Linked Life Data

10656323

Source:http://linkedlifedata.com/resource/pubmed/id/10656323

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-3-23
pubmed:abstractText
Adsorbed proteins on biomaterial surfaces determine whether cells adhere, but rheological variables are also critical. Neutrophil adhesion under well-defined radial flow conditions was studied on glass preadsorbed with plasma proteins or plasma protein domain fragments. Fibrinogen, low-molecular-weight kininogen (LK), high-molecular-weight kininogen (HK), cleaved HK (HKa), and recombinant HK domains 3 and 5 (D3 and D5H) were used. The number of adherent cells on the HK and HKa surfaces was less than 10% that found on the fibrinogen absorbed surface. The degree of spreading was minimal and detachment of adherent neutrophils was observed. HK and HKa contain binding sites for both anionic surfaces and neutrophils in the same domain (D5H). When adsorbed to surfaces, HK and HKa did not have the neutrophil binding sites available and therefore exhibited an anti-adhesive effect. Although D5H contains anionic surface binding sites, its small molecular size required a higher number of adsorbed molecules to cover the surface before a significant decrease in cell adhesion was observed. Since LK and D3 do not possess specific anionic surface binding sites, the adsorption of these proteins on glass was very low compared to HK and HKa. Thus, extensive cell adhesion and spreading were observed on the surfaces partially covered with preadsorbed LK and D3.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0142-9612
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
405-14
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
High-molecular-weight kininogen preadsorbed to glass surface markedly reduces neutrophil adhesion.
pubmed:affiliation
Department of Chemical Engineering, University of Delaware, Newark 19716, USA. yung@che.udel.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.