Vesely I
Department of Biomedical Engineering, The Cleveland Clinic Foundation, Lerner Research Institute, OH 44195, USA.
J Biomech. 1998 Feb;31(2):115-23. doi: 10.1016/s0021-9290(97)00122-x.
Recent morphologic observations of elastin structures in aortic valves suggest that elastin is mechanically coupled to collagen. Since the mechanical stiffness of elastin is considerably lower than that of collagen, and aortic valves contain relatively little elastin, the mechanical importance of elastin in heart valve function is not clear. We have hypothesized that elastin acts to return the collagen fiber structure back to a resting configuration between loading cycles. The objectives of this research were therefore to elucidate the mechanical relationship between elastin and collagen structures within the aortic valve. To isolate elastin in a morphologically intact state, whole porcine aortic valve leaflets were digested in 0.1 N sodium hydroxide solution (NaOH) at a temperature of 75 degrees C for 45 min. Elastin structures from the fibrosa and ventricularis were tested mechanically, and their loading curves compared to those of the original leaflet layers and to whole cusps. The elastin structures generated very low forces, having an elastic modulus only 0.05% that of the whole tissue. The contribution of elastin to tissue mechanics was significant at low strains and differed between the fibrosa and the ventricularis. Elastin tended to dominate the distensibility curves of the radial ventricularis, but participated very little in the fibrosa. The low but significant tensions produced by the elastin structures of the aortic valve, together with previously observed elastin morphology as well as the measurable preload of elastin, suggest that the purpose of elastin in the aortic valve leaflet is to maintain a specific collagen fiber configuration and return the fibers to this state, once external forces have been released.
最近对主动脉瓣中弹性蛋白结构的形态学观察表明,弹性蛋白与胶原蛋白存在机械耦合。由于弹性蛋白的机械刚度远低于胶原蛋白,且主动脉瓣中弹性蛋白含量相对较少,因此弹性蛋白在心脏瓣膜功能中的机械重要性尚不清楚。我们推测,弹性蛋白的作用是使胶原纤维结构在加载周期之间恢复到静止状态。因此,本研究的目的是阐明主动脉瓣内弹性蛋白与胶原蛋白结构之间的力学关系。为了分离出形态完整的弹性蛋白,将完整的猪主动脉瓣小叶在75摄氏度的0.1N氢氧化钠溶液(NaOH)中消化45分钟。对纤维层和心室层的弹性蛋白结构进行力学测试,并将其加载曲线与原始小叶层和整个瓣尖的加载曲线进行比较。弹性蛋白结构产生的力非常低,其弹性模量仅为整个组织的0.05%。在低应变时,弹性蛋白对组织力学的贡献显著,且在纤维层和心室层之间存在差异。弹性蛋白往往主导着心室层径向的扩张曲线,但在纤维层中参与度很低。主动脉瓣弹性蛋白结构产生的低但显著的张力,连同先前观察到的弹性蛋白形态以及可测量的弹性蛋白预负荷,表明主动脉瓣小叶中弹性蛋白的作用是维持特定的胶原纤维构型,并在外部力释放后使纤维恢复到该状态。