Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-12-15
pubmed:abstractText
Acetylcholine receptor clusters of cultured rat myotubes are examined by thin-section EM and by rapid-freeze, deep-etch, rotary-replication technique to observe the cortical cytoskeleton; AChR are localized by binding of fluorescent toxin. Cluster membrane is composed of three types of membrane domain which interdigitate with each other. The AChR domain is rich in the integral membrane receptor, lies further from the substrate than the other two, and is overlain by an extensive irregular meshwork of anastomosing filaments containing actin and a beta isoform of spectrin. Contact domains resemble focal contacts of fibroblasts, in that membrane lying close to the substrate is overlain by bundles of actin filaments running parallel to the membrane; some finer filaments link the parallel filaments to each other and to the membrane. Coated-membrane domains are overlain by polymerized clathrin and, like contact domains, lie close to the substrate and have external connections to it; these domains are associated with coated vesicles, but not with intracellular filaments. The three domains have few if any connections to each other, and occupy mutually exclusive territories in the cluster.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0738-0658
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
96-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Membrane domains of AChR clusters of cultured rat myotubes revealed by rapid-freeze, deep-etch, rotary-replication.
pubmed:affiliation
Department of Anatomy, 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