Linked Life Data

17957530

Source:http://linkedlifedata.com/resource/pubmed/id/17957530

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-10-24
pubmed:abstractText
The urokinase-type plasminogen activator receptor (uPAR) is a glycosylphosphatidyl inositol-anchored protein that mediates cell adhesion to the extracellular matrix protein vitronectin (VN). We demonstrate here that this cell adhesion process is accompanied by the formation of an adhesion patch characterized by an accumulation of uPAR into areas of direct contact between the cell and the matrix. The adhesion patch requires the glycolipid anchor and develops only on a VN-coated substrate, but not on fibronectin. It consists of detergent-insoluble microdomains that accumulate F-actin and tyrosine-phosphorylated proteins, but not beta(1) integrins. Lack of inhibition of adhesion in the presence of integrin-blocking reagents and adhesion on a VN fragment without the RGD sequence indicated that the adhesion of uPAR-bearing cells on VN could occur independently of integrins. Hence, uPAR-mediated cell adhesion on VN relies on the formation of a unique cellular structure that we have termed "detergent-insoluble adhesion patch" (DIAP).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1541-9061
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
137-55
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Urokinase receptor (CD87) clustering in detergent-insoluble adhesion patches leads to cell adhesion independently of integrins.
pubmed:affiliation
Institute for Biochemistry, Justus-Liebig University, Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't