title: A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction.
abstract: A striking example of topographic specificity in synapse formation is the preferential reinnervation of original synaptic sites on denervated muscle fibres by regenerating motor axons. This specificity is mediated by the basal lamina of the synaptic cleft. A glycoprotein, s-laminin, has now been identified that is selectively associated with synaptic basal lamina and is recognized by motoneurons. Molecular cloning reveals that s-laminin is a novel homologue of laminin, a potent promoter of neurite outgrowth.
authors.affiliation: Department of Anatomy, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: D D
authors.initials: DD
authors.lastname: Hunter
authors.forename: V
authors.initials: V
authors.lastname: Shah
authors.forename: J P
authors.initials: JP
authors.lastname: Merlie
authors.forename: J R
authors.initials: JR
authors.lastname: Sanes
mesh_terms: D001483:Base Sequence; D001485:Basement Membrane / Q000378:metabolism; D003001:Cloning, Molecular; D015151:Immunoblotting; D007797:Laminin / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009046:Motor Neurons / Q000378:metabolism; D009416:Nerve Regeneration; D009469:Neuromuscular Junction / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013569:Synapses / Q000378:metabolism*
chemical_list: D007797:Laminin; D011994:Recombinant Proteins; C058783:laminin beta2