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Phosphorylation of tau protein in rats subjected to cerebral ischemia-reperfusion injury

March 10th, 2014

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).

More information:
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.

Provided by Neural Regeneration Research

Citation: Phosphorylation of tau protein in rats subjected to cerebral ischemia-reperfusion injury (2014, March 10) retrieved 26 July 2026 from https://sciencex.com/wire-news/155909693/phosphorylation-of-tau-protein-in-rats-subjected-to-cerebral-isc.html
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