jesper J. Madsen, Ole H. Olsen

Protein Science > 23 > 12 > 1717 - 1727

Formation of the factor VIIa (FVIIa)‐tissue factor (TF) complex triggers the blood coagulation cascade. Using a structure‐based rationale, we investigated how the length of the linker region between the two epidermal growth factor (EGF)‐like domains in FVIIa influences TF binding and the allosteric activity enhancement, as well as the interplay between the γ‐carboxyglutamic acid (Gla)‐containing and...

article

Novel molecules for the correction of factor Xa generation and phenotype in hemophilia

Egon Persson

Thrombosis Research > 2012 > 129 > Supplement 2 > S51-S53

In the intact hemostatic system, the amount of factor Xa needed for efficient blood coagulation is supplied by the complex between factors VIIIa and IXa. Because hemophilia A patients lack factor VIII and hemophilia B patients lack factor IX, they share a bleeding phenotype that has its root in a dramatically decreased ability to generate factor Xa. These patients are currently treated by replacement...

article

Effects on the conformation of FVIIa by sTF and Ca2+ binding: Studies of fluorescence resonance energy transfer and quenching

Karin Carlsson, Egon Persson, Mikael Lindgren, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2011 > 413 > 4 > 545-549

The apparent length of FVIIa in solution was estimated by a FRET analysis. Two fluorescent probes, fluorescein (Fl-FPR) and a rhodamine derivative (TMR), were covalently attached to FVIIa. The binding site of Fl-FPR was in the protease domain whereas TMR was positioned in the Gla domain, thus allowing a length measure over virtually the whole extension of the protein. From the FRET measurements, the...

article

Intravascular inhibition of factor VIIa and the analogue NN1731 by antithrombin

Lars C. Petersen, Ditte M. Karpf, Henrik Agersø, Mette B. Hermit, more

British Journal of Haematology > 152 > 1 > 99 - 107

NN1731 is a recombinant activated factor VII (rFVIIa) analogue with increased intrinsic activity. This also applies to its reactivity towards antithrombin (AT), the role of which was investigated in a pharmacokinetic (PK) study. NN1731 or rFVIIa was administered to normal and haemophilia A dogs and elimination was measured by FVIIa clot activity, FVIIa‐ and FVIIa‐AT antigen. In vitro AT complex formation...

article

Extensive Small-Angle X-ray Scattering Studies of Blood Coagulation Factor VIIa Reveal Interdomain Flexibility

Charlotte Rode Mosbæk, David Nolan, Egon Persson, Dmitri I. Svergun, more

Biochemistry > 2010 > 49 > 45 > 9739 - 9745

article

Artificial contact pathway activation masks the haemostatic potential of rFVIIa and NN1731 in thrombocytopenic whole blood

Ole H. Larsen, Mirella Ezban, Egon Persson, Jørgen Ingerslev, more

British Journal of Haematology > 150 > 1 > 124 - 127

article

Recombinant coagulation factor VIIa – from molecular to clinical aspects of a versatile haemostatic agent

Egon Persson, Gert Bolt, Thomas D. Steenstrup, Mirella Ezban

Thrombosis Research > 2010 > 125 > 6 > 483-489

Recombinant factor VIIa (rFVIIa, NovoSeven ^® ) is currently the only bypassing agent produced by recombinant technology for the treatment of haemophiliacs whose disease is complicated by inhibitory antibodies. In addition, recombinant production of FVIIa has made it widely available for a variety of purposes and accelerated the growth of our knowledge about FVIIa by generating an abundance...

article

Current status on tissue factor activation of factor VIIa

Egon Persson, Ole H. Olsen

Thrombosis Research > 2010 > 125 > Supplement 1 > S11-S12

Free factor VIIa displays a zymogen-like behavior with low intrinsic activity. Formation of a complex between factor VIIa and tissue factor is necessary to enhance the procoagulant activity of factor VIIa, not only by providing membrane localization, substrate exosites and positioning the active site at an appropriate distance above the surface but also by allosteric enhancement of the enzymatic activity,...

article

Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor

Egon Persson

Thrombosis Research > 2008 > 123 > 1 > 171-176

It was recently reported that protein disulfide isomerase (PDI) stimulates factor X (FX) activation by factor VIIa (FVIIa) bound to soluble tissue factor (sTF) in a purified system and that PDI may be responsible for activating cellular tissue factor (TF) and switching it between its roles in blood coagulation and cellular signalling. This study further investigates the former effect of PDI.FX activations...

article

A loop of coagulation factor VIIa influencing macromolecular substrate specificity

Jais R. Bjelke, Egon Persson, Hanne B. Rasmussen, Birthe B. Kragelund, more

FEBS Letters > 2007 > 581 > 1 > 71-76

Coagulation factor VIIa (FVIIa) belongs to a family of proteases being part of the stepwise, self-amplifying blood coagulation cascade. To investigate the impact of the mutation Met ^298{156} Lys in FVIIa, we replaced the Gly ^283{140} –Met ^298{156} loop with the corresponding loop of factor Xa. The resulting variant exhibited increased intrinsic activity, concurrent with maturation...

article

Inhibitors of factor VIIa affect the interface between the protease domain and tissue factor

Karin Carlsson, Egon Persson, Uno Carlsson, Magdalena Svensson

Biochemical and Biophysical Research Communications > 2006 > 349 > 3 > 1111-1116

Blood coagulation is triggered by the formation of a complex between factor VIIa (FVIIa) and its cofactor, tissue factor (TF). The γ–carboxyglutamic acid-rich domain of FVIIa docks with the C-terminal domain of TF, the EGF1 domain of FVIIa contacts both domains of TF, and the EGF2 domain and protease domain (PD) form a continuous surface that sits on the N-terminal domain of TF. Our aim was to investigate...

article

Macromolecular substrate affinity for free factor VIIa is independent of a buried protease domain N-terminus

Egon Persson

Biochemical and Biophysical Research Communications > 2006 > 341 > 1 > 28-32

The initial recognition and binding of macromolecular substrates by factor VIIa (FVIIa) in complex with tissue factor has been shown to be mediated by areas distinct from the active site (so-called exosites). The present aim was to shed light on whether the N-terminal tail of the protease domain of FVIIa influences factor X (FX) binding, and whether the zymogen-like conformation of free FVIIa has...

article

Sequential coagulation factor VIIa domain binding to tissue factor

Maria Österlund, Egon Persson, Uno Carlsson, Per-Ola Freskgård, more

Biochemical and Biophysical Research Communications > 2005 > 337 > 4 > 1276-1282

Vessel wall tissue factor (TF) is exposed to blood upon vascular damage which enables association with factor VIIa (FVIIa). This leads to initiation of the blood coagulation cascade through localization and allosteric induction of FVIIa procoagulant activity. To examine the docking pathway of the FVIIa–TF complex, various residues in the extracellular part of TF (sTF) that are known to interact with...

article

Activity, Folding, Misfolding, and Aggregation in Vitro of the Naturally Occurring Human Tissue Factor Mutant R200W ^†

Jimmy Wiréhn, Karin Carlsson, Anna Herland, Egon Persson, more

Biochemistry > 2005 > 44 > 18 > 6755 - 6763

article

Transition state analysis of the complex between coagulation factor VIIa and tissue factor: suggesting a sequential domain-binding pathway

Maria Österlund, Egon Persson, Magdalena Svensson, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2005 > 327 > 3 > 789-793

Injury of a blood vessel exposes membrane-bound tissue factor (TF) to blood, which allows binding of coagulation factor VIIa (FVIIa). This initiation of the coagulation cascade is dictated by a specific multi-domain interaction between FVIIa and TF. To examine the energies involved in the transition state of the FVIIa:TF complex, various residues in the extracellular part of TF (sTF) that are known...

article

Characterization of recombinant murine factor VIIa and recombinant murine tissue factor: a human–murine species compatibility study

Lars C. Petersen, Peder L. Nørby, Sven Branner, Brit B. Sørensen, more

Thrombosis Research > 2005 > 116 > 1 > 75-85

Tissue factor (TF) is believed to play an important role in coagulation, inflammation, angiogenesis and wound healing as well as in tumor growth and metastasis. To facilitate in vivo studies in experimental murine models, we have produced recombinant murine factor VII (FVII) and the ectodomain of murine TF, TF(1–223). Murine FVII was activated to FVIIa with human factor Xa and upon reaction with FFR-chloromethyl...

article

Prevention of β Strand Movement into a Zymogen-like Position Does Not Confer Higher Activity to Coagulation Factor VIIa

Ole H. Olsen, Per F. Nielsen, Egon Persson

Biochemistry > 2004 > 43 > 44 > 14096 - 14103

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Keywords

FACTOR VIIA (12)
TISSUE FACTOR (10)
ALLOSTERY (3)
GLA DOMAIN (3)
PROTEIN–PROTEIN INTERACTION (3)
PROTEIN Z (2)
SURFACE PLASMON RESONANCE (2)
CA 2 + BINDING (1)
CA 2 + DEPENDENCE (1)
ACTIVATION POCKET (1)
ACTIVE SITE INHIBITOR (1)
ALLOSTERIC ACTIVATION (1)
ANTITHROMBIN (1)
BLOOD COAGULATION TESTS (1)
CA2+ BINDING (1)
COAGULATION FACTOR VIIA (1)
COAGULATION FACTORS (1)
CONFORMATIONAL DYNAMICS (1)
CORN TRYPSIN INHIBITOR (1)
EGF-LIKE MODULE (1)
EXOSITE INHIBITOR (1)
EXPRESSION (1)
EXTRINSIC XASE (1)
FACTOR IX (1)
FACTOR VII (1)
FACTOR VII DEFICIENCY (1)
FACTOR VIIA; OXIDATION; CHARACTERIZATION; KINETICS; ACTIVITY (1)
FACTOR X ACTIVATION (1)
FLUORESCEIN (1)
FLUORESCENCE (1)
FLUORESCENCE QUENCHING (1)
FLUORESCENCE RESONANCE ENERGY TRANSFER (1)
FLUORESCENT PROBE (1)
GLA MODULE (1)
GLA MUTATION (1)
HAEMOPHILIA B (1)
INITIATION COMPLEX (1)
KINETICS (1)
LIGHT CHAIN (1)
LINKER REGION (1)
MACROMOLECULAR SUBSTRATE SPECIFICITY (1)
MET298{156} (1)
MISSENSE MUTATION (1)
MONITORING (1)
MURINE FACTOR VII (1)
N-TERMINAL INSERTION (1)
N-TERMINUS (1)
NONACOG BETA PEGOL (1)
PROBE (1)
PROTEIN DISULFIDE ISOMERISE (1)
PROTEIN-PROTEIN INTERACTION (1)
RECOMBINANT FACTOR VIIA (1)
RECOMBINANT FACTOR VIIA ANALOGUE (1)
RHODAMINE (1)
STRUCTURAL COMPLEMENTARITY (1)
SUBSTRATE AFFINITY (1)
THROMBOCYTOPENIA (1)
THROMBOELASTOMETRY (1)
TISSUE FACTOR BINDING (1)
TITRATION (1)
TRANSITION STATE (1)
VITAMIN K-DEPENDENT (1)
ZYMOGEN-LIKE (1)
Γ-CARBOXYGLUTAMIC ACID (1)
Γ-CARBOXYLASE RECOGNITION SITE (1)
Γ-CARBOXYLATION (1)
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Data set

Elsevier (23)
ACS (5)
Wiley (4)

Journal

Thrombosis Research (7)
Biochemical and Biophysical Research Communications (5)
Biochemistry (5)
FEBS Letters (4)
Bioorganic & Medicinal Chemistry (2)
Biophysical Journal (2)
British Journal of Haematology (2)
Archives of Biochemistry and Biophysics (1)
BBA - Proteins and Proteomics (1)
Haemophilia (1)
Protein Science (1)
Seminars in Hematology (1)
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INFONA - science communication portal

Search results for: Egon Persson

FIXing postinfusion monitoring: Assay experiences with N9‐GP (nonacog beta pegol; Refixia^®; Rebinyn^®)

Factor VII Tokushima (Cys22→Gly) is not γ-carboxylated due to a disrupted γ-carboxylase recognition site

More efficient reversal of dabigatran inhibition of coagulation by activated prothrombin complex concentrate or recombinant factor VIIa than by four-factor prothrombin complex concentrate

The length of the linker between the epidermal growth factor‐like domains in factor VIIa is critical for a productive interaction with tissue factor

Novel molecules for the correction of factor Xa generation and phenotype in hemophilia

Effects on the conformation of FVIIa by sTF and Ca2+ binding: Studies of fluorescence resonance energy transfer and quenching

Intravascular inhibition of factor VIIa and the analogue NN1731 by antithrombin

Extensive Small-Angle X-ray Scattering Studies of Blood Coagulation Factor VIIa Reveal Interdomain Flexibility

Artificial contact pathway activation masks the haemostatic potential of rFVIIa and NN1731 in thrombocytopenic whole blood

Recombinant coagulation factor VIIa – from molecular to clinical aspects of a versatile haemostatic agent

Current status on tissue factor activation of factor VIIa

Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor

A loop of coagulation factor VIIa influencing macromolecular substrate specificity

Inhibitors of factor VIIa affect the interface between the protease domain and tissue factor

Macromolecular substrate affinity for free factor VIIa is independent of a buried protease domain N-terminus

Sequential coagulation factor VIIa domain binding to tissue factor

Activity, Folding, Misfolding, and Aggregation in Vitro of the Naturally Occurring Human Tissue Factor Mutant R200W ^†

Transition state analysis of the complex between coagulation factor VIIa and tissue factor: suggesting a sequential domain-binding pathway

Characterization of recombinant murine factor VIIa and recombinant murine tissue factor: a human–murine species compatibility study

Prevention of β Strand Movement into a Zymogen-like Position Does Not Confer Higher Activity to Coagulation Factor VIIa

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