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

doi:10.1016/0960-8966(93)90105-S

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

Medical Sciences

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	503-506
Number of pages	4
Journal	Neuromuscular Disorders
Volume	3
Issue number	5-6
DOIs	https://doi.org/10.1016/0960-8966(93)90105-S
Publication status	Published - 1993

Keywords

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

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10.1016/0960-8966(93)90105-S

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@article{f1f95435408b48fa8427d241b92f3d4d,

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

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.",

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

author = "Bewick, {Guy Smith} and Nicholson, {L V} and C Young and Slater, {C R}",

year = "1993",

doi = "10.1016/0960-8966(93)90105-S",

language = "English",

volume = "3",

pages = "503--506",

journal = "Neuromuscular Disorders",

issn = "0960-8966",

publisher = "PERGAMON-ELSEVIER SCIENCE LTD",

number = "5-6",

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TY - JOUR

T1 - Relationship of a dystrophin-associated glycoprotein to junctional acetylcholine receptor clusters in rat skeletal muscle

AU - Bewick, Guy Smith

AU - Nicholson, L V

AU - Young, C

AU - Slater, C R

PY - 1993

Y1 - 1993

N2 - 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.

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.

KW - Amino Acid Sequence

KW - Animals

KW - Antibodies, Monoclonal

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

U2 - 10.1016/0960-8966(93)90105-S

DO - 10.1016/0960-8966(93)90105-S

M3 - Article

C2 - 8186701

VL - 3

SP - 503

EP - 506

JO - Neuromuscular Disorders

JF - Neuromuscular Disorders

SN - 0960-8966

IS - 5-6

ER -

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

Abstract

Keywords

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