Interaction of a blood coagulation factor on electrically polarized hydroxyapatite surfaces.
Interaction of a blood coagulation factor on electrically polarized hydroxyapatite surfaces.
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DOI：
10.1002/jbm.b.30701
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发表时间：
2007-07
期刊：
影响因子：
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通讯作者：
Miho Nakamura;K. Niwa;Satoshi Nakamura;Y. Sekijima;K. Yamashita
中科院分区：
文献类型：
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作者：
Miho Nakamura;K. Niwa;Satoshi Nakamura;Y. Sekijima;K. Yamashita
尽管羟基磷灰石（HA）的极化处理显着增强了骨传导性，但其机制尚未完全了解。据报道，血液和组织液中的蛋白质与生物材料的相互作用触发了后来的细胞反应，并在骨传导过程中发挥了重要作用。考虑到这一点，我们揭示了极化 HA 表面与凝血因子、纤维蛋白稳定因子 XIII (FXIII) 的相互作用。根据分配给稳定纤维蛋白的 α-聚合物和 γ-二聚体条带的 SDS-PAGE 检测，即使在无 Ca2+ 的缓冲液中，HA 也会激活 FXIII。检查可能从 HA 表面释放的 Ca2+ 离子是否启动 FXIII 的激活。 ICP分析实验证明，电极化HA上感应的大量负电荷在3分钟的短暂预孵育时间内显着增加了释放的Ca2+浓度。带负电荷的 HA (N-HA) 表面释放的 Ca2+ 离子越多，对 FXIII 的激活就越有效，导致纤维蛋白中的 γ 链带更快消失。与非极化 HA 相比，带正电荷的 HA 中的 Ca2+ 浓度稍低，以几乎相同的速率激活 FXIII。加速活化有助于纤维蛋白支架的稳定。因此，极化 HA 表面感应电荷的极性差异改变了 FXIII 的激活速率。 HA表面与血液蛋白的早期相互作用被认为是植入的N-HA表面附近加速新骨形成的重要过程。
Although the polarization treatment of hydroxyapatite (HA) remarkably enhances the osteoconductivity, the mechanisms have not yet been completely understood. The interaction of proteins in blood and tissue fluids with biomaterials are reportedly triggers for later cellular responses and played a major role in osteoconductive processes. Considering this, we disclosed the interaction of polarized HA surface with a coagulation factor, fibrin stabilizing factor XIII (FXIII). The HA activated FXIII even in Ca2+ free buffer, based on the SDS-PAGE detections of alpha-polymer and gamma-dimer bands assigned to stabilized fibrin. The Ca2+ ions, possibly released from the HA surfaces, were examined whether they initiate the activation of the FXIII. It was experimentally proved by ICP analysis that the induced large negative charges on the electrically polarized HA significantly increased the released Ca2+ concentration for the short pre-incubation time of 3 min. The more Ca2+ ions released from the negatively charged HA (N-HA) surfaces were more effective in the activation of the FXIII, resulting in the rapider disappearance of the gamma-chain bands in fibrin. The slightly lower Ca2+ concentration in the positively charged HA, compared to the nonpolarized HA activated the FXIII at an almost equal rate. The accelerated activation contributed to the stabilization of fibrin scaffold. Therefore, the polarity difference of the induced charges of the polarized HA surface altered the rate of the FXIII activation. The early stage interaction of the HA surfaces with blood proteins was considered to be an essential process of the accelerated new bone formation near implanted N-HA surface.