Yoshikane H, Honda M, Goto Y, Morioka S, Ooshima A, Moriyama K
4th Department of Internal Medicine, Shimane Medical University, Izumo, Japan.
Jpn Circ J. 1992 Sep;56(9):899-910. doi: 10.1253/jcj.56.899.
The ultrastructural characteristics of collagen and the localization of collagen types were studied in formalin-fixed autopsied human hearts from patients who died in an advanced stage of dilated cardiomyopathy (DCM). The three-dimensional architecture of collagen fibers was studied by scanning electron microscopy by using the cell-maceration method. The localization of collagen type I-VI was demonstrated immunohistochemically using monoclonal antibodies specific to each collagen following the treatment of specimens with trypsin. In the hearts obtained from control subjects without heart disease, there were no significant differences in the ultrastructure and localization of collagens between the fresh and the formalin-fixed hearts. Therefore, formalin-fixation did not affect the ultrastructure of collagen or the immunoreactivity. In DCM, a dense endomysial weave network consisting of fine fibrils was associated predominantly with collagen type I and III, associated moderately with type VI collagen, but less associated with type IV collagen. Perimysial collagen bundles and collagen strands increased both in number and thickness. The outstanding finding was the presence of giant coiled perimysial fibers measuring about 20-30 microns in diameter. The prominent increase in perimysial fibrosis was closely associated with the accumulation of both type I and type III collagen, and associated moderately with type VI collagen. Interestingly, type V collagen increased in the intracellular matrix of the myocardium in DCM. Type II collagen was not present in either normal or diseased hearts. These structural and immunohistochemical characteristics of collagen may provide insights important to assessing the pathogenesis of the cardiac lesion of DCM.
对死于扩张型心肌病（DCM）晚期患者的福尔马林固定尸检人心脏中胶原蛋白的超微结构特征及胶原类型定位进行了研究。采用细胞浸渍法，通过扫描电子显微镜研究胶原纤维的三维结构。在用胰蛋白酶处理标本后，使用针对每种胶原蛋白的单克隆抗体免疫组织化学显示I-VI型胶原的定位。在从无心脏病的对照受试者获得的心脏中，新鲜心脏和福尔马林固定心脏之间胶原蛋白的超微结构和定位没有显著差异。因此，福尔马林固定不会影响胶原蛋白的超微结构或免疫反应性。在DCM中，由细纤维组成的致密肌内膜编织网络主要与I型和III型胶原相关，与VI型胶原中度相关，但与IV型胶原相关性较低。肌束膜胶原束和胶原纤维数量和厚度均增加。突出的发现是存在直径约20-30微米的巨大盘绕肌束膜纤维。肌束膜纤维化的显著增加与I型和III型胶原的积累密切相关，与VI型胶原中度相关。有趣的是，在DCM中，V型胶原在心肌细胞内基质中增加。正常或患病心脏中均不存在II型胶原。胶原蛋白的这些结构和免疫组织化学特征可能为评估DCM心脏病变的发病机制提供重要见解。
