Linked Life Data

3294235

Source:http://linkedlifedata.com/resource/pubmed/id/3294235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-9-2
pubmed:abstractText
Using a previously described model system for the incorporation of plasma fibronectin into the extracellular matrix (McKeown-Longo, P.J. and Mosher, D.F., 1985. J. Cell Biol., 100:364-374), we compared the binding of cell-derived and plasma-derived fibronectins to human fibroblast cell layers. Binding was measured in time course experiments using metabolically labeled cell-derived, iodinated cell-derived, and iodinated plasma-derived fibronectins. The kinetics of matrix assembly of cell- and plasma-derived fibronectins were the same. Competitive binding curves using intact fibronectin or the 70-kD amino-terminal fragment of fibronectin suggested that cell surface binding sites have equal affinity for cell- and plasma-derived fibronectins. Iodinated fibronectins did not bind to isolated matrices containing collagen type I, fibronectin, and thrombospondin. These results suggest that fibroblasts do not distinguish between cell-derived and plasma-derived fibronectins when assembling exogenous fibronectin into extracellular matrix.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9541
pubmed:author
pubmed:issnType
Print
pubmed:volume
135
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
459-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Extracellular matrix assembly of cell-derived and plasma-derived fibronectins by substrate-attached fibroblasts.
pubmed:affiliation
Department of Physiology, Albany Medical College, New York 12208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.