Schafer D A, Mooseker M S, Cooper J A
Department of Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110.
J Cell Biol. 1992 Jul;118(2):335-46. doi: 10.1083/jcb.118.2.335.
We have localized capping protein in epithelial cells of several chicken tissues using affinity-purified polyclonal antibodies and immunofluorescence. Capping protein has a distribution in each tissue coincident with proteins of the cell-cell junctional complex, which includes the zonula adherens, zonula occludens, and desmosome. "En face" views of the epithelial cells showed capping protein distributed in a polygonal pattern coincident with cell boundaries in intestinal epithelium, sensory epithelium of the cochlea, and the pigmented epithelium of the retina and at regions of cell-cell contact between chick embryo kidney cells in culture. "Edge-on" views obtained by confocal microscopy of intact single intestinal epithelial cells and of retinal pigmented epithelium showed that capping protein is located in the apical region of the epithelial cells coincident with the junctional complexes. These images do not resolve the individual types of junctions of the junctional complex. Immunolabeling of microvilli or stereocilia was faint or not detectable. Capping protein was also detected in the cytoplasm of intact intestinal epithelial cells and in nuclei of cells in the pigmented retina and in the kidney cell cultures, but not in nuclei of cells of the intestinal epithelium or sensory epithelium. Biochemical fractionation of isolated intestinal epithelial cells shows capping protein in the brush border fraction, which contains the junctional complexes, and in the soluble fraction. These results are consistent with the results of the immunolabeling experiments. Highly purified microvilli of the brush borders also contained capping protein; this result was unexpected based on the low intensity of immunofluorescence staining of microvilli and stereocilia. The microvilli were not contaminated with junctional complexes, as defined by the absence of several markers for cell junctions. The cause and significance of this discrepancy is not certain at this time. Since capping protein binds the barbed end of actin filaments in vitro, we hypothesize that capping protein is bound to the barbed ends of actin filaments associated with one or more of the junctions of the junctional complex.
我们使用亲和纯化的多克隆抗体和免疫荧光技术,在几种鸡组织的上皮细胞中定位了封端蛋白。封端蛋白在每个组织中的分布与细胞间连接复合体的蛋白质一致,该复合体包括黏着小带、紧密连接和桥粒。上皮细胞的“正面”视图显示,封端蛋白以多边形模式分布,与肠上皮、耳蜗感觉上皮、视网膜色素上皮中的细胞边界以及培养的鸡胚肾细胞之间的细胞接触区域一致。通过共聚焦显微镜对完整的单个肠上皮细胞和视网膜色素上皮进行“边缘”观察发现,封端蛋白位于上皮细胞的顶端区域,与连接复合体一致。这些图像无法分辨连接复合体的各个连接类型。微绒毛或静纤毛的免疫标记很微弱或无法检测到。在完整的肠上皮细胞的细胞质、色素视网膜细胞的细胞核以及肾细胞培养物中也检测到了封端蛋白,但在肠上皮或感觉上皮细胞的细胞核中未检测到。对分离的肠上皮细胞进行生化分级分离显示,封端蛋白存在于包含连接复合体的刷状缘部分和可溶部分。这些结果与免疫标记实验的结果一致。高度纯化的刷状缘微绒毛也含有封端蛋白;基于微绒毛和静纤毛免疫荧光染色强度较低,这个结果出乎意料。微绒毛没有被连接复合体污染,这是根据缺乏几种细胞连接标记来定义的。目前尚不确定这种差异的原因和意义。由于封端蛋白在体外结合肌动蛋白丝的带刺末端,我们推测封端蛋白与与连接复合体的一个或多个连接相关的肌动蛋白丝的带刺末端结合。