Fitzgerald P G, Bok D, Horwitz J
J Cell Biol. 1983 Nov;97(5 Pt 1):1491-9. doi: 10.1083/jcb.97.5.1491.
The in situ distribution of the 26-kdalton Main Intrinsic Polypeptide (MIP or MP 26), a putative gap junction protein in ocular lens fibers, was defined at the electron microscope level using indirect immunoferritin labeling of ultrathin frozen sections of rat lens. MIP was found distributed throughout the plasma membrane of the lens fiber cell, with no apparent distinction between junctional and nonjunctional membrane. MIP was not detectable in the basal or lateral plasma membrane of the lens epithelial cell, including the interepithelial cell gap junctions; nor was MIP detectable in the plasma membrane or gap junctions of the hepatocyte. Previous reports have indicated that the protein composition of the lens fiber cell junction differs from that of the hepatocyte gap junction. The evidence presented here suggests that the composition of the fiber cell junction and plasma membrane is also immunocytochemically distinct from that of its progenitor, the lens epithelial cell.
利用大鼠晶状体超薄冰冻切片的间接免疫铁蛋白标记技术,在电子显微镜水平确定了26千道尔顿主要内在多肽(MIP或MP 26)的原位分布,MIP是晶状体纤维中一种假定的间隙连接蛋白。发现MIP分布于晶状体纤维细胞的整个质膜,连接膜和非连接膜之间无明显差异。在晶状体上皮细胞的基底或侧面质膜中,包括上皮细胞间的间隙连接,均未检测到MIP;在肝细胞的质膜或间隙连接中也未检测到MIP。先前的报道表明,晶状体纤维细胞连接的蛋白质组成与肝细胞间隙连接的不同。此处提供的证据表明,纤维细胞连接和质膜的组成在免疫细胞化学上也与其祖细胞即晶状体上皮细胞不同。