title: The binding of natural variants of human factor IX to endothelial cells.
abstract: The Gla-domain of human factor IX contains a specific element required for the binding of factor IX to an endothelial cell surface protein. We have investigated the dependence of this interaction on the structural integrity of the adjacent hydrophobic stack and epidermal growth factor-like domains. The ability of purified natural variants of human factor IX to compete with wild-type factor IX binding to the endothelial cell surface was used to obtain apparent Ki values of the variants. Our data suggest that the functional integrity of the Gla domain, enabling factor IX to specifically interact with an endothelial cell surface protein, depends on the structural and functional integrity of both the hydrophobic stack domain and the first epidermal growth factor-like domain.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, UK.
authors.forename: M
authors.initials: M
authors.lastname: Mayhew
authors.forename: P
authors.initials: P
authors.lastname: Handford
authors.forename: G G
authors.initials: GG
authors.lastname: Brownlee
mesh_terms: D015153:Blotting, Western; D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000166:cytology / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000378:metabolism; D005164:Factor IX / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding
chemical_list: D004815:Epidermal Growth Factor; D005164:Factor IX