Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-6-22
pubmed:abstractText
Acetylcholine receptors (AChR) are associated with several peripheral membrane proteins that are concentrated on the cytoplasmic face of the plasma membrane at the neuromuscular junction, and at aggregates of AChR that form in vitro. We tested the linkage among these proteins by inducing microaggregation of AChR, then determining if a given peripheral membrane protein accumulated with the receptors in microaggregates. In most experiments, we used isolated membrane fragments that are rich in AChR and accessible to antibodies against intracellular antigens. We showed that the 43 kD receptor-associated protein always aggregated with AChR, whether microaggregation was driven by antibodies to the 43 kD protein, or to the receptor itself. Antibodies to the 58 kD receptor-associated protein also always aggregated the 58 kD protein with the receptor. Our results are consistent with a model for AChR-rich membrane in which the 43 kD and 58 kD proteins are both closely associated with the AChR. When we induced microaggregation in intact muscle cells with anti-AChR antibodies, our results were less definitive. The 43 kD receptor-associated protein microaggregated with AChR, but the 58 kD protein was not especially enriched at AChR microaggregates. We discuss the advantages of using isolated AChR-rich membrane fragments to study the association of AChR with peripheral membrane proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2631
pubmed:author
pubmed:issnType
Print
pubmed:volume
138
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-28
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Association of acetylcholine receptors with peripheral membrane proteins: evidence from antibody-induced coaggregation.
pubmed:affiliation
Department of Physiology, University of Maryland School of Medicine, Baltimore 21201.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't