AGE RELATED CHANGES IN REDUCIBLE CROSS-LINKS OF COLLAGEN
AGE RELATED CHANGES IN REDUCIBLE CROSS-LINKS OF COLLAGEN
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DOI：
10.1016/0014-5793(71)80338-1
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发表时间：
1971-01-01
期刊：
影响因子：
3.5
通讯作者：
SHIMOKOM.MS
中科院分区：
文献类型：
--
作者：
BAILEY, AJ;SHIMOKOM.MS
人们普遍认为，随着年龄的增长，胶原纤维对外部影响的稳定性稳步提高，例如热变性、膨胀、溶解度和酶（有关评论，请参见[l-3]。所有这些变化都可以通过Verzar最初提出的肽链之间的共价交联数量逐渐增加来解释[4]。最近的研究揭示了有关胶原蛋白中交联性质的大量信息。存在两种类型的交联，即分子内交联原胶原分子 [5] 和完整纤维中分子间的交联 [6-9] 由于发现分子间键对稀释酸和热不稳定，因此考虑到溶解度随着年龄的增长而降低，因此我们现在使用人类、牛和大鼠组织更详细地研究了该机制，以便比较不同生命的动物的过程。跨度。
It is generally agreed that with increasing age the collagen fibre steadily increases in stability to external influences, eg, thermal denaturation, swelling, solubility and enzymes (for reviews see [l-3]. All these changes could be accounted for by a gradual increase in the number of the covalent cross-linkages between the peptide chains as originally proposed by Verzar [4].Recent studies have revealed a great deal about the nature of the cross-links in collagen. Two types of cross-link occur, intramolecular cross-links within the tropocollagen molecule [5] and intermolecular cross-links between molecules in the intact fibre [6-9]. Since intem-rolecular bonds identified were found to be labile to dilute acids and heat then to account for the decrease in solubility with age it was proposed that they were biosynthetic intermediates of the final as yet unknown stable form [IO]. We have now studied the mechanism in more detail using human, bovine and rat tissues in order to compare the process in animals of widely different life spans.