scholarly journals Laminin induces acetylcholine receptor aggregation on cultured myotubes and enhances the receptor aggregation activity of a neuronal factor

1983 ◽  
Vol 3 (5) ◽  
pp. 1058-1068 ◽  
Author(s):  
Z Vogel ◽  
CN Christian ◽  
M Vigny ◽  
HC Bauer ◽  
P Sonderegger ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Receptor Aggregation ◽  
Cultured Myotubes ◽  
Aggregation Activity

scholarly journals Neuregulin Inhibits Acetylcholine Receptor Aggregation in Myotubes

2004 ◽  
Vol 279 (30) ◽  
pp. 31622-31628 ◽  
Author(s):  
Jonathan C. Trinidad ◽  
Jonathan B. Cohen
Keyword(s):  
Acetylcholine Receptor ◽  
Receptor Aggregation

RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes

Neuron ◽  
1992 ◽  
Vol 8 (6) ◽  
pp. 1079-1086 ◽  
Author(s):  
Michael Ferns ◽  
Werner Hoch ◽  
James T. Campanelli ◽  
Fabio Rupp ◽  
Zach W. Hall ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Rna Splicing ◽  
Receptor Clustering ◽  
Cultured Myotubes

scholarly journals Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

1987 ◽  
Vol 105 (6) ◽  
pp. 2471-2478 ◽  
Author(s):  
R M Nitkin ◽  
M A Smith ◽  
C Magill ◽  
J R Fallon ◽  
Y M Yao ◽  
...  
Keyword(s):  
Acetylcholine Receptors ◽  
Neuromuscular Junctions ◽  
Gel Filtration ◽  
Electric Organ ◽  
Molecular Characteristics ◽  
Active Components ◽  
Cultured Myotubes ◽  
Aggregation Activity ◽  
Two Peaks

Extracts of the electric organ of Torpedo californica contain a proteinaceous factor that causes the formation of patches on cultured myotubes at which acetylcholine receptors (AChR), acetylcholinesterase (AChE), and butyrylcholinesterase (BuChE) are concentrated. Results of previous experiments indicate that this factor is similar to the molecules in the synaptic basal lamina that direct the aggregation of AChR and AChE at regenerating neuromuscular junctions in vivo. We have purified the active components in the extracts 9,000-fold. mAbs against four different epitopes on the AChR/AChE/BuChE-aggregating molecules each immunoprecipitated four polypeptides from electric organ extracts, with molecular masses of 150, 135, 95, and 70 kD. Gel filtration chromatography of electric organ extracts revealed two peaks of AChR/AChE/BuChE-aggregation activity; one comigrated with the 150-kD polypeptide, the other with the 95-kD polypeptide. The 135- and 70-kD polypeptides did not cause AChR/AChE/BuChE aggregation. Based on these molecular characteristics and on the pattern of staining seen in sections of muscle labeled with the mAbs, we conclude that the electric organ-aggregating factor is distinct from previously identified molecules, and we have named it "agrin."

scholarly journals α-Dystroglycan Functions in Acetylcholine Receptor Aggregation But Is Not a Coreceptor for Agrin-MuSK Signaling

1998 ◽  
Vol 18 (16) ◽  
pp. 6340-6348 ◽  
Author(s):  
Christian Jacobson ◽  
Federica Montanaro ◽  
Michael Lindenbaum ◽  
Salvatore Carbonetto ◽  
Michael Ferns
Keyword(s):  
Acetylcholine Receptor ◽  
Receptor Aggregation

scholarly journals Agrin Can Mediate Acetylcholine Receptor Gene Expression in Muscle by Aggregation of Muscle-derived Neuregulins

1998 ◽  
Vol 141 (3) ◽  
pp. 715-726 ◽  
Author(s):  
Thomas Meier ◽  
Fabrizio Masciulli ◽  
Chris Moore ◽  
Fabrice Schoumacher ◽  
Urs Eppenberger ◽  
...  
Keyword(s):  
Gene Expression ◽  
Neuromuscular Junction ◽  
Acetylcholine Receptor ◽  
Gene Transcription ◽  
Radioligand Binding ◽  
Muscle Fibers ◽  
Erbb Receptors ◽  
Pcr Analysis ◽  
Subunit Gene ◽  
Cultured Myotubes

The neural isoforms of agrin can stimulate transcription of the acetylcholine receptor (AChR) ε subunit gene in electrically active muscle fibers, as does the motor neuron upon the formation of a neuromuscular junction. It is not clear, however, whether this induction involves neuregulins (NRGs), which stimulate AChR subunit gene transcription in vitro by activating ErbB receptors. In this study, we show that agrin- induced induction of AChR ε subunit gene transcription is inhibited in cultured myotubes overexpressing an inactive mutant of the ErbB2 receptor, demonstrating involvement of the NRG/ErbB pathway in agrin- induced AChR expression. Furthermore, salt extracts from the surface of cultured myotubes induce tyrosine phosphorylation of ErbB2 receptors, indicating that muscle cells express biological NRG-like activity on their surface. We further demonstrate by RT-PCR analysis that muscle NRGs have Ig-like domains required for their immobilization at heparan sulfate proteoglycans (HSPGs) of the extracellular matrix. In extrasynaptic regions of innervated muscle fibers in vivo, ectopically expressed neural agrin induces the colocalized accumulation of AChRs, muscle-derived NRGs, and HSPGs. By using overlay and radioligand-binding assays we show that the Ig domain of NRGs bind to the HSPGs agrin and perlecan. These findings show that neural agrin can induce AChR subunit gene transcription by aggregating muscle HSPGs on the muscle fiber surface that then serve as a local sink for focal binding of muscle-derived NRGs to regulate AChR gene expression at the neuromuscular junction.

Sign in / Sign up

Export Citation Format

Share Document