Fry D W, Ambroso L A
Department of Cancer Research, Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Ann Arbor, MI 48105, USA.
Cancer Biochem Biophys. 1993 Sep;13(4):265-78.
Immunoprecipitation of cell lysates from serum-starved HCT-8 colon carcinoma cells with monoclonal antibodies raised to PLC-gamma 1 precipitates proteins which can be detected by immunoblotting; the 148 Kd PLC-gamma 1 and a smaller protein of approximately 118 Kd (p118). Expression of p118 is suppressed in cells grown in serum but is present 8 to 12 h after cells are placed in serum-free medium. Conversely, serum-starved cells that express this protein suppress it 6 to 8 h after exposure to 10% fetal calf serum. Pulse chase experiments indicate that the protein is not a degradation product of PLC. This protein has thus far been detected only in human carcinoma cells and not in normal or transformed fibroblasts. Although the protein has not been identified, its expression pattern may suggest a role contributing to the serum-independent nature of human carcinoma cell lines.
用针对PLC-γ1产生的单克隆抗体对血清饥饿的HCT-8结肠癌细胞的细胞裂解物进行免疫沉淀，沉淀出的蛋白质可通过免疫印迹检测到；148 Kd的PLC-γ1和一种约118 Kd的较小蛋白质（p118）。p118的表达在血清中生长的细胞中受到抑制，但在细胞置于无血清培养基中8至12小时后出现。相反，表达这种蛋白质的血清饥饿细胞在暴露于10%胎牛血清后6至8小时会抑制它。脉冲追踪实验表明该蛋白质不是PLC的降解产物。迄今为止，这种蛋白质仅在人癌细胞中检测到，而在正常或转化的成纤维细胞中未检测到。尽管该蛋白质尚未被鉴定，但其表达模式可能表明它在人癌细胞系的血清非依赖性特性中发挥作用。
