Establishment of Neuromuscular Contacts in Cultures of Rat Embryonic Cells: Effect of Tetrodotoxin on Maturation of Muscle Fibers and on Formation and Maintenance of Acetylcholinesterase and Acetylcholine Receptor Clusters

1982 ◽  
Vol 5 (4) ◽  
pp. 314-325 ◽  
Author(s):  
J. Koenig ◽  
M. Oren ◽  
M.A.B. Melone
Keyword(s):  
Acetylcholine Receptor ◽  
Muscle Fibers ◽  
Embryonic Cells ◽  
Receptor Clusters

scholarly journals Ultrastructure of acetylcholine receptor clusters on cultured muscle fibers.

1976 ◽  
Vol 69 (2) ◽  
pp. 501-507 ◽  
Author(s):  
Z Vogel ◽  
M P Daniels
Keyword(s):  
Skeletal Muscle ◽  
Acetylcholine Receptor ◽  
Muscle Fibers ◽  
The Other ◽  
Immunoperoxidase Staining ◽  
High Concentration ◽  
Receptor Clusters ◽  
Ach Receptors

The structure of regions with a high concentration of ACh receptors (clusters) on cultured skeletal muscle myotubes was examined by immunoperoxidase staining of bound alphaBT. The clusters did not appear to differ from the other regions except in their higher concentration of receptor.

scholarly journals Might prepatterned acetylcholine-receptor clusters on surface myotubes be a sign of neuromuscular-junction maturation failure?

2013 ◽  
Vol 4 ◽  
pp. 319-323
Author(s):  
Anna Fidziańska ◽  
Maria Jędrzejowska ◽  
Agnieszka Madej-Pilarczyk ◽  
Jacek Bojakowski
Keyword(s):  
Neuromuscular Junction ◽  
Acetylcholine Receptor ◽  
Receptor Clusters

A novel AP180-related protein in vesicles that concentrate at acetylcholine receptor clusters

1998 ◽  
Vol 68 (4) ◽  
pp. 457-471 ◽  
Author(s):  
S. Bursztajn ◽  
S. Vincent ◽  
F.M. Brodsky ◽  
F. Benes ◽  
S.A. Morris
Keyword(s):  
Acetylcholine Receptor ◽  
Related Protein ◽  
Receptor Clusters

scholarly journals Defective Acetylcholine Receptor Subunit Switch Precedes Atrophy of Slow-Twitch Skeletal Muscle Fibers Lacking ERK1/2 Kinases in Soleus Muscle

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Shuo Wang ◽  
Bonnie Seaberg ◽  
Ximena Paez-Colasante ◽  
Mendell Rimer
Keyword(s):  
Skeletal Muscle ◽  
Acetylcholine Receptor ◽  
Soleus Muscle ◽  
Muscle Fibers ◽  
Neuromuscular Synapse ◽  
Fiber Morphology ◽  
Skeletal Muscle Fibers ◽  
Slow Twitch

Abstract To test the role of extracellular-signal regulated kinases 1 and 2 (ERK1/2) in slow-twitch, type 1 skeletal muscle fibers, we studied the soleus muscle in mice genetically deficient for myofiber ERK1/2. Young adult mutant soleus was drastically wasted, with highly atrophied type 1 fibers, denervation at most synaptic sites, induction of “fetal” acetylcholine receptor gamma subunit (AChRγ), reduction of “adult” AChRε, and impaired mitochondrial biogenesis and function. In weanlings, fiber morphology and mitochondrial markers were mostly normal, yet AChRγ upregulation and AChRε downregulation were observed. Synaptic sites with fetal AChRs in weanling muscle were ~3% in control and ~40% in mutants, with most of the latter on type 1 fibers. These results suggest that: (1) ERK1/2 are critical for slow-twitch fiber growth; (2) a defective γ/ε-AChR subunit switch, preferentially at synapses on slow fibers, precedes wasting of mutant soleus; (3) denervation is likely to drive this wasting, and (4) the neuromuscular synapse is a primary subcellular target for muscle ERK1/2 function in vivo.

The membrane skeleton of acetylcholine receptor domains in rat myotubes contains antiparallel homodimers of beta-spectrin in filaments quantitatively resembling those of erythrocytes

1995 ◽  
Vol 108 (9) ◽  
pp. 3145-3154 ◽  
Author(s):  
D.W. Pumplin
Keyword(s):  
Monoclonal Antibody ◽  
Acetylcholine Receptor ◽  
Acetylcholine Receptors ◽  
Cytoplasmic Membrane ◽  
Membrane Surface ◽  
Membrane Skeleton ◽  
Immunogold Labeling ◽  
Platinum Coating ◽  
High Concentrations ◽  
Receptor Clusters

I used immunogold labeling and quick-freeze, deep-etch, rotary replication to characterize the membrane skeleton at regions with high concentrations of acetylcholine receptor domains in receptor clusters of cultured rat muscle cells. This membrane skeleton consists of a network of filaments closely applied to the cytoplasmic membrane surface. The filaments are specifically decorated by immunogold labeling with a monoclonal antibody, VIIF7, that recognizes an isoform of beta-spectrin colocalizing with acetylcholine receptors. The filaments are 32 +/- 11 nm in length and three to four filaments (average 3.1-3.3) join at each intersection to form the network. These parameters are nearly identical to those reported previously for the membrane skeleton of erythrocytes. Depending on the amount of platinum coating, filament diameters range from 9 to 11 nm in diameter, and are 1.4 nm larger on average than spectrin filaments of erythrocytes replicated at the same time. Filaments are decorated with gold particles close to one end, consistent with the location of the epitope recognized by the monoclonal antibody. Computer modeling shows that all filament intersections in the membrane skeletal network are equally capable of being labeled by the monoclonal antibody. This pattern of labeling is consistent with a network containing antiparallel homodimers of beta-spectrin.

Sign in / Sign up

Export Citation Format

Share Document