Human factor IX binds to specific sites on the collagenous domain of collagen IV.
The primary region of factor IX that mediates binding to bovine aortic endothelial cells resides in residues 3-11 of the N-terminal region known as the Gla domain. Recently, it was proposed that the observed binding to endothelial cells is actually a measure of the interaction between factor IX and collagen IV (Cheung, W. F., van den Born, J., Kuhn, K., Kjellen, L., Hudson, B. G., and Stafford, D. W. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 11068-11073). To confirm that factor IX binds to collagen IV and to examine the specificity of this interaction, we used scanning force microscopy to examine factor IX binding to collagen IV. We imaged collagen IV in the presence and the absence of factor IX and observed specific interactions between factor IX and collagen IV. Our results demonstrate that factor IX binds to collagen IV at specific sites in the collagenous domain approximately 98 and approximately 50 nm from the C-terminal pepsin-cleaved end.
Wolberg
A S
AS
Department of Biology and Center for Thrombosis and Hemostasis, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Stafford
D W
DW
Erie
D A
DA
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D005164:Factor IX / Q000378:metabolism*; D006801:Humans; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D011485:Protein Binding
D005164:Factor IX; D003094:Collagen