Yang K, Taft W C, Dixon C E, Yu R K, Hayes R L
Department of Neurosurgery, University of Texas Health Sciences Center at Houston.
J Neurotrauma. 1994 Oct;11(5):523-32. doi: 10.1089/neu.1994.11.523.
Acute biochemical consequences of moderate traumatic brain injury (TBI) include activation of kinases, including protein kinase C (PKC). To determine the possible consequences of PKC activation at the substrate level, we have examined protein phosphorylation patterns 1 h following injury. Although the phosphorylation of most proteins remained unchanged following injury, we observed a significant increase in the phosphorylation of a 61,000 dalton protein (TBI61) in injured rat hippocampus (121% higher than sham control) in vitro. TBI61 phosphorylation could be enhanced by phosphatidyl serine and diacylglycerol or by addition of exogenous PKC. In addition, TBI61 phosphorylation was inhibited by the PKC inhibitor, staurosporine, suggesting further that this protein may be a PKC substrate. These data suggest that TBI increases the phosphorylation of a 61 kD hippocampal protein in vitro. Increases in the protein level and activity of PKC could contribute to this increased phosphorylation.
中度创伤性脑损伤（TBI）的急性生化后果包括激酶的激活，其中包括蛋白激酶C（PKC）。为了确定PKC激活在底物水平上可能产生的后果，我们检测了损伤后1小时的蛋白质磷酸化模式。尽管损伤后大多数蛋白质的磷酸化保持不变，但我们观察到在体外，损伤大鼠海马体中一种61,000道尔顿蛋白质（TBI61）的磷酸化显著增加（比假手术对照组高121%）。磷脂酰丝氨酸和二酰基甘油或添加外源性PKC可增强TBI61的磷酸化。此外，PKC抑制剂星形孢菌素可抑制TBI61的磷酸化，这进一步表明该蛋白质可能是PKC的底物。这些数据表明，在体外TBI会增加一种61 kD海马体蛋白质的磷酸化。PKC蛋白质水平和活性的增加可能导致这种磷酸化增加。
