Linked Life Data

9367446

Source:http://linkedlifedata.com/resource/pubmed/id/9367446

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1997-12-11
pubmed:abstractText
Agrin, a basal lamina-associated proteoglycan, is a crucial nerve-derived organizer of postsynaptic differentiation at the skeletal neuromuscular junction. Because integrins serve as cellular receptors for many basal lamina components, we asked whether agrin interacts with integrins. Agrin-induced aggregation of acetylcholine receptors on cultured myotubes was completely blocked by antibodies to the beta1 integrin subunit and partially blocked by antibodies to the alpha(v) integrin subunit. Agrin-induced clustering was also inhibited by antisense oligonucleotides to alpha(v) and a peptide that blocks the alpha(v) binding site. Non-muscle cells that expressed alpha(v) and beta1 integrin subunits adhered to immobilized agrin, and this adhesion was blocked by anti-alpha(v) and anti-beta1 antibodies. Integrin alpha(v)-negative cells that did not adhere to agrin were rendered adherent by introduction of alpha(v). Together, these results implicate integrins, including alpha(v)beta1, as components or modulators of agrin's signal transduction pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0950-1991
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3909-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Integrins mediate adhesion to agrin and modulate agrin signaling.
pubmed:affiliation
Department of Anatomy and Neurobiology, Washington University School of Medicine, St Louis, MO 63110, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't