Foisy S, Joly E C, Bibor-Hardy V
Institut du cancer de Montréal, Centre de recherche Louis-Charles Simard, QC, Canada.
Biochem Cell Biol. 1997;75(6):721-32.
Research on the structure of the nuclear lamina and the nuclear matrix of cells devoid of lamins A and C has been hampered by the fact that intact residual nuclear structures are difficult to isolate from such cells. In this paper, we show that some extraction parameters, such as buffer composition and the nature of the detergent used to remove nuclear membranes, are critical for achieving isolation of whole nuclear residual structures from the lymphoblastic cell line Raji, used as a model for cells without lamins A and C. Electron microscopic analysis shows that the nuclear lamina of Raji cells is formed by a network of intermediate-size filaments interrupted with circular discontinuities. Both lamins B1 and B2, and lamin D/E, are present in this structure. In addition, a group of 45-kDa proteins or intermediate filament protein--reacting proteins (IFA-RPs), located uniquely in the lamina, were found to exhibit the same immunological and chemical characteristics as lamins. Although they behave like nuclear lamins, microsequencing analysis of the IFA-RPs has revealed no homology with known lamins. These IFA-RPs may contribute to the formation of the nuclear lamina filament network in the absence of lamins A and C.
由于难以从缺乏核纤层蛋白A和C的细胞中分离出完整的残余核结构,对这类细胞的核纤层和核基质结构的研究受到了阻碍。在本文中,我们表明,一些提取参数,如缓冲液组成和用于去除核膜的去污剂的性质,对于从用作缺乏核纤层蛋白A和C的细胞模型的淋巴母细胞系Raji中分离出完整的核残余结构至关重要。电子显微镜分析表明,Raji细胞的核纤层由中间大小的细丝网络形成,这些细丝网络被圆形间断打断。核纤层蛋白B1和B2以及核纤层蛋白D/E都存在于这种结构中。此外,发现一组仅位于核纤层的45 kDa蛋白或中间丝蛋白反应蛋白(IFA-RPs)与核纤层蛋白具有相同的免疫和化学特性。尽管它们的行为类似于核纤层蛋白,但对IFA-RPs的微量测序分析表明,它们与已知的核纤层蛋白没有同源性。这些IFA-RPs可能在缺乏核纤层蛋白A和C的情况下有助于核纤层细丝网络的形成。