Weller N K
Center for Cancer Research, Massachusets Institute of Technology, Cambridge 02139.
Biol Cell. 1988;63(3):307-17.
When eukaryotic cells are exposed to environmental stress such as elevated temperature, the synthesis of heat shock proteins (HSP) is stimulated. We have raised a monoclonal antibody to a 70 kDa cytoskeleton-associated protein; this antibody also appears to recognize HSPs 68, 70 and 90, as well as an additional 40 kDa non-heat shock protein. We have used this monoclonal antibody to study the localization of the 70 kDa protein in the cytoskeletons of NIL8 hamster fibroblasts. By selective sequential solubilization of the components of NIL8 cells and analysis of the resulting cytoskeletal preparations by Western blot technique and indirect immunofluorescence, we have shown that the 70 kDa protein is associated with microtubules in mitotic and interphase cells and comigrates with HSP70 on 2-dimensional gel electrophoretigrams.
当真核细胞暴露于诸如温度升高之类的环境应激时，热休克蛋白（HSP）的合成会受到刺激。我们制备了一种针对70 kDa细胞骨架相关蛋白的单克隆抗体；该抗体似乎还能识别HSP68、70和90，以及另一种40 kDa的非热休克蛋白。我们使用这种单克隆抗体来研究70 kDa蛋白在NIL8仓鼠成纤维细胞骨架中的定位。通过对NIL8细胞成分进行选择性顺序溶解，并利用蛋白质印迹技术和间接免疫荧光对所得细胞骨架制剂进行分析，我们发现70 kDa蛋白在有丝分裂细胞和间期细胞中与微管相关，并且在二维凝胶电泳图上与HSP70共迁移。
