Scheck M, Siegel R C, Parker J, Chang Y H, Fu J C
J Anat. 1979 Oct;129(Pt 3):645-57.
Aneurysmal aortic tissue and the mitral valve of a patient with Marfan's syndrome were examined. Biochemical analysis of the tissue showed a qualitative and quantitative defect in alpha 2 chain production of Type I collagen. On polyacrylamide gel electrophoresis of the aortic extract, two separate bands in the alpha 2 region and an increase of the alpha 1 to alpha 2 ratio were found. Examination by electron microscopy revealed elastic fibre degeneration, helical collagen fibres, and metabolically active modified smooth muscle cells. The formation of helical collagen fibres is attributed to a defect in the development of chains and cross-links of collagen precursors produced by the hypertrophic smooth muscle cells. Elastic fibre disintegration is believed to be due to a lack of support by Type I collagen fibres, which have decreased tensile strength. A scheme for the pathogenesis of aortic aneurysm and other connective tissue abnormalities in Marfan's syndrome is proposed as follows. Type I collagen fibres have decreased tensile strength because of a defect in the alpha 2 chain biosynthesis and decreased cross-linking. Over many years the wall of the ascending aorta is subjected to cyclic stresses and it dilates. Elastic fibres disintegrate. The attempt at repair by metabolically activated modified smooth muscle cells is abortive, and rupture is likely to occur.
对一名马凡氏综合征患者的动脉瘤性主动脉组织和二尖瓣进行了检查。组织的生化分析显示I型胶原蛋白α2链产生存在定性和定量缺陷。在主动脉提取物的聚丙烯酰胺凝胶电泳中,在α2区域发现了两条分开的条带,且α1与α2的比例增加。电子显微镜检查显示弹性纤维变性、螺旋状胶原纤维以及代谢活跃的修饰平滑肌细胞。螺旋状胶原纤维的形成归因于肥大平滑肌细胞产生的胶原前体链和交联发育缺陷。弹性纤维解体被认为是由于I型胶原纤维的支撑不足,其抗张强度降低。提出了马凡氏综合征主动脉瘤及其他结缔组织异常发病机制的方案如下。由于α2链生物合成缺陷和交联减少,I型胶原纤维的抗张强度降低。多年来,升主动脉壁承受周期性应力并扩张。弹性纤维解体。代谢激活的修饰平滑肌细胞进行修复的尝试失败,可能会发生破裂。