Linked Life Data

8205617

Source:http://linkedlifedata.com/resource/pubmed/id/8205617

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-7-11
pubmed:abstractText
Aggregation of acetylcholine receptors (AChRs) on skeletal muscle fibers is thought to be mediated by the basal lamina protein agrin. Structural similarities shared by agrin and laminin suggested that the laminin receptor dystroglycan-alpha, part of a dystrophin-receptor complex, might also bind agrin. We show here that dystroglycan-alpha and dystrophin-related protein (DRP/utrophin) are concentrated within AChR aggregates in cultures of C2 myotubes and that agrin binds specifically to dystroglycan-alpha in in vitro assays. This binding is calcium dependent and is inhibited by monoclonal antibody (MAb) IIH6 against dystroglycan-alpha, heparin, and laminin, but not by fibronectin. In S27 cells, which do not aggregate AChRs spontaneously, agrin and laminin binding to dystroglycan-alpha are dramatically decreased. Moreover, MAb IIH6 significantly inhibits agrin-induced AChR aggregation on C2 cells. We conclude that dystroglycan-alpha is an agrin-binding protein and part of a dystrophin-receptor complex involved in AChR aggregation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
675-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor.
pubmed:affiliation
Centre for Research in Neuroscience, McGill University, Montreal General Hospital Research Institute, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't