SITE COMPARISONS OF DENTIN COLLAGEN CROSS-LINKS FROM EXTRACTED HUMAN TEETH
SITE COMPARISONS OF DENTIN COLLAGEN CROSS-LINKS FROM EXTRACTED HUMAN TEETH
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DOI：
10.1016/0003-9969(93)90118-6
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发表时间：
1993-07-01
影响因子：
3
通讯作者：
YAMAUCHI, M
中科院分区：
文献类型：
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作者：
RIVERA, EM;YAMAUCHI, M
胶原蛋白中的共价分子间交联为牙本质基质提供了稳定性和拉伸强度。胶原蛋白交联的密度根据同一组织内的部位而变化。这种差异可能是由于不同地点的压力大小和人员流动率不同等因素造成的。目的是量化不同牙齿组中的胶原蛋白交联，以适应功能要求。为此，测量并比较了三个不同部位的人类牙齿的牙本质胶原蛋白中主要交联的类型和含量：门牙、前磨牙-犬齿和臼齿。去除牙骨质和牙髓后，将23颗不同年龄（27-69岁）拔出的牙齿单独粉碎并用EDTA脱矿质。用标准化 (NaBH4)-H-3 还原胶原蛋白，水解，并进行氨基酸和交联分析。每个交联都根据每摩尔胶原蛋白的摩尔数进行量化。结果表明（1）所有牙齿都含有不稳定的、可还原的（脱氢二羟基赖氨酸正亮氨酸和脱氢羟基赖氨酸正亮氨酸）和稳定的、不可还原的（吡啶啉及其赖氨酰类似物）交联，（2）可还原和不可还原交联的含量在门牙中最少，在臼齿中最多。这表明牙本质胶原基质可能具有功能适应性。
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 (NaBH4)-H-3, 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.