Electron microscopic detection of salivary α-amylase in the pellicle formed in situ
Electron microscopic detection of salivary α-amylase in the pellicle formed in situ
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DOI：
10.1111/j.1600-0722.2004.00168.x
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发表时间：
2004-12-01
影响因子：
1.9
通讯作者：
Hannig, M
中科院分区：
文献类型：
--
作者：
Deimling, D;Breschi, L;Hannig, M
免疫学和生物化学分析表明，α-淀粉酶是获得性表膜的重要组成部分。吸附后，这种酶可能作为细菌粘附的受体。然而，数据表明，淀粉酶结合到表膜表面在体内，从而可用于粘附细菌是罕见的。因此，本研究的重点是α-淀粉酶内形成的表膜原位，使用金免疫标记电子显微镜技术。在6名受试者中，通过口腔内暴露釉质样本30和120分钟形成膜。透射电子显微镜观察结果表明，淀粉酶随机分布在表膜层中，没有任何优先定位在表膜内。因此，唾液α-淀粉酶可能被认为是一个重要的结构组成部分，甚至参与了早期阶段的薄膜形成。场发射透镜扫描电子显微镜的结果提供了证据，酶位于表膜表面。因此，α-淀粉酶可能是细菌在体内粘附于表膜的受体。
Immunological and biochemical analyses have shown that alpha-amylase is an essential component of the acquired pellicle. After adsorption, this enzyme might act as a receptor for bacterial adherence. However, data indicating that amylase is bound to the pellicle surface in vivo and thus available for adhering bacteria are rare. Therefore, the present study focused on alpha-amylase within the pellicle formed in situ, using gold-immunolabeling electron microscopic techniques. Pellicles were formed by intra-oral exposure of enamel specimens for 30 and 120 min in six subjects. The results obtained by transmission electron microscopy indicate that amylase was randomly distributed in the pellicle layer without any preferential localization within the pellicle. Thus, salivary alpha-amylase might be considered as an important structural component that is even involved in the early stages of pellicle formation. The findings of field emission in-lens scanning electron microscopy provided evidence that the enzyme is located on the pellicle surface. It could be concluded that alpha-amylase might act as a receptor for bacterial adherence to the pellicle in vivo.