Relationship of a dystrophin-associated glycoprotein to junctional acetylcholine receptor clusters in rat skeletal muscle
Copyright policy )Relationship of a dystrophin-associated glycoprotein to junctional acetylcholine receptor clusters in rat skeletal muscle
The relationship of a member of the transmembrane dystrophin-associated glycoprotein (DAG) complex to acetylcholine receptors (AChRs) was investigated using immunofluorescence techniques at rat neuromuscular junctions (NMJs) viewed en face. These results were compared with those from a similar previous study of dystrophin and an autosomal homologue (utrophin or dystrophin-related protein, DRP) (Bewick et al. Neuro Report 1992; 3: 857-860). The region of highest 43 K DAG (43DAG) labelling projected beyond the AChRs by approximately 0.3 microns, as does that for dystrophin. By contrast DRP labelling precisely co-localizes with the AChRs. These results suggest that at the NMJ, the region of high 43DAG concentration encompasses the area of highest intensity labelling for both DRP and dystrophin.
- Newcastle University United Kingdom
Membrane Glycoproteins, Muscles, Molecular Sequence Data, Neuromuscular Junction, Antibodies, Monoclonal, Rats, Dystrophin, Cytoskeletal Proteins, Animals, Receptors, Cholinergic, Amino Acid Sequence, Dystroglycans, Peptides
Membrane Glycoproteins, Muscles, Molecular Sequence Data, Neuromuscular Junction, Antibodies, Monoclonal, Rats, Dystrophin, Cytoskeletal Proteins, Animals, Receptors, Cholinergic, Amino Acid Sequence, Dystroglycans, Peptides
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