Nygren H, Tengvall P, Lundström I
Department of Anatomy and Cell Biology, University of Goteborg, Sweden.
J Biomed Mater Res. 1997 Mar 15;34(4):487-92. doi: 10.1002/(sici)1097-4636(19970315)34:4<487::aid-jbm9>3.0.co;2-g.
The natural titanium oxide (TiO2) layer of commercial sheet titanium was dissolved in hydrofluoric acid. A new oxide layer was grown by oxidation in nitric acid or by annealing at 700 degrees C in air. At this temperature, reaction with nitrogen is unlikely. The purity of the oxidized sheet-titanium surfaces was investigated by Auger spectroscopy. The composition of both surfaces was TiO2 with carbon impurities. The carbon content of the acid-oxidized titanium was 20 +/- 2%, and the carbon content of the heat-oxidized titanium was 14 +/- 2% The initial reactions of the TiO2 surfaces with blood were investigated by short-time exposure to capillary blood and by detection of surface-adsorbed plasma proteins and cells with immunofluorescence. Antibodies specific to fibrinogen, complement factor C1q, prothrombin/thrombin, and platelet membrane antigen were used, and the fluorescence was quantitated by computer-aided image analysis. The results show that serine proteases are the dominating proteins adsorbed onto annealed titanium (C1q = 67 +/- 4.6; pt/t = 97 +/- 0.2; fib = 47 +/- 0.2). The adsorption of serine proteases was lower and the amount of fibrinogen was higher on the acid-oxidized surface (C1q = 46.3 +/- 2.6; pt/t = 25 +/- 2.9; fib = 64 +/- 0.7). Platelets adhered and spread on the annealed titanium surface within 5 sec of blood-material contact. The number of adhering platelets was higher on the acid-oxidized surface.
