Mukai M, Torikata C, Iri H, Mikata A, Sakamoto T, Hanaoka H, Shinohara C, Baba N, Kanaya K, Kageyama K
Am J Pathol. 1984 Sep;116(3):398-406.
As an initial step to elucidate the nature of the unique characteristics of the crystalloids of alveolar soft part sarcoma, a three-dimensional model of the crystalloids was prepared by digital image analysis of electron micrographs by computer. It was revealed that occult periodicities are present at two intervals, 60 A and 380 A, in the filamentous structure of the crystalloid; and it was also revealed by the observation of each cross-section that two globular substances with a diameter of 60 A are arranged in a dumbbell pattern in each filamentous structure. The model prepared based on these data showed the double strands crossing each other at intervals of 380 A, each of which consists of successive arrangement of the globular substances with a diameter of 60 A. This structure is clearly similar to that of actin. The similarities and differences between these results and the well-known studies of the organization of naturally occurring actin bundles are discussed.
作为阐明肺泡软组织肉瘤晶体独特特征本质的第一步,通过计算机对电子显微镜照片进行数字图像分析,制备了晶体的三维模型。结果显示,在晶体的丝状结构中,存在60埃和380埃两种间隔的隐匿周期性;通过对每个横截面的观察还发现,在每个丝状结构中,两个直径为60埃的球状物质呈哑铃状排列。基于这些数据制备的模型显示,双链以380埃的间隔相互交叉,每条双链由直径为60埃的球状物质连续排列组成。这种结构与肌动蛋白的结构明显相似。讨论了这些结果与天然存在的肌动蛋白束组织的著名研究之间的异同。