QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (22) Citing Articles via Google Scholar Google Scholar Articles by Bowen, D. C. Articles by Hall, Z. W. Search for Related Content PubMed PubMed Citation Articles by Bowen, D. C. Articles by Hall, Z. W.

Next Article 

Volume 16, Number 12, Issue of June 15, 1996 pp. 3791-3797
Copyright ©1996 Society for Neuroscience

Neural Agrin Activates a High-Affinity Receptor in C2 Muscle Cells that Is Unresponsive to Muscle Agrin

Received Jan. 10, 1996; revised March 18, 1996; accepted March 25, 1996.

David C. Bowen¹, Janice Sugiyama², Michael Ferns³, and Zach W. Hall²

¹ Regeneron Pharmaceuticals, Tarrytown, New York 10591, ² National Institute of Mental Health, National Institutes of Health, Bethesda, Maryland 20892, and ³ Department of Neurosurgery, Montréal General Hospital Research Institute, Montréal, Québec, Canada H3G 1A4

During synaptogenesis, agrin, released by motor nerves, causes the clustering of acetylcholine receptors (AChRs) in the skeletal muscle membrane. Although muscle -dystroglycan has been postulated to be the receptor for the activity of agrin, previous experiments have revealed a discrepancy between the biological activity of soluble fragments of two isoforms of agrin produced by nerves and muscles, respectively, and their ability to bind -dystroglycan. We have determined the specificity of the signaling receptor by investigating whether muscle agrin can block the activity of neural agrin on intact C2 myotubes. We find that a large excess of muscle agrin failed to inhibit either the number of AChR clusters or the phosphorylation of the AChR induced by picomolar concentrations of neural agrin. These results indicate that neural, but not muscle, agrin interacts with the signaling receptor. Muscle agrin did block the binding of neural agrin to isolated -dystroglycan, however, suggesting either that -dystroglycan is not the signaling receptor or that its properties in the membrane are altered. Direct assay of the binding of muscle or neural agrin to intact myotubes revealed only low-affinity binding. We conclude that the signaling receptor for agrin is a high-affinity receptor that is highly specific for the neural form.

Key words: acetylcholine receptor; agrin; dystroglycan; muscle; receptor; synaptogenesis

This article has been cited by other articles:

				C. M. Bose, D. Qiu, A. Bergamaschi, B. Gravante, M. Bossi, A. Villa, F. Rupp, and A. Malgaroli Agrin Controls Synaptic Differentiation in Hippocampal Neurons J. Neurosci., December 15, 2000; 20(24): 9086 - 9095. [Abstract] [Full Text] [PDF]

				C. Weston, B. Yee, E. Hod, and J. Prives Agrin-induced Acetylcholine Receptor Clustering Is Mediated by the Small Guanosine Triphosphatases Rac and Cdc42 J. Cell Biol., July 11, 2000; 150(1): 205 - 212. [Abstract] [Full Text] [PDF]

				L. G. W. Hilgenberg, C. L. Hoover, and M. A. Smith Evidence of an Agrin Receptor in Cortical Neurons J. Neurosci., September 1, 1999; 19(17): 7384 - 7393. [Abstract] [Full Text] [PDF]

				C. Jacobson, F. Montanaro, M. Lindenbaum, S. Carbonetto, and M. Ferns alpha -Dystroglycan Functions in Acetylcholine Receptor Aggregation But Is Not a Coreceptor for Agrin-MuSK Signaling J. Neurosci., August 15, 1998; 18(16): 6340 - 6348. [Abstract] [Full Text] [PDF]

				J.E. Sugiyama, D.J. Glass, G.D. Yancopoulos, and Z.W. Hall Laminin-induced Acetylcholine Receptor Clustering: An Alternative Pathway J. Cell Biol., October 6, 1997; 139(1): 181 - 191. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help