Linked Life Data

2537118

Source:http://linkedlifedata.com/resource/pubmed/id/2537118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-3-29
pubmed:abstractText
It has been previously shown that fibrinogen (FG) associates specifically with human umbilical vein and bovine aortic endothelial cells (EC) in culture and induces EC migration. In the present study, we have investigated whether the FG-EC interaction is mediated by an Arg-Gly-Asp (RGD) recognition specificity and whether EC membrane proteins related to platelet GPIIb-IIIa are involved. Highly purified radioiodinated human FG, containing no detectable fibronectin, interacted with cultured human and bovine EC in suspension in a time-dependent and specific manner. The binding was inhibited by EDTA. Two polyclonal antibodies to platelet GPIIb-IIIa, which immunoprecipitated a heterodimer molecule from EC, inhibited FG binding to EC. These same antibodies inhibited FG-induced EC migration in a dose-dependent manner as measured in a Boyden chamber. Preabsorption of the antibodies with purified platelet GPIIb-IIIa markedly reduced both inhibitory activities. A series of synthetic RGD-containing peptides inhibited FG binding to EC and FG-induced EC migration. Gly-Arg-Gly-Asp (GRGD) was the most active peptide tested in inhibiting FG binding and EC migration (ID50 of 30 microM), and conservative substitutions in the RGD sequence markedly reduced inhibitory activity (ID50 greater than 1,000 microM). These results indicate that FG binding and EC migration are events mediated by an RGD recognition specificity and that EC surface proteins immunologically related to the GPIIb-IIIa complex on platelets are involved in this recognition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
734-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Fibrinogen-endothelial cell interaction in vitro: a pathway mediated by an Arg-Gly-Asp recognition specificity.
pubmed:affiliation
Institute of Pharmacological Research Mario Negri, Milan, Italy.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't