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Motor Neurons Contain Agrin-like Molecules

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1988 Nov 1
PMID 2846587
Citations 22
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Abstract

Molecules antigenically similar to agrin, a protein extracted from the electric organ of Torpedo californica, are highly concentrated in the synaptic basal lamina of neuromuscular junctions in vertebrate skeletal muscle. On the basis of several lines of evidence it has been proposed that agrin-like molecules mediate the nerve-induced formation of acetylcholine receptor (AChR) and acetylcholinesterase (AChE) aggregates on the surface of muscle fibers at developing and regenerating neuromuscular junctions and that they help maintain these postsynaptic specializations in the adult. Here we show that anti-agrin monoclonal antibodies selectively stain the cell bodies of motor neurons in embryos and adults, and that the stain is concentrated in the Golgi apparatus. We also present evidence that motor neurons in both embryos and adults contain molecules that cause the formation of AChR and AChE aggregates on cultured myotubes and that these AChR/AChE-aggregating molecules are antigenically similar to agrin. These findings are consistent with the hypothesis that agrin-like molecules are synthesized by motor neurons, and are released from their axon terminals to become incorporated into the synaptic basal lamina where they direct the formation of synapses during development and regeneration.

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References
1.
Schaffner A, Daniels M . Conditioned medium from cultures of embryonic neurons contains a high molecular weight factor which induces acetylcholine receptor aggregation on cultured myotubes. J Neurosci. 1982; 2(5):623-32. PMC: 6564262. View

2.
Claude P, Hawrot E, Dunis D, Campenot R . Binding, internalization, and retrograde transport of 125I-nerve growth factor in cultured rat sympathetic neurons. J Neurosci. 1982; 2(4):431-42. PMC: 6564245. View

3.
McMahan U, Slater C . The influence of basal lamina on the accumulation of acetylcholine receptors at synaptic sites in regenerating muscle. J Cell Biol. 1984; 98(4):1453-73. PMC: 2113239. DOI: 10.1083/jcb.98.4.1453. View

4.
Jacob M, Berg D, Lindstrom J . Shared antigenic determinant between the Electrophorus acetylcholine receptor and a synaptic component on chicken ciliary ganglion neurons. Proc Natl Acad Sci U S A. 1984; 81(10):3223-7. PMC: 345254. DOI: 10.1073/pnas.81.10.3223. View

5.
GODFREY E, Nitkin R, Wallace B, Rubin L, McMahan U . Components of Torpedo electric organ and muscle that cause aggregation of acetylcholine receptors on cultured muscle cells. J Cell Biol. 1984; 99(2):615-27. PMC: 2113273. DOI: 10.1083/jcb.99.2.615. View