Brooks S F, Evans F J, Aitken A
Laboratory of Protein Structure, National Institute for Medical Research, Mill Hill, London.
FEBS Lett. 1987 Nov 16;224(1):109-16. doi: 10.1016/0014-5793(87)80431-3.
Using a pituitary tumour cell line (GH3), we have studied the phosphorylation of intracellular proteins induced by phorbol esters of diverse biological activity. All the active phorbol esters, including the weakly tumour-promoting but non-platelet aggregatory compound DOPPA, stimulated the phosphorylation of a cytosolic 80 kDa protein. A protein of this molecular mass has been suggested to be a marker of PKC activity. In contrast, only TPA and the non-tumour promoting but highly active phorbol ester SAP A stimulated the phosphorylation of a 130 kDa membrane protein. The results suggest that these phorbol esters activate PKC, but induce the differential phosphorylation of a variety of intracellular proteins.
利用一种垂体肿瘤细胞系（GH3），我们研究了具有不同生物活性的佛波酯所诱导的细胞内蛋白质磷酸化。所有活性佛波酯，包括促肿瘤作用较弱但无血小板聚集作用的化合物DOPPA，均刺激一种80 kDa胞质蛋白的磷酸化。有人提出这种分子量的蛋白质是蛋白激酶C（PKC）活性的标志物。相比之下，只有佛波醇酯TPA和无促肿瘤作用但活性很高的佛波酯SAP A刺激一种130 kDa膜蛋白的磷酸化。结果表明，这些佛波酯激活PKC，但诱导多种细胞内蛋白质发生差异性磷酸化。
