Adsorption of fibrinogen to droplets of liquid hydrophobic phases - Functionality of the bound protein and biological implications

Citation
Gs. Retzinger et al., Adsorption of fibrinogen to droplets of liquid hydrophobic phases - Functionality of the bound protein and biological implications, ART THROM V, 18(12), 1998, pp. 1948-1957
Citations number
50
Categorie Soggetti
Cardiovascular & Hematology Research
Journal title
ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
ISSN journal
10795642 → ACNP
Volume
18
Issue
12
Year of publication
1998
Pages
1948 - 1957
Database
ISI
SICI code
1079-5642(199812)18:12<1948:AOFTDO>2.0.ZU;2-D
Abstract
Fibrinogen adsorbs spontaneously from aqueous media containing that protein to droplets of liquid hydrophobic phases dispersed in those same media. Ex amples of such phases include mineral oils, straight-chain hydrocarbons, an d various plant- and animal-derived oils. Lecithin preexisting on the surfa ce of oil droplets reduces significantly the amount of fibrinogen that can otherwise bind to them. When bound, fibrinogen remains active in the classi c sense of fibrin gelation. As a consequence, oil droplets coated with fibr inogen can participate in a host of biologically important adhesive process es in which the protein would be expected to participate. Certain polyanion s, eg, heparin, pentosan polysulfate, dextran sulfate, and suramin, bind to adsorbed fibrin(ogen) and prevent thrombin-dependent adhesion of fibrinoge n-coated surfaces. Thus, these polyanions can be used to prevent adhesion b etween fibrin(ogen)-coated oil droplets and other fibrin(ogen)-coated surfa ces. Potential practical applications and biological implications of these phenomena are presented and discussed.