The endothelial cell binding determinant of human factor IX resides in the. gamma. -carboxyglutamic acid domain
- Univ. of North Carolina, Chapel Hill (United States)
- Univ. of New Mexico, Albuquerque, NM (United States) United Blood Services, Albuquerque, NM (United States)
The blood coagulation factor IX(a) binds specifically to a site on endothelial cells with a K{sub d} of 2.0-3.0 nM. A number of previous studies have attempted to define the region(s) of factor IX(a) that mediate this interaction. These studies suggested that there are two regions of factor IX(a), the {gamma}-carboxyglutamic acid (Gla) domain and the epidermal growth factor like (EGF-like) domains, that mediate high-affinity binding to endothelial cells. Recently, however, the participation of the EGF1 domain has been excluded from the interaction. This indicated that if there was an EGF component of factor IX contributing to the binding affinity, then it must be in the second EGF-like domain. In order to further evaluate this relationship, the authors performed competitive binding experiments between {sup 125}I plasma factor IX and a set of six chimeric proteins composed of portions of factor VII and factor IX. The data suggest that the high-affinity interaction between factor IX and the endothelial cell binding site is mediated by the factor IX Gla domain and that the factor IX EGF domains are not involved in binding specificity.
- OSTI ID:
- 5687683
- Journal Information:
- Biochemistry; (United States), Vol. 31:6; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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