Blood plasma contact activation on silicon, titanium and aluminium.
In the present work, blood plasma protein deposition to spontaneously air oxidized silicon, titanium and aluminium was re-investigated in vitro. Immunological- and null ellipsometry methods were used to detect and quantitate adsorbed proteins, RIA methods to study the retention of preadsorbed 125I-HSA upon exposure to buffer or blood plasma, and kallikrein-specific colorimetric substrate S-2302 to follow the surface generation of kallikrein. The results show that the contact activation of coagulation and complement systems are connected on Si and Ti, but not on Al, via coagulation factor XII. Preadsorbed 125I-HSA was most readily displaced on silicon, followed by titanium and aluminium. The surfaces displayed different antibody binding patterns after short and long-time exposures to plasma. Titanium and silicon bound anti-HMWK after 1 min in plasma, but aluminium did not. When the plasma incubation time was prolonged up to 2h the anti-HMWK binding disappeared totally on titanium and decreased on silicon. During the same time period, anti-C3c binding increased to the three types of surfaces. Also, the anti-C3c binding onto Si and Ti, but not Al, disappeared after incubation in Factor XII deficient plasma or when a specific coagulation factor XII (Factor XII) inhibitor, corn trypsin inhibitor (CTI) was added to normal plasma. The surface contacted plasmas cleaved the kallikrein-specific reagent S-2302 both after single surface contact, and after reincubation of surfaces in fresh plasma. The results show that C3b and Factor XIIa and their degradation products were retained at the surfaces.
Arvidsson
Sara
S
Division of Applied Physics, Department of Physics, Chemistry and Biology, Linköping University, SE-581 83 Linköping, Sweden.
Askendal
Agneta
A
Tengvall
Pentti
P
D000327:Adsorption; D000535:Aluminum; D001672:Biocompatible Materials; D001777:Blood Coagulation; D001798:Blood Proteins / Q000378:metabolism; D002021:Buffers; D003124:Colorimetry; D003167:Complement Activation; D006493:Heparin; D006801:Humans; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D007610:Kallikreins / Q000096:biosynthesis; D008422:Materials Testing; D010949:Plasma / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D012825:Silicon; D013499:Surface Properties; D014025:Titanium
D001672:Biocompatible Materials; D001798:Blood Proteins; D002021:Buffers; D007457:Iodine Radioisotopes; D012709:Serum Albumin; D006493:Heparin; D000535:Aluminum; D014025:Titanium; D007610:Kallikreins; D012825:Silicon