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PRIMARY SEQUENCE OF A MOTOR NEURON SELECTIVE ADHESIVE SITE IN THE SYNAPTIC BASAL LAMINA PROTEIN S-LAMININ CELL Hunter, D. D., Porter, B. E., BULOCK, J. W., Adams, S. P., Merlie, J. P., Sanes, J. R. 1989; 59 (5): 905-913

Abstract

S-laminin, a novel homolog of laminin, is concentrated in a subset of basal laminae including the basal lamina that passes between motor nerve terminals and muscle fibers at the neuromuscular junction. Here we used recombinant fragments to localize a neuronal attachment site to the C-terminal 10% of s-laminin. We then used synthetic peptides spanning the active fragment to identify the primary sequence of the adhesive site as Leu-Arg-Glu (LRE): neurons attach to an immobilized LRE-containing peptide, and soluble LRE blocks attachment of neurons to the s-laminin fragment. Whereas ciliary ganglion neurons (which normally innervate muscle fibers) adhered well both to laminin and to an s-laminin fragment, sensory and central neurons and several neuronal cell lines all adhered well to laminin but poorly to the s-laminin fragment. Together, these results define a motor neuron-selective attachment site on s-laminin.

View details for Web of Science ID A1989CC79800015

View details for PubMedID 2590946