Darbon J M, Issandou M, Tournier J F, Bayard F
Inserm U168, Department of Endocrinology, CHU Rangueil, Université Paul Sabatier, Toulouse, France.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):527-36. doi: 10.1016/0006-291x(90)92353-2.
The phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) stimulated the phosphorylation of two distinct 27 kDa and 28 kDa proteins, respectively, in bovine vascular endothelial cells and in MCF-7 human breast cancer cells. These protein phosphorylation events were correlated to striking opposite cell growth responses to TPA, i.e., stimulation of vascular endothelial cell proliferation and inhibition of MCF-7 cell growth. Exposure of both vascular endothelial and MCF-7 cells to heat shock induced synthesis of the respective 27 kDa and 28 kDa proteins among a set of common and distinct other proteins as well as an increase in the degree of phosphorylation of the two 27 kDa and 28 kDa proteins. These results suggest that the two protein kinase C substrates very likely belong to the family of low molecular mass stress proteins.
佛波酯12 - O -十四酰佛波醇13 -乙酸酯（TPA）分别刺激牛血管内皮细胞和MCF - 7人乳腺癌细胞中两种不同的27 kDa和28 kDa蛋白质的磷酸化。这些蛋白质磷酸化事件与对TPA截然不同的细胞生长反应相关，即刺激血管内皮细胞增殖和抑制MCF - 7细胞生长。血管内皮细胞和MCF - 7细胞暴露于热休克下会诱导在一组共同和不同的其他蛋白质中合成各自的27 kDa和28 kDa蛋白质，同时这两种27 kDa和28 kDa蛋白质的磷酸化程度增加。这些结果表明，这两种蛋白激酶C底物很可能属于低分子量应激蛋白家族。
