Deligianni D D, Katsala N, Ladas S, Sotiropoulou D, Amedee J, Missirlis Y F
Department of Mechanical Engineering and Aeronautics, Universihy of Patras, Rion, Greece.
Biomaterials. 2001 Jun;22(11):1241-51. doi: 10.1016/s0142-9612(00)00274-x.
The effect of surface roughness of the titanium alloy Ti-6Al-4V (Ti alloy) on the short- and long-term response of human bone marrow cells in vitro and on protein adsorption was investigated. Three different values in a narrow range of surface roughness were used for the substrata (R(alpha): 0.320, 0.490 and 0.874 microm). Cell attachment, cell proliferation and differentiation (alkaline phosphatase specific activity) were determined past various incubation periods. The protein adsorption of bovine serum albumin and fibronectin, from single protein solutions, on rough and smooth Ti alloy surfaces was examined with two methods, X-ray photoelectron spectroscopy (XPS) and radiolabeling. Cell attachment and proliferation were surface roughness sensitive and increased as the roughness of Ti alloy increased. No statistically significant difference was observed in the expression of ALP activity on all three Ti alloy surfaces and culture plastic. Both methods, XPS and protein radiolabeling, showed that human serum albumin was adsorbed preferentially onto the smooth substratum. XPS technique showed that the rough substratum bound a higher amount of total protein (from culture medium supplied with 10% serum) and fibronectin (10-fold) than did the smooth one. The cell attachment may be explained by the differential adsorption of the two proteins onto smooth and rough Ti alloy surfaces.
研究了钛合金Ti-6Al-4V（Ti合金）表面粗糙度对人骨髓细胞体外短期和长期反应以及蛋白质吸附的影响。在较窄的表面粗糙度范围内使用了三个不同的值作为基质（R(α)：0.320、0.490和0.874微米）。在不同的孵育时间后测定细胞附着、细胞增殖和分化（碱性磷酸酶比活性）。采用X射线光电子能谱（XPS）和放射性标记两种方法，检测了牛血清白蛋白和纤连蛋白在粗糙和光滑Ti合金表面从单一蛋白质溶液中的蛋白质吸附情况。细胞附着和增殖对表面粗糙度敏感，且随着Ti合金粗糙度的增加而增加。在所有三种Ti合金表面和培养塑料上，碱性磷酸酶活性的表达未观察到统计学上的显著差异。XPS和蛋白质放射性标记这两种方法均表明，人血清白蛋白优先吸附在光滑基质上。XPS技术表明，粗糙基质比光滑基质结合了更高量的总蛋白（来自添加10%血清的培养基）和纤连蛋白（高出10倍）。细胞附着可能是由于这两种蛋白质在光滑和粗糙Ti合金表面的差异吸附所致。
