NDLI: Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance.

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Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sen, Prosenjit Neuenschwander, Pierre F. Pendurthi, Usha R. Rao, L. Vijaya Mohan
Description	Country affiliation: United States Author Affiliation: Sen P ( The University of Texas Health Science Center at Tyler, Texas 75708, USA.)
Abstract	Kinetic analysis of the tissue factor (TF)-factor VIIa (FVIIa) binding interaction is helpful in investigating the structure-function relationships of TF-FVIIa. However, a wide variation exists among the reported binding affinities of FVIIa to TF, particularly when comparing KD values obtained from functional activity assays versus ligand binding studies. Surface plasmon resonance (SPR) technique was used frequently to investigate binding kinetics of FVIIa to TF in a lipid-free environment. In the present study we used TF embedded in a phospholipid bilayer for determining binding kinectis using SPR. The data revealed that FVIIa had a much higher binding affinity (>100-fold) for TF embedded in the phospholiid bilayer than TF in a lipid-free environment, approaching the KD values that were noted in the enzymatic activity assays. The present data suggest that SPR binding studies using TF embedded in phospholipids is more appropriate for investigating how FVIIa (or FVIIa mutants/derivatives) may interact with TF in physiological settings.
File Format	HTM / HTML
ISSN	09575235
e-ISSN	14735733
DOI	10.1097/MBC.0b013e328333b084
Journal	Blood Coagulation & Fibrinolysis
Issue Number	4
Volume Number	21
Language	English
Publisher	Lippincott Williams & Wilkins
Publisher Date	2010-06-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Hematology Factor Viia Metabolism Surface Plasmon Resonance Thromboplastin Kinetics Phospholipids Protein Binding Recombinant Proteins Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Hematology

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Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance

Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor.

Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa.

Factor VIIa interaction with tissue factor and endothelial cell protein C receptor on cell surfaces.

Determining selectivity of phosphoinositide-binding domains.

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

Disulfide reduction abolishes tissue factor cofactor function.

Surface plasmon resonance analysis of the mechanism of binding of apoA-I to high density lipoprotein particles.

Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.

Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance.

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Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance

Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor.

Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa.

Factor VIIa interaction with tissue factor and endothelial cell protein C receptor on cell surfaces.

Determining selectivity of phosphoinositide-binding domains.

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

Disulfide reduction abolishes tissue factor cofactor function.

Surface plasmon resonance analysis of the mechanism of binding of apoA-I to high density lipoprotein particles.

Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.

Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance.