Zalewska T, Domanska-Janik K
Department of Neurochemistry, Medical Research Center, Polish Academy of Science, Warsaw, Poland.
Neuroreport. 1996 Jan 31;7(2):637-41. doi: 10.1097/00001756-199601310-00062.
The activity of Ca2+/calmodulin-dependent protein kinase II (CaM-KII) during short-term global ischaemia was investigated in the gerbil brain hippocampus and cortex. Ischaemia of 0.5 min duration significantly stimulated Ca(2+)-independent 'autonomous' activity, indicating activation of the first step of intramolecular enzyme phosphorylation just after ischaemia has developed. Prolongation of the ischaemic period up to 5 min inhibited both Ca(2+)-dependent and, to a lesser extent, Ca(2+)-independent activities of CaM-KII. These last events coincide with an extensive translocation of CaM-KII protein from the soluble to the membranous fraction. In effect, in spite of inhibition of total CaM-KII activity, its Ca(2+)-independent, persistently active component can still remain more abundant at specific membrane regions.
在沙鼠脑海马体和皮质中研究了短期全脑缺血期间钙/钙调蛋白依赖性蛋白激酶II（CaM-KII）的活性。持续0.5分钟的缺血显著刺激了不依赖钙的“自主”活性，表明在缺血发生后分子内酶磷酸化的第一步被激活。缺血时间延长至5分钟会抑制CaM-KII的钙依赖性活性以及程度较轻的不依赖钙的活性。这些最后的事件与CaM-KII蛋白从可溶性部分向膜性部分的广泛转位相吻合。实际上，尽管总CaM-KII活性受到抑制，但其不依赖钙的、持续活跃的成分在特定膜区域仍可能保持更丰富。
