Rivera E M, Yamauchi M
Department of Endodontics, University of Iowa, College of Dentistry, Iowa City 52242-1382.
Arch Oral Biol. 1993 Jul;38(7):541-6. doi: 10.1016/0003-9969(93)90118-6.
Covalent intermolecular cross-links in collagen provide the dentine matrix with stability and tensile strength. The density of collagen cross-links varies depending on the site within the same tissue. This variation is probably due to factors such as the different amounts of stress and different turnover rates at the respective sites. The aim was to quantify the collagen cross-links in different tooth groups as an adaptation to functional requirements. For this purpose, the types and content of major cross-links in dentine collagen of human teeth from three different sites were measured and compared: incisors, premolar-canines and molars. After removal of cementum and pulp, 23 extracted teeth at different ages (27-69 yr) were individually pulverized and demineralized with EDTA. Collagen was reduced with standardized NaB3H4, hydrolysed, and subjected to amino acid and cross-link analyses. Each cross-link was quantified on the basis of mole per mole of collagen. The results indicated: (1) all teeth contained labile, reducible (dehydro-dihydroxylysinonorleucine and dehydro-hydroxylysinonorleucine) and stable, non-reducible (pyridinoline and its lysyl analogue) cross-links, and (2) the content of both reducible and non-reducible cross-links was least in incisors and greatest in molars. This suggests that dentine collagen matrix maybe functionally adaptive.
胶原蛋白中的共价分子间交联为牙本质基质提供稳定性和抗张强度。同一组织内不同部位的胶原蛋白交联密度各不相同。这种差异可能是由于各部位应力大小不同和周转率不同等因素所致。本研究旨在量化不同牙组中的胶原蛋白交联情况，以适应功能需求。为此，对来自三个不同部位的人牙牙本质胶原蛋白中的主要交联类型和含量进行了测量和比较：切牙、前磨牙 - 尖牙和磨牙。去除牙骨质和牙髓后，将23颗不同年龄（27 - 69岁）的离体牙分别粉碎，并用乙二胺四乙酸（EDTA）脱矿。胶原蛋白用标准化的硼氢化钠（NaB3H4）还原、水解，然后进行氨基酸和交联分析。每种交联均基于每摩尔胶原蛋白的摩尔数进行量化。结果表明：（1）所有牙齿均含有不稳定的、可还原的（脱氢 - 二羟基赖氨酰正亮氨酸和脱氢 - 羟基赖氨酰正亮氨酸）以及稳定的、不可还原的（吡啶啉及其赖氨酰类似物）交联；（2）可还原交联和不可还原交联的含量在切牙中最少，在磨牙中最多。这表明牙本质胶原蛋白基质可能具有功能适应性。
