Laboratoire de Physique des Polymères, Institut Carnot, CIRIMAT UMR 5085, Université Paul Sabatier, 31062 Toulouse cedex 9, France.
J Biomed Mater Res A. 2010 Nov;95(2):611-9. doi: 10.1002/jbm.a.32835.
Abdominal aortic aneurysms (AAA) are characterized by structural alterations of the aortic wall resulting from the degradation of elastic fibres and an increase of collagen/elastin ratio. In this study we investigated the chain dynamics of AAA tissues by two techniques generally used for the characterization of polymers, Differential scanning calorimetry (DSC) and thermally stimulated currents (TSC), and we correlated the obtained data with biochemical analyses. The thermal denaturation of collagen observed by DSC allowed us to evaluate the thermal stability of the triple helix domain: notable modifications were evidenced between collagen from control tissue and collagen from AAA, particularly concerning the thermal denaturation. The dielectric analysis of pathologic aortic walls by TSC revealed a relevant change of collagen mobility in AAA, with the occurrence of a specific mode of relaxation between -60 and -40°C. Biochemical, thermal, and dielectric results are compatible with increase of new collagen deposition and/or impairment of the collagen phase stability in the extracellular matrix of AAAs.
腹主动脉瘤(AAA)的特征是主动脉壁的结构改变,这是由于弹性纤维的降解和胶原蛋白/弹性蛋白比例的增加所致。在这项研究中,我们通过两种通常用于聚合物特性描述的技术——差示扫描量热法(DSC)和热刺激电流法(TSC),研究了 AAA 组织的链动力学,并将获得的数据与生化分析相关联。DSC 观察到的胶原蛋白热变性使我们能够评估三螺旋结构域的热稳定性:在来自对照组织的胶原蛋白和来自 AAA 的胶原蛋白之间,观察到了明显的变化,特别是在热变性方面。TSC 对病变主动脉壁的介电分析显示 AAA 中胶原蛋白的迁移率发生了显著变化,在-60 至-40°C 之间出现了一种特定的松弛模式。生化、热和介电结果与细胞外基质中胶原蛋白的新沉积增加和/或胶原蛋白相稳定性受损是一致的。