Interactions of fibrinolytic system proteins with lysine-containing surfaces.
J Biomed Mater Res A
; 66(4): 795-801, 2003 Sep 15.
Article
en En
| MEDLINE
| ID: mdl-12926031
Studies on the interactions of tissue plasminogen activator (tPA) and plasminogen with polyurethane surfaces containing epsilon-lysine moieties (epsilon-amino group free) are reported. These surfaces are considered to have the potential to dissolve nascent clots that may be formed on them. For adsorption from both single protein solutions and plasma, the surfaces were found to have a high capacity for tPA as well as plasminogen. A significant fraction of preadsorbed tPA was displaced from the epsilon-lysine surfaces upon contact with plasma. These surfaces, when preadsorbed with tPA and then incubated with plasma, were able to dissolve incipient clots formed around them. However, the clot-dissolving capacity diminished as the time of plasma incubation increased, presumably due to loss of tPA. It was also shown that in plasma, preadsorbed tPA is displaced from these surfaces largely by plasminogen, which thus appears to have a greater binding affinity than tPA for the epsilon-lysine moieties. Finally, it was found that in plasma, the epsilon-lysine surfaces interact with plasminogen in a dynamic manner, and that about 70% of the bound plasminogen is exchanging continuously with plasminogen in the plasma.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Fibrinólisis
/
Lisina
Límite:
Humans
Idioma:
En
Revista:
J Biomed Mater Res A
Asunto de la revista:
ENGENHARIA BIOMEDICA
Año:
2003
Tipo del documento:
Article
País de afiliación:
Canadá
Pais de publicación:
Estados Unidos