p(RGD:Mapt, pmod(Ph))

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Name

Mapt

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rgd

Namespace Version

20181021

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https://raw.githubusercontent.com/pharmacome/terminology/f2f993e599694ab5ce989cc39d789a499f75db99/external/rgd-names.belns

This document contains the bel code for the Article Alzheimer’s disease-type neuronal tau hyperphosphorylation induced by Abeta oligomers by De Felice et al

TAU Interactions Section of NESTOR

Tau Modifications Sections of NESTOR

We then investigated whether bADDLs also induced tau phosphorylation in rat hippocampal neurons. To this end, we initially used frozen dissociated rat hippocampal cell preparations (Cambrex). Cells were maintained in the presence of 1M bADDLs (Fig. 2I and J) or vehicle (not shown) for 6 h at 37 ◦C. We observed a marked P-tau immunostaining in a subpopulation of neurons that also had ADDLs bound (Fig. 2I, arrowheads), while cells that did not bind bADDLs had no AT8 staining (Fig. 2J). PubMed:17403556

Thus, Tau and FKBP52 form a complex in rat brain. These findings indicate a direct interaction between FKBP52 and Tau. As shown in Fig. 3B, the amount of FKBP52 recruited by Tau depends on its phosphorylation state.In any case, these results underline the importance of Tau phosphorylation for its binding to FKBP52. PubMed:20133804

In the present study we injected bilaterally 3-morpholino-sydnonimine (SIN-1), a recognized and widely used peroxynitrite donor (25–30), into rat hippocampus, and investigated whether or not peroxynitrite could induce simultaneously nitration and hyperphosphorylation of tau and the underlying mechanisms in vivo. The level of nitrated and hyperphosphorylated tau was markedly increased in rat hippocampus 24 h, and prevented by preinjection of uric acid, a natural scavenger of peroxynitrite. GSK-3beta and p38 MAPKs, including p38alpha, p38beta, and p38delta activity was increased, but no change in the activity of p38gamma, ERK, and c-Jun amino-terminal kinase (JNK). Both nitrated tau and hyperphosphorylated tau were aggregated in the hippocampus, with activity of 20S proteasome significantly arrested in SIN-1-injected rats. Hyperphosphorylated tau was degraded as efficiently as normal tau by 20S proteasome, but the nitrated tau with an unorderly secondary structure became more resistant to the proteolysis, providing evidence that peroxynitrite simultaneously induces tau hyperphosphorylation, nitration, and accumulation, and that activation of GSK-3beta, p38alpha, p38beta, p38delta isoforms and the inhibition of proteasome activity are respectively responsible for the peroxynitrite-induced tau hyperphosphorylation and accumulation. PubMed:16816118

Thus, Tau and FKBP52 form a complex in rat brain. These findings indicate a direct interaction between FKBP52 and Tau. As shown in Fig. 3B, the amount of FKBP52 recruited by Tau depends on its phosphorylation state.In any case, these results underline the importance of Tau phosphorylation for its binding to FKBP52. PubMed:20133804