Wang K, Singer S J
Proc Natl Acad Sci U S A. 1977 May;74(5):2021-5. doi: 10.1073/pnas.74.5.2021.
Filamin is a major high-molecular-weight protein in smooth muscle which was recently identified and isolated [Wang, K., Ash, J. F. & Singer, S. J. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 4483-4486]. In the present studies, we shown that highly purified chicken gizzard filamin and muscle F-actin react in solution to form aggregates containing both proteins. Occasionally, these aggregates coagulate and contract into a dense gel in the absence of MgATP or CaATP. Immunofluorescence and electron microscopic studies suggest that the F-actin filaments are collected into fiber bundles and a crosslinked fiber meshwork by the binding of filamin molecules. These studies suggest that the function of filamin intact cells may be to regulate the ultrastructural state of F-actin filaments in a variety of dynamic cellular processes.
细丝蛋白是平滑肌中一种主要的高分子量蛋白质，最近已被鉴定和分离出来[王，K.，阿什，J. F. & 辛格，S. J.（1975年）《美国国家科学院院刊》72，4483 - 4486]。在目前的研究中，我们发现高度纯化的鸡肫细丝蛋白与肌肉F - 肌动蛋白在溶液中反应形成含有这两种蛋白质的聚集体。偶尔，这些聚集体在没有MgATP或CaATP的情况下会凝结并收缩成致密凝胶。免疫荧光和电子显微镜研究表明，F - 肌动蛋白丝通过细丝蛋白分子的结合被收集成纤维束和交联的纤维网络。这些研究表明，完整细胞中细丝蛋白的功能可能是在各种动态细胞过程中调节F - 肌动蛋白丝的超微结构状态。
