Binding of coagulation factors IX and X to the endothelial cell surface

Ronald L. Heimark, Stephen M. Schwartz

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

Bovine coagulation factors IX and X bind to independent sites on bovine aortic endothelial cells. Binding studies with cells maintained serum-free showed that there are at least two classes of binding sites for factor IX and factor X with a dissociation constant of 4.9 × 10-9 M and 2.1 × 10-8 M for the respective high affinity sites. Ca+2 was required for specific binding and was reversed by addition of EDTA or EGTA. Competition experiments showed that factor IX and factor IXa bind to the same sites, which are different from the factor X binding sites. Neither binding of factor IX or factor X is inhibited by addition of prothrombin or protein C. Indirect immunofluorescence of factor IX indicated that binding was diffuse on the cell surface.

Original languageEnglish (US)
Pages (from-to)723-731
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume111
Issue number2
DOIs
StatePublished - Mar 16 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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