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人牙髓中胶原蛋白的浓度、可提取性及特性

The concentration, extractability and characterization of collagen in human dental pulp.

作者信息

van Amerongen J P, Lemmens I G, Tonino G J

出版信息

Arch Oral Biol. 1983;28(4):339-45. doi: 10.1016/0003-9969(83)90076-6.

Abstract

Premolar and third molar dental pulps were studied. The amount of collagen in the dried pulps was 25.7 per cent in premolars and 31.9 per cent in third molars. These percentages are much higher than those reported for pulps in other species. Significant differences were further found in the collagen content and cell distribution (DNA) of the coronal, middle and apical parts of the pulp. Collagen content was the lowest in the coronal part, while the cell content was the lowest in the middle part. The extractability of collagen in a neutral salt solution or 0.5 M acetic acid was found to be extremely low (less than 1 per cent). Pretreatment of the pulp with hyaluronidase in order to remove proteoglycans had no effect on the solubility. It is concluded that human pulp collagen is highly cross-linked and cannot be considered as immature. Characterization of collagen was performed by methods in which limited pepsin digestion or CNBr cleavage was used. The digests were analysed by means of quantitative electrophoresis which revealed an amount of 42.6 per cent type III of the total collagen. Because of the large differences between dental pulps from man and experimental animals, extreme caution should be exercised in drawing conclusions from data of other species to explain phenomena observed in human teeth.

摘要

对前磨牙和第三磨牙的牙髓进行了研究。干燥牙髓中胶原蛋白的含量在前磨牙中为25.7%,在第三磨牙中为31.9%。这些百分比远高于其他物种牙髓的报道值。在牙髓的冠部、中部和根尖部的胶原蛋白含量和细胞分布(DNA)方面进一步发现了显著差异。冠部的胶原蛋白含量最低,而中部的细胞含量最低。发现在中性盐溶液或0.5M乙酸中胶原蛋白的可提取性极低(低于1%)。用透明质酸酶预处理牙髓以去除蛋白聚糖对溶解度没有影响。结论是人类牙髓胶原蛋白高度交联,不能被视为未成熟的。通过使用有限的胃蛋白酶消化或溴化氰裂解的方法对胶原蛋白进行了表征。通过定量电泳分析消化产物,结果显示总胶原蛋白中III型胶原蛋白含量为42.6%。由于人类牙髓与实验动物牙髓之间存在巨大差异,在从其他物种的数据得出结论以解释人类牙齿中观察到的现象时应极其谨慎。

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