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J Biol Chem, Vol. 274, Issue 35, 24602-24610, August 27, 1999
From the Tumor Immunology Programme, G0100, German Cancer Research
Center, D-69120 Heidelberg, Germany and the The cell adhesion molecule L1, a 200-220-kDa
type I membrane glycoprotein of the Ig superfamily, mediates many
neuronal processes. Originally studied in the nervous system, L1 is
expressed by hematopoietic and many epithelial cells, suggesting a more
expanded role. L1 supports homophilic L1-L1 and integrin-mediated cell
binding and can also bind with high affinity to the neural proteoglycan
neurocan; however, the binding site is unknown. We have dissected the
L1 molecule and investigated the cell binding ability of Ig domains 1 and 6. We report that RGD sites in domain 6 support
Integrin and Neurocan Binding to L1 Involves Distinct Ig
Domains
, and Department of
Experimental Pathology, University of Lund, University Hospital,
S-22185 Lund, Sweden
5
1- or v3-mediated integrin binding and that both RGD sites are
essential. Cooperation of RGD sites with neighboring domains are
necessary for 51. A T cell
hybridoma and activated T cells could bind to L1 in the absence of
RGDs. This binding was supported by Ig domain 1 and mediated by cell
surface-exposed neurocan. Lymphoid and brain-derived neurocan were
structurally similar. We also present evidence that a fusion protein of
the Ig 1-like domain of L1 can bind to recombinant neurocan. Our
results support the notion that L1 provides distinct cell binding sites
that may serve in cell-cell or cell-matrix interactions.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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