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(Received for publication, November 14, 1996, and in revised form, April 28, 1997)
,
and
From the 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 ~98 and ~50 nm from the C-terminal
pepsin-cleaved end.
Department of Biology and Center for
Thrombosis and Hemostasis and the ¶ Department of Chemistry,
University of North Carolina, Chapel Hill, North Carolina 27599
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