Hahnel R, Gschwendt M
GERMAN CANC RES CTR,NEUENHEIMER FELD 280,D-69120 HEIDELBERG,GERMANY.
Int J Oncol. 1995 Jul;7(1):11-6. doi: 10.3892/ijo.7.1.11.
The interactions between protein kinase C (PKC) and the steroid hormone estradiol or its receptor (ER) are reviewed. Estradiol upregulates PKC both in vitro and in vivo in the ovary, the anterior pituitary and in mammary tissue of several mammalian species. The antiestrogen tamoxifen inhibits PKC. Activation of PKC leads to a marked decrease of ER protein and ERmRNA in human breast cancer cells and some other cell lines. Inhibition or down-regulation of PKC enhances ER binding. These results indicate that there are links between the PKC signal transduction pathway and the steroid receptor family. Further studies are needed to clarify the role of PKC isoforms in normal and cancerous tissues which are known to be influenced by estradiol.
本文综述了蛋白激酶C（PKC）与甾体激素雌二醇或其受体（ER）之间的相互作用。在几种哺乳动物的卵巢、垂体前叶和乳腺组织中，雌二醇在体外和体内均可上调PKC。抗雌激素他莫昔芬可抑制PKC。PKC的激活导致人乳腺癌细胞和其他一些细胞系中ER蛋白和ERmRNA显著减少。PKC的抑制或下调增强了ER结合。这些结果表明PKC信号转导途径与甾体受体家族之间存在联系。需要进一步研究以阐明PKC同工型在已知受雌二醇影响的正常组织和癌组织中的作用。
