Dimethylsulfoxide, retinoic acid and 12-O-tetradecanoylphorbol-13-acetate induce a selective decrease in the phosphorylation of P150, a surface membrane phosphoprotein of HL60 cells resistant to adriamycin.
Dimethylsulfoxide, retinoic acid and 12-O-tetradecanoylphorbol-13-acetate induce a selective decrease in the phosphorylation of P150, a surface membrane phosphoprotein of HL60 cells resistant to adriamycin.
复制标题
二甲亚砜、视黄酸和 12-O-十四烷酰佛波醇-13-乙酸酯可选择性降低 P150 的磷酸化，P150 是对阿霉素耐药的 HL60 细胞的表面膜磷蛋白。
DOI：
10.1016/0006-291x(86)90239-1
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发表时间：
1986
影响因子：
3.1
通讯作者：
Center,MS
中科院分区：
文献类型：
--
作者：
Marsh,W;Center,MS
已经进行了研究以分析从阿霉素抗性HL 60细胞分离的膜中的蛋白磷酸化，所述细胞已经在二甲亚砜（DMSO）、视黄酸（RA）或12-0-十四酰基佛波醇-13-乙酸酯（TPA）存在下生长了不同的时间段。结果表明，从用这些试剂处理的细胞中分离的膜在P150的磷酸化中是缺陷的，P150是与HL 60细胞中的耐药性相关的膜磷蛋白。这种反应是高度选择性的，因为只有少数膜蛋白在这些条件下显示磷酸化水平降低。在P150磷酸化显著降低的条件下，来自用DMSO、RA或TPA处理的细胞的膜中的镁依赖性蛋白激酶活性相对于未处理的膜没有改变。另外的研究还表明，用TPA处理耐药细胞导致P150的体内磷酸化显著降低。因此，这些结果表明，能够诱导HL 60细胞分化的试剂可以选择性地调节P150的磷酸化。这个系统应该是有价值的，在澄清这种蛋白质的磷酸化参与的机制。
Studies have been carried out to analyze protein phosphorylation in membranes isolated from adriamycin resistant HL60 cells which have been grown for various time periods in the presence of dimethylsulfoxide (DMSO), retinoic acid (RA) or 12-0-tetradecanoylphorbol-13-acetate (TPA). The results show that membranes isolated from cells treated with these agents are defective in the phosphorylation of P150, a membrane phosphoprotein associated with drug resistance in HL60 cells. This response is highly selective since only a few membrane proteins show decreased phosphorylation levels under these conditions. Magnesium dependent protein kinase activity in membranes from cells treated with DMSO, RA or TPA is not altered relative to untreated membranes under conditions where there is a major decrease in P150 phosphorylation. Additional studies also show that treatment of resistant cells with TPA results in a major decrease in the in vivo phosphorylation of P150. These results thus demonstrate that agents capable of inducing differentiation in HL60 cells can selectively modulate the phosphorylation of P150. This system should be of value in clarifying mechanisms involved in the phosphorylation of this protein.