Kapprell H P, Owaribe K, Franke W W
Division of Membrane Biology and Biochemistry, German Cancer Research Center, Heidelberg.
J Cell Biol. 1988 May;106(5):1679-91. doi: 10.1083/jcb.106.5.1679.
Desmosomes are intercellular adhering junctions characterized by a special structure and certain obligatory constituent proteins such as the cytoplasmic protein, desmoglein. Desmosomal fractions from bovine muzzle epidermis contain, in addition, a major polypeptide of Mr approximately 75,000 ("band 6 protein") which differs from all other desmosomal proteins so far identified by its positive charge (isoelectric at pH approximately 8.5 in the denatured state) and its avidity to bind certain type I cytokeratins under stringent conditions. We purified this protein from bovine muzzle epidermis and raised antibodies to it. Using affinity-purified antibodies, we identified a protein of identical SDS-PAGE mobility and isoelectric pH in all epithelia of higher complexity, including representatives of stratified, complex (pseudostratified) and transitional epithelia as well as benign and malignant human tumors derived from such epithelia. Immunolocalization studies revealed the location of this protein along cell boundaries in stratified and complex epithelia, often resolved into punctate arrays. In some epithelia it seemed to be restricted to certain cell types and layers; in rat cornea, for example, it was only detected in upper strata. Electron microscopic immunolocalization showed that this protein is a component of the desmosomal plaque. However, it was not found in the desmosomes of all simple epithelia examined, in the tumors and cultured cells derived thereof, in myocardiac and Purkinje fiber cells, in arachnoideal cells and meningiomas, and in dendritic reticulum cells of lymphoid tissue, i.e., all cells containing typical desmosomes. The protein was also absent in all nondesmosomal adhering junctions. From these results we conclude that this basic protein is not an obligatory desmosomal plaque constituent but an accessory component specific to the desmosomes of certain kinds of epithelial cells with stratified tissue architecture. This suggests that the Mr 75,000 basic protein does not serve general desmosomal functions but rather cell type-specific ones and that the composition of the desmosomal plaque can be different in different cell types. The possible diagnostic value of this protein as a marker in cell typing is discussed.
桥粒是细胞间的黏附连接,其特征在于具有特殊结构和某些必需的组成蛋白,如细胞质蛋白桥粒芯糖蛋白。此外,来自牛口鼻部表皮的桥粒组分含有一种主要的分子量约为75,000的多肽(“6带蛋白”),该多肽与迄今鉴定的所有其他桥粒蛋白不同,其带正电荷(变性状态下的等电点约为pH 8.5),并且在严格条件下对结合某些I型细胞角蛋白具有亲和力。我们从牛口鼻部表皮中纯化了这种蛋白质并制备了针对它的抗体。使用亲和纯化的抗体,我们在所有更高复杂性的上皮组织中鉴定出一种具有相同SDS-PAGE迁移率和等电pH值的蛋白质,包括复层、复层(假复层)和移行上皮的代表,以及源自此类上皮的良性和恶性人类肿瘤。免疫定位研究揭示了这种蛋白质在复层和复层上皮细胞边界处的位置,通常呈点状排列。在某些上皮组织中,它似乎仅限于某些细胞类型和层;例如,在大鼠角膜中,仅在上层检测到。电子显微镜免疫定位显示该蛋白质是桥粒斑的一个组成部分。然而,在所有检查的单层上皮、源自其的肿瘤和培养细胞、心肌和浦肯野纤维细胞、蛛网膜细胞和脑膜瘤以及淋巴组织的树突状网状细胞(即所有含有典型桥粒的细胞)的桥粒中均未发现。该蛋白质在所有非桥粒黏附连接中也不存在。从这些结果我们得出结论,这种碱性蛋白质不是桥粒斑的必需组成成分,而是特定于某些具有复层组织结构的上皮细胞桥粒的辅助成分。这表明分子量75,000的碱性蛋白质不发挥一般的桥粒功能,而是细胞类型特异性的功能,并且桥粒斑的组成在不同细胞类型中可能不同。讨论了这种蛋白质作为细胞分型标志物的可能诊断价值。