Scott M, Vesely I
John P. Robarts Research Institute, University of Western Ontario, London, Canada.
Ann Thorac Surg. 1995 Aug;60(2 Suppl):S391-4. doi: 10.1016/0003-4975(95)00263-k.
The aortic valve cusp is a three-layered structure, composed of differing amounts of collagen, elastin, and glycosaminoglycans. Little quantitative information is presently available on the amount, location, orientation, and overall structure of these constituents, particularly of elastin. We developed a technique to isolate aortic valve elastin in a morphologically intact state. Whole leaflets were digested in 0.1 N sodium hydroxide solution at a temperature of 75 degrees C. Both scanning electron microscopy and computerized three-dimensional reconstructions of serial sections showed a well-defined honeycomb or spongelike structure, suggesting that elastin forms a matrix that surrounds and links the collagen fiber bundles. This relationship between collagen and elastin is further supported by the naturally wavy configuration of the valve cusps, permitting elongations of 40%, even though collagen fibrils typically strain to 1% to 2% before fracture. Elastin likely acts to return collagen fibers back to their undeformed state, maintaining rest geometry.
主动脉瓣叶是一种三层结构,由不同数量的胶原蛋白、弹性蛋白和糖胺聚糖组成。目前关于这些成分的数量、位置、取向和整体结构,尤其是弹性蛋白的定量信息很少。我们开发了一种技术,以形态完整的状态分离主动脉瓣弹性蛋白。将整个瓣叶在75摄氏度的0.1N氢氧化钠溶液中消化。扫描电子显微镜和连续切片的计算机三维重建均显示出明确的蜂窝状或海绵状结构,表明弹性蛋白形成了围绕并连接胶原纤维束的基质。瓣膜叶自然的波浪状形态进一步支持了胶原蛋白与弹性蛋白之间的这种关系,即使胶原纤维通常在断裂前应变至1%至2%,瓣膜叶仍可伸长40%。弹性蛋白可能起到使胶原纤维恢复到未变形状态的作用,维持静止时的几何形状。