Relationship of a dystrophin-associated glycoprotein to junctional acetylcholine receptor clusters in rat skeletal muscle

Guy Smith Bewick, L V Nicholson, C Young, C R Slater

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)503-506
Number of pages4
JournalNeuromuscular Disorders
Volume3
Issue number5-6
DOIs
Publication statusPublished - 1993

Fingerprint

Dystrophin
Utrophin
Cholinergic Receptors
Glycoproteins
Skeletal Muscle
Neuromuscular Junction
Fluorescent Antibody Technique

Keywords

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Cytoskeletal Proteins
  • Dystroglycans
  • Dystrophin
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Muscles
  • Neuromuscular Junction
  • Peptides
  • Rats
  • Receptors, Cholinergic

Cite this

Relationship of a dystrophin-associated glycoprotein to junctional acetylcholine receptor clusters in rat skeletal muscle. / Bewick, Guy Smith; Nicholson, L V; Young, C; Slater, C R.

In: Neuromuscular Disorders, Vol. 3, No. 5-6, 1993, p. 503-506.

Research output: Contribution to journalArticle

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abstract = "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.",
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AB - 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.

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KW - Animals

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KW - Cytoskeletal Proteins

KW - Dystroglycans

KW - Dystrophin

KW - Membrane Glycoproteins

KW - Molecular Sequence Data

KW - Muscles

KW - Neuromuscular Junction

KW - Peptides

KW - Rats

KW - Receptors, Cholinergic

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JO - Neuromuscular Disorders

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