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• W1567503172 endingPage "20287" @default.
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• W1567503172 abstract "Previous studies have indicated that Factor IX/IXa interacts in a specific and high affinity manner with a binding site on the endothelial cell surface. In this study, the contributions of the gamma-carboxyglutamic acid-containing (GLA) and growth factor domains to the finding of Factor IX to the endothelium were assessed. While GLA-containing peptides from Factors IX, X, and prothrombin were inhibitors of 125I-Factor IX-endothelial cell binding, the GLA peptide from Factor IX was about 250-800-fold more effective than those from prothrombin and Factor X, respectively. In contrast to its relative efficacy as an inhibitor of Factor IX-cell surface interaction, the Factor IX-GLA peptide neither bound to lipid vesicles nor inhibited Factor IX-lipid interaction. A synthetic peptide comprising the entire first epidermal growth factor (EGF) exon was also an inhibitor of 125I-Factor IX-endothelial cell binding, although it did not interact with lipid vesicles. Experiments with synthetic peptides comprising each of the three loops of the first EGF domain or the entire first EGF region with specific substitutions indicated the importance of determinants in both the first and probably third loops for Factor IX-endothelial interaction. In contrast, the second loop of the first EGF domain and the first loop of the second EGF exon are probably not involved in Factor IX-endothelial interaction based on their inability to block 125I-Factor IX binding to cells. These results indicate that determinants in both the GLA and the first EGF domain contribute to the specific binding of Factor IX to the endothelial cell surface and that structural requirements for Factor IX-cell surface interaction are distinct from those for Factor IX binding to lipids." @default.
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• W1567503172 date "1989-12-01" @default.
• W1567503172 modified "2023-09-27" @default.
• W1567503172 title "Structural Determinants of the Factor IX Molecule Mediating Interaction with the Endothelial Cell Binding Site Are Distinct from Those Involved in Phospholipid Binding" @default.
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• W1567503172 doi "https://doi.org/10.1016/s0021-9258(19)47059-2" @default.
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