AORTIC-VALVE CUSP MICROSTRUCTURE - THE ROLE OF ELASTIN
AORTIC-VALVE CUSP MICROSTRUCTURE - THE ROLE OF ELASTIN
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DOI：
10.1016/0003-4975(95)00263-k
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发表时间：
1995-08-01
影响因子：
4.6
通讯作者：
VESELY, I
中科院分区：
文献类型：
--
作者：
SCOTT, M;VESELY, I
主动脉瓣尖是三层结构，由不同量的胶原蛋白、弹性蛋白和糖胺聚糖组成。关于这些成分的数量、位置、方向和整体结构，特别是弹性蛋白的数量、位置、方向和整体结构，目前几乎没有定量的信息。我们开发了一种技术，以分离主动脉瓣弹性蛋白在形态完整的状态。在75 ℃的温度下，在0.1 N氢氧化钠溶液中消化整个小叶。扫描电子显微镜和连续切片的计算机三维重建都显示出轮廓分明的蜂窝状或海绵状结构，这表明弹性蛋白形成了一种围绕并连接胶原纤维束的基质。胶原蛋白和弹性蛋白之间的这种关系进一步得到瓣膜尖的自然波浪形构型的支持，允许40%的伸长，即使胶原蛋白原纤维在断裂前通常应变至1%至2%。弹性蛋白可能用于使胶原纤维返回到其未变形状态，保持静止几何形状。
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.