Skalli O, Jones J C, Gagescu R, Goldman R D
Department of Cell, Molecular, and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
J Cell Biol. 1994 Apr;125(1):159-70. doi: 10.1083/jcb.125.1.159.
The distribution of IFAP 300, a protein previously characterized as cross-linking vimentin intermediate filaments (IF), has been investigated in epithelial cells. In frozen sections of bovine tongue epithelium the staining obtained with IFAP 300 antibodies is concentrated in the peripheral cytoplasm of keratinocytes, including the entire peripheral region of basal cells. Further immunofluorescence studies reveal that in primary cultures of mouse keratinocytes the distribution of IFAP 300 is similar to that of the desmosomal protein desmoplakin. In rat bladder carcinoma 804G cells the staining pattern of IFAP 300 antibodies coincides with that obtained with antibodies against the hemidesmosomal protein BP 230. By immunogold electron microscopy IFAP 300 is mainly located at sites where IF appear to attach to desmosomes and hemidesmosomes. Morphometric analyses of the distribution of the gold particles show that IFAP 300 overlaps with desmoplakin and BP 230, but also that it extends deeper into the cytoplasm than these latter two proteins. The staining reaction seen in epithelial cells by immunofluorescence and immunogold is specific for IFAP 300 as shown by immunoblotting. Immunoblotting also reveals that IFAP 300 is present in both cell-free preparations of desmosomes and hemidesmosomes. These morphological and biochemical results are intriguing since, in recent years, the proteins appearing in these two types of junctions have been found to be different. One possible exception is plectin, a protein that has been suggested to be very similar to IFAP 300. However, we show here that IFAP 300 differs from plectin in several respects, including differences at the primary sequence level. We also show that purified IFAP 300 pellets with in vitro polymerized IF prepared from desmosome-associated keratins under conditions in which IFAP 300 alone is not sedimentable. This indicates that IFAP 300 can associate with keratin IF. These data, taken together with the immunogold results, suggest that IFAP 300 functions in epithelial cells as a linker protein connecting IF to desmosomes as well as to hemidesmosomes, possibly through structurally related proteins such as desmoplakin and BP 230, respectively.
IFAP 300是一种先前被鉴定为交联波形蛋白中间丝(IF)的蛋白质,其在上皮细胞中的分布已得到研究。在牛舌上皮的冰冻切片中,用IFAP 300抗体获得的染色集中在角质形成细胞的外周细胞质中,包括基底细胞的整个外周区域。进一步的免疫荧光研究表明,在小鼠角质形成细胞的原代培养物中,IFAP 300的分布与桥粒蛋白桥粒斑蛋白相似。在大鼠膀胱癌804G细胞中,IFAP 300抗体的染色模式与针对半桥粒蛋白BP 230的抗体所获得的染色模式一致。通过免疫金电子显微镜观察,IFAP 300主要位于IF似乎附着于桥粒和半桥粒的部位。对金颗粒分布的形态计量分析表明,IFAP 300与桥粒斑蛋白和BP 230重叠,但它也比后两种蛋白质更深地延伸到细胞质中。免疫印迹显示,上皮细胞中通过免疫荧光和免疫金观察到的染色反应对IFAP 300具有特异性。免疫印迹还表明,IFAP 300存在于桥粒和半桥粒的无细胞制剂中。这些形态学和生化结果很有趣,因为近年来,已发现出现在这两种连接中的蛋白质是不同的。一个可能的例外是网蛋白,一种被认为与IFAP 300非常相似的蛋白质。然而,我们在此表明,IFAP 300在几个方面与网蛋白不同,包括一级序列水平的差异。我们还表明,在IFAP 300单独不可沉降的条件下,纯化的IFAP 300与从桥粒相关角蛋白制备的体外聚合IF一起沉淀。这表明IFAP 300可以与角蛋白IF结合。这些数据与免疫金结果一起表明,IFAP 300在上皮细胞中作为一种连接蛋白发挥作用,将IF连接到桥粒以及半桥粒,可能分别通过结构相关蛋白如桥粒斑蛋白和BP 230。