Linked Life Data

3519254

Source:http://linkedlifedata.com/resource/pubmed/id/3519254

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-7-24
pubmed:abstractText
In order to provide evidence for an association of cell surface laminin with the cytoskeleton, we have examined the detergent extractability of cell surface laminin on murine fibrosarcoma cells. We utilized indirect immunofluorescence with affinity-purified anti-laminin antibodies to determine the distribution, mobility and detergent extractability of laminin bound to the cell surface. We demonstrate that antibody induces clustering of cell surface laminin rendering it resistant to detergent extraction. At low receptor occupancy, approx. 80% of cell surface laminin is detergent-extractable. If cell surface laminin is induced to cluster with anti-laminin antibody, IB4 isolectin from Bandeiraea simplicifolia or by high receptor occupancy, then it is rendered resistant to detergent extraction. This process is temperature-sensitive and inhibited by cytochalasin D (CD). On the basis of these findings, we propose a model in which laminin anchored in the basement membrane in vivo affects the cellular cytoskeleton by facilitating the clustering of cell surface transmembrane laminin receptors which are able to interact with cellular actin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
165
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-16
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Clustering of cell surface laminin enhances its association with the cytoskeleton.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't