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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin.

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.[1]

References

  1. Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin. Hunter, D.D., Porter, B.E., Bulock, J.W., Adams, S.P., Merlie, J.P., Sanes, J.R. Cell (1989) [Pubmed]
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