Kalluri Haviryaji S G, Ticku Maharaj K
Department of Pharmacology. University of Texas Health Science Center, San Antonio, Texas 78229-3900, USA.
Neurochem Res. 2004 Apr;29(4):781-4. doi: 10.1023/b:nere.0000018850.03002.57.
In the present investigation, changes in the calcium calmodulin-dependent phosphorylation of proteins have been examined in murine fetal cortical neurons and adult cortex. An approximately 80-kD protein in the fetal neurons was not phosphorylated/dephosphorylated in a calmodulin-dependent manner. However, this protein was phosphorylated by PMA both in the presence and absence of calcium. These data suggest that calmodulin inhibits the phosphorylation of a approximately 80-kD protein by inhibiting PKC in murine fetal cortical neurons but not in the adult cortex. More importantly, we demonstrate that the calmodulin-mediated inhibition of phosphorylation was restored by preincubating the cortical neurons with KN-62, a CaM kinase inhibitor.
在本研究中,已对小鼠胎儿皮质神经元和成年皮质中钙调蛋白依赖性蛋白磷酸化的变化进行了检测。胎儿神经元中一种约80-kD的蛋白不会以钙调蛋白依赖性方式发生磷酸化/去磷酸化。然而,无论有无钙存在,该蛋白都能被佛波酯磷酸化。这些数据表明,在小鼠胎儿皮质神经元中,钙调蛋白通过抑制蛋白激酶C来抑制一种约80-kD蛋白的磷酸化,但在成年皮质中则不然。更重要的是,我们证明,通过用钙调蛋白激酶抑制剂KN-62对皮质神经元进行预孵育,可恢复钙调蛋白介导的磷酸化抑制作用。