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Volume 272, Number 15, Issue of April 11, 1997 pp. 10125-10134
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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The First Immunoglobulin-like Neural Cell Adhesion Molecule (NCAM) Domain Is Involved in Double-reciprocal Interaction with the Second Immunoglobulin-like NCAM Domain and in Heparin Binding

(Received for publication, June 6, 1996, and in revised form, December 26, 1996)

From the Protein Laboratory, Panum Institute, University of Copenhagen, Blegdamsvej 3C, Building 6.2, DK-2200 Copenhagen, and the ^§ Department of Biology, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100 Copenhagen, Denmark

To study the function of the first immunoglobulin (Ig)-like domain of the neural cell adhesion molecule (NCAM), it was produced as a recombinant fusion protein in a bacterial expression system and as a recombinant protein in a eukaryotic expression system of the yeast Pichia pastoris. For comparison, other NCAM domains were also produced as fusion proteins. By means of surface plasmon resonance analysis, it was shown that the first Ig-like NCAM domain binds the second Ig-like NCAM domain with a dissociation constant 5.5 ± 1.6 × 10⁵ M. Furthermore, it was found that the first Ig-like domain binds heparin. It was also demonstrated that the second Ig-like NCAM domain binds heparin and that both domains bind collagen type I via heparin but not collagen type I directly.

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