Synthesis and transport of agrin-like molecules in motor neurons.
Several lines of evidence indicate that agrin, or a protein very similar to it, directs the formation and maintenance of the postsynaptic apparatus at the neuromuscular junction. We discuss the results of studies involving immunohistochemical, biochemical and in situ hybridization techniques that support the hypothesis that agrin or agrin-like molecules active at the junction are produced by motor neurons.
Magill-Solc
C
C
Department of Neurobiology, Stanford University School of Medicine, CA 94305-5401.
McMahan
U J
UJ
D018171:Agrin; D000818:Animals; D000911:Antibodies, Monoclonal; D001369:Axons / Q000502:physiology; D002645:Chickens; D009046:Motor Neurons / Q000502:physiology*; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D009469:Neuromuscular Junction / Q000502:physiology*; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D013569:Synapses / Q000502:physiology*; D014101:Torpedo
D018171:Agrin; D000911:Antibodies, Monoclonal; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger