Lehto V P, Virtanen I, Paasivuo R, Ralston R, Alitalo K
EMBO J. 1983;2(10):1701-5. doi: 10.1002/j.1460-2075.1983.tb01645.x.
Biochemical and immunofluorescence studies have demonstrated that p36, a major substrate for the tyrosine-specific protein kinases induced by several sarcoma viruses and epidermal growth factor, is associated with plasma membranes and detergent-resistant cytoskeletal structures of cultured cells. We have used here polyclonal antisera and monoclonal antibodies in indirect immunofluorescence microscopy to study the subcellular location of p36 and the p230, which is a subplasmalemmal polypeptide showing immunologic cross-reactivity with erythrocyte alpha-spectrin. Both p36 and p230 showed a diffuse distribution in fixed and permeabilized cells and were localized in a surface lamina-like network in Triton-extracted cells. In double-staining experiments, an extensive co-distribution between these proteins was seen in detergent-treated cultured fibroblasts. These results, together with our previous work, suggest that the p36 protein is an integral part of the detergent-resistant proteinaceous network at the cytoplasmic face of the plasma membrane.
生化和免疫荧光研究表明，p36是几种肉瘤病毒和表皮生长因子诱导的酪氨酸特异性蛋白激酶的主要底物，与培养细胞的质膜和抗去污剂细胞骨架结构相关。我们在此使用多克隆抗血清和单克隆抗体进行间接免疫荧光显微镜检查，以研究p36和p230的亚细胞定位，p230是一种质膜下多肽，与红细胞α-血影蛋白具有免疫交叉反应性。p36和p230在固定和通透的细胞中均呈弥漫性分布，并定位于经Triton处理的细胞中的表面层状网络。在双重染色实验中，在经去污剂处理的培养成纤维细胞中，这些蛋白质之间存在广泛的共分布。这些结果，连同我们之前的工作，表明p36蛋白是质膜细胞质面抗去污剂蛋白质网络的一个组成部分。
