Kurisaki T, Magae J, Nagai K, Hirata A, Kusaka I, Shinji H, Morikawa M, Yoshida T, Isono K, Yamasaki M
Department of Agricultural Chemistry, University of Tokyo, Japan.
Cell Struct Funct. 1993 Feb;18(1):33-9. doi: 10.1247/csf.18.33.
A protein phosphatase inhibitor, tautomycin induces blebs on the surface of human myeloid leukemia K562 cells within 10 min. In this paper we examined the cytoskeleton of tautomycin-treated cells. In the presence of tautomycin, cells with blebs turned into segmented forms with smooth surfaces after 15 min and into smooth round shapes without microprotuberance after 60 min. Observation with fluorescence microscopy showed that F-actin detached from the plasma membrane at the site of the blebs. Further treatment with tautomycin induced the accumulation of F-actin at the segmentation centers. Under electron microscopy, an electron dense ring-structure was detected at the segmentation center. Tautomycin did not induce major changes of the microtubule network although F-actin accumulated near the microtubule organizing center. The amount of F-actin increased in tautomycin-treated cells. These results indicate that the morphological changes are induced by reorganization of actinfilaments.
一种蛋白磷酸酶抑制剂，鬼笔环肽在10分钟内可诱导人髓系白血病K562细胞表面形成泡状结构。在本文中，我们研究了经鬼笔环肽处理的细胞的细胞骨架。在鬼笔环肽存在的情况下，有泡状结构的细胞在15分钟后变成表面光滑的分段形式，60分钟后变成没有微突起的光滑圆形。荧光显微镜观察显示，F-肌动蛋白在泡状结构部位从质膜上脱离。用鬼笔环肽进一步处理会导致F-肌动蛋白在分段中心积累。在电子显微镜下，在分段中心检测到电子致密的环状结构。尽管F-肌动蛋白在微管组织中心附近积累，但鬼笔环肽并未引起微管网络的重大变化。在经鬼笔环肽处理的细胞中F-肌动蛋白的量增加。这些结果表明，形态变化是由肌动蛋白丝的重组诱导的。
