Transient brain ischemia has been shown to induce hyperphosphorylation of the microtu-bule-associated protein tau. To further determine the mechanisms underlying these processes, Dr, Bo Song and co-workers from School of Life Sciences, Tsinghua University in China found for the first time that the interaction of tau with glycogen synthase kinase (GSK)-3β and protein phosphatase 2A is altered during transient brain ischemia. In addition, the researchers found that the neuroprotective function of lithium chloride may depend partly on the altered phosphorylation of tau, by regulating the associations between tau, GSK-3β and protein phosphatase 2A during cerebral ischemia. These findings were published in the Neural Regeneration Research (Vol. 8, No. 34, 2013).
Article: " Phosphorylation of tau protein over time in rats subjected to transient brain ischemia " by Bo Song1, 2, Qiang Ao1, 3, Zhen Wang3, Weiqiang Liu3, Ying Niu2, Qin Shen4, Huancong Zuo1, Xiufang Zhang2, Yandao Gong2 (1 Institute of Neurology Disorders, Yuquan Hospital, Tsinghua University, Beijing 100049, China; 2 State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China; 3 Center for Advanced Materials and Biotechnology, Research Institute of Tsinghua-University in Shenzhen, Shenzhen High-Tech Industrial Estate, Shenzhen 518057, China; 4Medical School, Tsinghua University, Beijing 100084, China)
Song B, Ao Q, Wang Z, Liu WQ, Niu Y, Shen Q, Zuo HC, Zhang XF, Gong YD. Phosphorylation of tau protein over time in rats subjected to transient brain ischemia. Neural Regen Res. 2013;8(34):3173-3182.
Contact: Meng Zhao
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Neural Regeneration Research
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Neural Regeneration Research