Summary
The deposition of proteins on blood-contacting surfaces is known to be a determining
factor in subsequent thromboembolic events. The composition of the protein layers
and how they change with time are unknown. To generate information relevant to these
questions, the quantities of albumin, fibrinogen and IgG adsorbed on seven surfaces
from human plasma as a function of time were measured using a tracelabeling method.
Materials studied include several segmented polyether-urethanes, glass, siliconized
glass (SG), polystyrene (PS) and polyethylene (PE).
Fibrinogen, surprisingly, was not adsorbed from plasma to any of the hydrophilic surfaces.
On PE and SG adsorption passed through an early maximum (before 2 min) then declined
to near zero. Only on PS was adsorption substantial and constant with time. Albumin
was also not detected on the hydrophilic materials, but was adsorbed substantially
on the hydrophobic surfaces. IgG was detected on all surfaces, although in relatively
low surface concentrations.
These results suggest: 1. that the plasma itself interacts with initially adsorbed
proteins, 2. that the role of fibrinogen adsorption in foreign-surface initiated thrombosis
may need to be reevaluated and 3. that since the major plasma proteins are only minimally
adsorbed, trace proteins may be important in blood-material interactions.
Key words
Blood-material interactions - Artificial surfaces - Plasma protein adsorption
