Angenstein F, Staak S, Jork R
Institute of Neurobiology and Brain Research Magdeburg, F.R.G.
Neurosci Lett. 1992 Feb 3;135(2):269-72. doi: 10.1016/0304-3940(92)90453-e.
Studies on glycoprotein fucosylation were carried out using hippocampal slices from rat brain. These slices were incubated in the presence of the protein kinase C (PKC) activating phorbol ester, 4 beta-phorbol-12,13-dibutyrate (PDBu), or an inactive isoform, 4 alpha-phorbol-12,13-didecanoate (PDD), respectively, for 7 min followed by a 60 min pulse of [3H]fucose. PDBu caused an increase in [3H]fucose incorporation into glycoproteins by 29% as well as an activation of the fucokinase enzyme reaction by 21%. The PDBu-induced stimulation of [3H]fucose insertion into hippocampal glycoproteins was abolished by the PKC inhibitors, staurosporine and H7. The importance of a PKC-regulated glycoprotein fucosylation in mechanisms underlying changes in neuronal plasticity is discussed.
利用大鼠脑海马切片进行了糖蛋白岩藻糖基化研究。这些切片分别在蛋白激酶C(PKC)激活剂佛波酯4β-佛波醇-12,13-二丁酸酯(PDBu)或无活性异构体4α-佛波醇-12,13-二十二酸酯(PDD)存在的情况下孵育7分钟,随后进行60分钟的[3H]岩藻糖脉冲标记。PDBu使[3H]岩藻糖掺入糖蛋白的量增加了29%,同时使岩藻糖激酶酶反应激活了21%。PKC抑制剂星形孢菌素和H7消除了PDBu诱导的[3H]岩藻糖插入海马糖蛋白的刺激作用。本文讨论了PKC调节的糖蛋白岩藻糖基化在神经元可塑性变化潜在机制中的重要性。