Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1985-3-14
pubmed:abstractText
Binding curves for the adsorption of plasma fibronectin, alpha-1-antitrypsin, alpha-2-macroglobulin, ceruloplasmin, transferrin and bovine serum albumin to plain and to hydroxylated polystyrene surfaces were measured. These curves were correlated with the adhesion of BHK cells and leucocytes to these adsorbed protein surfaces in protein-free culture media. Hydroxylated polystyrene adsorbed less of alpha-1-antitrypsin, alpha-2-macroglobulin and albumin than the plain polystyrene. On the other hand the hydroxylated surfaces bound more fibronectin than the plain polystyrene surfaces. Hydroxylated polystyrene surfaces were also more adhesive for both BHK cells and leucocytes than plain polystyrene: a result confirming earlier work. The competition of fibronectin for adsorption to plain polystyrene with alpha-1-antitrypsin, alpha-2-macroglobulin and ceruloplasmin was measured and correlated with effects on cell adhesion. The results suggest that the low adhesiveness of BHK cells and leucocytes on plain polystyrene in sera-containing media is due both to the low binding of fibronectin and to the binding of serum albumin, alpha-1-antitrypsin and alpha-2-macroglobulin. The relative unimportance of fibronectin in adhesion to these surfaces is shown by the finding that cell attachment will not occur to polystyrene surfaces that have bound high levels of the antiadhesive proteins in the presence of fibronectin, even though attachment will occur in the absence of fibronectin provided that the antiadhesive proteins are lacking.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-35
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The competitive effects of serum proteins on cell adhesion.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't