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Vol. 9, Issue 2, 277-290, February 1998
v
3 Integrin
and
*Banting and Best Department of Medical Research and Department of
Biochemistry, University of Toronto, Toronto, Ontario M5G 1L6, Canada;
and
The cell adhesion molecule L1 is a potent inducer of neurite
outgrowth and it has been implicated in X-linked hydrocephalus and
related neurological disorders. To investigate the mechanisms of
neurite outgrowth stimulated by L1, attempts were made to identify the
neuritogenic sites in L1. Fusion proteins containing different segments
of the extracellular region of L1 were prepared and different neuronal
cells were assayed on substrate-coated fusion proteins. Interestingly,
both immunoglobulin (Ig)-like domains 2 and 6 (Ig2, Ig6) promoted
neurite outgrowth from dorsal root ganglion cells, whereas neural
retinal cells responded only to Ig2. L1 Ig2 contains a previously
identified homophilic binding site, whereas L1 Ig6 contains an
Arg-Gly-Asp (RGD) sequence. The neuritogenic activity of Ig6 was
abrogated by mutations in the RGD site. The addition of RGD-containing
peptides also inhibited the promotion of neurite outgrowth from dorsal
root ganglion cells by glutathione S-transferase-Ig6, implicating the involvement of an integrin. The monoclonal
antibody LM609 against Department of Immunology, The Scripps Research
Institute, La Jolla, California 92037
v
3
integrin, but not an anti-1 antibody, inhibited the neuritogenic effects of Ig6. These data thus provide the first evidence that the RGD motif in L1 Ig6 is capable of promoting neurite
outgrowth via interaction with the v3
integrin on neuronal cells.
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