JBC Transcription and Nuclear Factor Monoclonals

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Volume 272, Number 27, Issue of July 4, 1997 pp. 16717-16720
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Human Factor IX Binds to Specific Sites on the Collagenous Domain of Collagen IV

(Received for publication, November 14, 1996, and in revised form, April 28, 1997)

Alisa S. Wolberg Dagger , Darrel W. Stafford Dagger and Dorothy A. Erie

From the Dagger  Department of Biology and Center for Thrombosis and Hemostasis and the  Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599

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.


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