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Journal of Neuroscience, Vol 11, 3960-3971, Copyright © 1991 by Society for Neuroscience
An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to S-laminin
DD Hunter, N Cashman, R Morris-Valero, JW Bulock, SP Adams and JR Sanes
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
S-laminin is a homolog of laminin that is concentrated in the synaptic
cleft of the neuromuscular junction. We previously showed that the
tripeptide LRE is a crucial determinant for binding of ciliary motoneurons
to recombinant s-laminin. Here, we describe a neuroblastoma- spinal neuron
hybrid cell line, NSC-34, that binds to an LRE-containing s-laminin
fragment and to a synthetic LRE-protein conjugate. NSC-34 cells exhibit
several properties of motoneurons; other cell lines tested were not
motoneuron-like and did not display LRE-dependent adhesion. We therefore
used NSC-34 cells to characterize the LRE- dependent adhesion mechanism.
Inhibition studies with a series of 20 tripeptide LRE analogs showed that
the cells exhibit a high degree of selectivity for LRE, and suggested that
ligand binding requires a combination of electrostatic and hydrophobic
interactions. The effects of cations on LRE-dependent adhesion are unlike
those of previously described adhesion molecules including the integrins, a
family of receptors for extracellular matrix proteins, including laminin.
Specifically, adhesion to LRE does not require divalent cations and is
inhibited by Ca2+ (but not by Mg2+) in the physiological range. In
contrast, adhesion of NSC-34 cells to laminin is LRE- and Ca2+ independent
but Mg2+ dependent, and appears to be mediated by integrins. Additionally,
experiments using mixed substrates demonstrated that LRE-protein conjugates
inhibit neurite outgrowth promoted by laminin. Finally, we show that, under
ionic conditions that minimize integrin-dependent adhesion, NSC-34 cells
bind to s-laminin- rich basal laminae in tissue sections in an
LRE-dependent manner. Together, these results suggest that LRE comprises a
motoneuron- selective adhesion site that is accessible in native basal
laminae and that acts to inhibit neurite outgrowth.
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