IMMUNOCYTOCHEMICAL AND IMMUNOCHEMICAL DETECTION OF A 32 KDA NONAMELOGENIN AND RELATED PROTEINS IN PORCINE TOOTH GERMS
IMMUNOCYTOCHEMICAL AND IMMUNOCHEMICAL DETECTION OF A 32 KDA NONAMELOGENIN AND RELATED PROTEINS IN PORCINE TOOTH GERMS
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DOI：
10.1679/aohc.54.527
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发表时间：
1991-12-01
影响因子：
--
通讯作者：
SHIMIZU, M
中科院分区：
文献类型：
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作者：
UCHIDA, T;TANABE, T;SHIMIZU, M
采用免疫化学和免疫细胞化学方法，对猪牙胚进行了免疫细胞化学和免疫细胞化学研究。在免疫化学制剂中，这些抗体对许多不同分子量的蛋白起反应，特别是对140 kDa、89 kDa、56 kDa、45 kDa和32 kDa蛋白。对釉质层的分析表明，在新形成的釉质中发现的140 kDa和/或89 kDa蛋白是成釉细胞分泌的亲本蛋白，它们被降解产生32 kDa和其他与进展矿化相关的低分子量蛋白。在免疫组化制备中，牙本质钙化小球周围的无定形致密物质或细原纤维在分化阶段初步检测到免疫反应性，而点状物质则无免疫反应性。这种无定形的致密物质似乎形成了一层连续的初始牙釉质。在基质形成阶段，未成熟牙釉质的免疫反应性在假定的分泌面下方是强烈的。从釉质基质表面到约100 μ m深度，棱柱鞘的免疫反应性弱于釉质棱柱，形成反向的蜂窝状图案。在深度大于100 μ m的牙釉质基质中，免疫反应性弱且分布均匀。分泌性成釉细胞的高尔基体和分泌颗粒表现出免疫反应性。这些结果表明，32 kDa非淀粉原蛋白可能的亲本蛋白，即140 kDa和/或89 kDa蛋白，在牙釉质基质的钙化中起重要作用。
Porcine tooth germ was investigated immunochemically and immunocytochemically using antibodies against a synthetic N-terminal peptide fragment from a 32 kDa nonamelogenin found in the inner (old) secretory enamel. In immunochemical preparations, these antibodies reacted to many proteins of differing molecular weights, especially to 140 kDa, 89 kDa, 56 kDa, 45 kDa, and 32 kDa proteins. Analysis of the layers of enamel suggested that the 140 kDa and/or 89 kDa proteins, both of which were found in newly formed enamel, were the parental proteins secreted by the ameloblasts, and that they were degraded to produce 32 kDa and other low molecular-weight proteins associated with progressive mineralization. In immunohistochemical preparation, immunoreactivity at the differentiation stage was detected initially over the amorphous dense material or fine fibrils around calcified globules in predentin, while the stippled material was devoid of immunoreactivity. The amorphous dense material seemed to give rise to a continuous layer of initial enamel. At the matrix formation stage, the immunoreactivity of immature enamel just beneath the putative secretory face of the Tomes' processes was intense. From the surface of the enamel matrix to a depth of about 100-mu-m, immunoreactivity of prism sheaths was weaker than that of enamel prisms, producing a reverse honeycomb pattern. In the enamel matrix deeper than 100-mu-m, immunoreactivity was weak and homogeneously distributed. The Golgi apparatus and secretory granules of the secretory ameloblasts showed immunoreactivity. These results suggest that the likely parent proteins of the 32 kDa nonamelogenin protein, i.e., the 140 kDa and/or 89 kDa proteins, play a significant role in the calcification of the enamel matrix.