title: Identification of agrin in electric organ extracts and localization of agrin-like molecules in muscle and central nervous system.
abstract: The portion of the muscle fibre's basal lamina that occupies the synaptic cleft at the neuromuscular junction contains molecules that cause the aggregation of acetylcholine receptors and acetylcholinesterase on regenerating muscle fibres. Agrin, which is extracted from basal lamina-containing fractions of the Torpedo electric organ and causes the formation of acetylcholine receptor and acetylcholinesterase aggregates on cultured myotubes, may be similar, if not identical, to the acetylcholine receptor- and acetylcholinesterase-aggregating molecules at the neuro-muscular junction. Here we summarize experiments which led to the identification of agrin and established that the basal lamina at the neuromuscular junction contains molecules antigenically similar to agrin. We also discuss results which raise the possibility that agrin-like molecules at the neuromuscular junction are produced by motor neurones.
authors.affiliation: Department of Neurobiology, Stanford University School of Medicine, CA 94305.
authors.forename: M A
authors.initials: MA
authors.lastname: Smith
authors.forename: Y M
authors.initials: YM
authors.lastname: Yao
authors.forename: N E
authors.initials: NE
authors.lastname: Reist
authors.forename: C
authors.initials: C
authors.lastname: Magill
authors.forename: B G
authors.initials: BG
authors.lastname: Wallace
authors.forename: U J
authors.initials: UJ
authors.lastname: McMahan
mesh_terms: D018171:Agrin; D000818:Animals; D002490:Central Nervous System / Q000032:analysis*; D004557:Electric Organ / Q000032:analysis*; D009132:Muscles / Q000032:analysis*; D009419:Nerve Tissue Proteins / Q000032:analysis*; D014101:Torpedo / Q000502:physiology*
chemical_list: D018171:Agrin; D009419:Nerve Tissue Proteins