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Related Experiment Videos

Platelet factor Xa receptor.

P B Tracy1, M E Nesheim, K G Mann

  • 1Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.

Methods in Enzymology
|January 1, 1992
PubMed
Summary
This summary is machine-generated.

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Factor Va binding to cell membranes is key for prothrombinase complex assembly. Component E of factor Va mediates binding, while component D influences factor Xa interaction and cofactor activity.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Hematology

Background:

  • The prothrombinase complex is crucial for blood coagulation.
  • Factor Va acts as a cofactor in this complex, assembling on cell membranes.

Purpose of the Study:

  • To elucidate the binding interactions and roles of factor Va subunits in prothrombinase complex assembly and function on various cell surfaces.
  • To investigate the contribution of factor Va components E and D to factor Xa binding and catalytic activity.

Main Methods:

  • Investigated factor Va binding to bovine platelets, human monocytes, lymphocytes, neutrophils, and phospholipid vesicles.
  • Utilized biophysical and biochemical assays to study protein-protein interactions and enzymatic activity.

Main Results:

Related Experiment Videos

  • Factor Va component E mediates binding to cell membranes and phospholipid vesicles.
  • Factor Va component D associates with component E via metal ion-dependent interactions.
  • Factor Va, particularly component E, forms part of the receptor for factor Xa on the membrane surface.
  • Component D's interaction with factor Xa is implied, and its cleavage by activated protein C abolishes factor Va cofactor activity.

Conclusions:

  • Factor Va assembly on membranes involves specific subunit interactions.
  • Component E is essential for membrane binding and factor Xa interaction.
  • Component D plays a significant role in factor Xa binding and cofactor activity, potentially mediating prothrombin binding and enhancing catalytic efficiency.