Effect of Glycation on Interlamellar Bonding of Arterial Elastin.
Effect of Glycation on Interlamellar Bonding of Arterial Elastin.
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DOI：
10.1007/s11340-020-00644-y
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发表时间：
2021-01
影响因子：
2.4
通讯作者：
Zhang Y
中科院分区：
文献类型：
--
作者：
Wang R;Yu X;Gkousioudi A;Zhang Y
动脉壁中的层间结合常常受到心血管疾病的损害。然而，最近几项全国性和医院研究一致报告糖尿病患者胸主动脉夹层风险降低。作为动脉壁的主要结构成分之一，弹性蛋白在提供其层间结构完整性方面起着重要作用。本研究的目的是研究糖化对动脉弹性蛋白层间结合特性的影响。从猪胸降主动脉分离纯化的弹性蛋白网络，并在37 °C下在2M葡萄糖溶液中孵育7、14或21天。剥离和直接拉伸试验进行了解与糖化效应的弹性蛋白网络的层间层分离性能提供补充信息。剥离试验采用内聚区模型（CZM）进行模拟。多光子成像被用来可视化的层间弹性蛋白纤维的样品进行剥离和直接张力。剥离和直接拉伸试验表明，随着葡萄糖处理时间的延长，层间能量释放速率和强度均增加。在损伤开始时的牵引力估计CZM同意与直接拉伸试验的层间强度测量。糖化也被发现增加动脉弹性蛋白的层间破坏应变。多光子成像证实了弹性蛋白纤维的放射状运行的贡献，以抵抗夹层。非酶糖基化降低动脉弹性蛋白的夹层倾向。这项研究还表明，CZM有效地描述了动脉弹性蛋白的层间结合特性。
Interlamellar bonding in the arterial wall is often compromised by cardiovascular diseases. However, several recent nationwide and hospital-based studies have uniformly reported reduced risk of thoracic aortic dissection in patients with diabetes. As one of the primary structural constituents in the arterial wall, elastin plays an important role in providing its interlamellar structural integrity. The purpose of this study is to examine the effects of glycation on the interlamellar bonding properties of arterial elastin. Purified elastin network was isolated from porcine descending thoracic aorta and incubated in 2 M glucose solution for 7, 14 or 21 days at 37 °C. Peeling and direct tension tests were performed to provide complimentary information on understanding the interlamellar layer separation properties of elastin network with glycation effect. Peeling tests were simulated using a cohesive zone model (CZM). Multiphoton imaging was used to visualize the interlamellar elastin fibers in samples subjected to peeling and direct tension. Peeling and direct tension tests show that interlamellar energy release rate and strength both increases with the duration of glucose treatment. The traction at damage initiation estimated for the CZM agrees well with the interlamellar strength measurements from direct tension tests. Glycation was also found to increase the interlamellar failure strain of arterial elastin. Multiphoton imaging confirmed the contribution of radially running elastin fibers to resisting dissection. Nonenzymatic glycation reduces the propensity of arterial elastin to dissection. This study also suggests that the CZM effectively describes the interlamellar bonding properties of arterial elastin.
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影响因子：
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作者：
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