Jimenez de Asua L, Goin M
Department of Biochemistry, Institute of Animal Physiology and Genetics Research, Babraham, Cambridge, UK.
FEBS Lett. 1992 Mar 16;299(3):235-8. doi: 10.1016/0014-5793(92)80122-w.
Prostaglandin F2 alpha (PGF2 alpha) selectively decreases the binding of 125I-labelled epidermal growth factor ([125I]EGF) to intact Swiss 3T3 cells. Scatchard analysis reveals that PGF2 alpha decreases the number of high-affinity EGF binding sites without changing the total number of receptors. Prostaglandins E1 (PGE1), E2 (PGE2) or F2 beta (PGF2 beta) do not alter the EGF binding to these cells and do not enhance the PGF2 alpha effect. R-59022 and R-59949, two diacylglycerol kinase inhibitors, enhance the inhibitory effect of PGF2 alpha, whereas down-modulation of protein kinase C (PKC) abolishes the effect. These results indicate that PGF2 alpha decreases EGF binding in Swiss 3T3 cells via PKC activation.
前列腺素F2α(PGF2α)可选择性降低125I标记的表皮生长因子([125I]EGF)与完整的瑞士3T3细胞的结合。Scatchard分析表明,PGF2α可减少高亲和力EGF结合位点的数量,而不改变受体总数。前列腺素E1(PGE1)、E2(PGE2)或F2β(PGF2β)不会改变EGF与这些细胞的结合,也不会增强PGF2α的作用。两种二酰基甘油激酶抑制剂R-59022和R-59949可增强PGF2α的抑制作用,而蛋白激酶C(PKC)的下调则可消除该作用。这些结果表明,PGF2α通过激活PKC降低瑞士3T3细胞中的EGF结合。