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首页> 外文期刊>Journal of orthopaedic research >Integrin subunits responsible for adhesion of human osteoblast-like cells to biomimetic peptide surfaces.
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Integrin subunits responsible for adhesion of human osteoblast-like cells to biomimetic peptide surfaces.

机译：整联蛋白亚基负责将人成骨细胞样细胞粘附到仿生肽表面。

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We have identified the integrin subunits responsible for the initial adhesion of human osteoblast-like cells to peptide-modified surfaces. Biomimetic peptide surfaces containing homogenous RGD (Arg-Gly-Asp), homogenous FHRRIKA (Phe-His-Arg-Arg-Ile-Lys-Ala), and a mixed ratio of FHRRIKA:RGD (25:75) were used to assess integrin-mediated adhesion. The RGD and FHRRIKA peptides were selected from the cell-binding and putative heparin-binding domains of bone sialoprotein. A panel of monoclonal antibodies against human alpha1, alpha2, alpha3, alpha4, alpha5, beta1, alpha(v), and alpha(v)beta3 was used to identify the subunits most dominant in mediating short-term (10 or 30 minutes) and long-term (4 hours) cell adhesion to the peptide surfaces. Anti-alpha2, anti-beta1, and anti-alpha(v) significantly (p < 0.05) diminished cell attachment to homogenous RGD surfaces following 30 minutes of incubation. After 4 hours of incubation on RGD-grafted surfaces, immunostaining of these integrin subunits revealed discrete localization of the alpha(v) subunit at the periphery of the cell (similar to focal contact points), whereas the alpha2 and beta1 subunits stained very diffusely throughout the cell. A radial-flow apparatus was used to determine the effect of anti-integrin antibodies on strength of cell detachment following 10 minutes of incubation on peptide-grafted surfaces. The strength of detachment from surfaces containing RGD was significantly reduced (p < 0.05) in the presence of anti-alpha2, anti-alpha(v), or anti-beta1 compared with controls (presence of preimmune mouse IgG). None of the antibodies significantly influenced cell attachment to homogenous FHRRIKA-grafted surfaces. These results demonstrate that initial (30 minutes) attachment of human osteoblast-like cells to homogenous RGD surfaces was mediated by the collagen receptor alpha2beta1 and the vitronectin receptor alpha(v)beta3, whereas only the vitronectin receptor governed longer term (longer than 30 minutes) adhesion (localization to focal contacts). The importance of distinct integrins in mediating the attachment of bone cells to RGD-immobilized surfaces indicates a strategy for engineering orthopaedic implants with a built-in surface specificity for cell adhesion.
机译：我们已经鉴定出负责人类成骨细胞样细胞对肽修饰表面的初始粘附的整联蛋白亚基。含有均质RGD（Arg-Gly-Asp），均质FHRRIKA（Phe-His-Arg-Arg-Ile-Lys-Ala）和FHRRIKA：RGD（25:75）混合比例的仿生肽表面用于评估整联蛋白介导的粘附。 RGD和FHRRIKA肽选自骨唾液蛋白的细胞结合域和推定的肝素结合域。使用一组针对人类alpha1，alpha2，alpha3，alpha4，alpha5，beta1，alpha（v）和alpha（v）beta3的单克隆抗体来鉴定在短期（10或30分钟）介导中最主要的亚基和长期（4小时）细胞粘附到肽表面。温育30分钟后，抗alpha2，抗beta1和抗alpha（v）显着（p <0.05）减少了细胞与均质RGD表面的附着。在RGD嫁接的表面上孵育4小时后，这些整联蛋白亚基的免疫染色显示出alpha（v）亚基在细胞外围的离散定位（类似于焦点接触点），而alpha2和beta1亚基在整个过程中都非常分散地染色细胞。在肽移植物表面孵育10分钟后，使用径向流动仪确定抗整联蛋白抗体对细胞分离强度的影响。与对照（存在免疫前小鼠IgG）相比，在存在抗α2，抗α（v）或抗β1的情况下，与含RGD的表面分离的强度显着降低（p <0.05）。没有一种抗体显着影响细胞对同种FHRRIKA移植表面的附着。这些结果表明，人类成骨细胞样细胞最初（30分钟）附着于均质的RGD表面是由胶原受体α2beta1和玻连蛋白受体α（v）beta3介导的，而只有玻连蛋白受体控制更长的时间（超过30分钟） ）附着力（定位到焦点接触）。不同的整联蛋白在介导骨细胞与RGD固定表面的附着中的重要性表明了一种工程化骨科植入物的策略，该植入物具有对细胞粘附的内置表面特异性。

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