Research reportOverexpressed tau protein in cultured cells is phosphorylated without formation of PHF: implication of phosphoprotein phosphatase involvement
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To target Tau pathologies, we must embrace and reconstruct their complexities
2021, Neurobiology of DiseaseCitation Excerpt :Recently, Mirbaha et al. reported the existence of the two populations of the metastable inert (Mi) and seed-competent Tau monomers (Ms) (Mirbaha et al., 2018), however, others failed to replicate their findings (Fichou et al., 2018a) and further studies are needed to test this hypothesis. Tau found in the NFTs generally exhibits high levels of phosphorylation (Pettegrew et al., 1988; Lee et al., 1991; Hasegawa, 2019), however early on, following contradicting reports (Baum et al., 1995; Kimura et al., 1996), it was unclear whether phosphorylation of Tau was sufficient or at all necessary for the formation of Tau fibrils. Therefore, to tease out the sequential order of the events associated with Tau fibril formation, researchers sought to decouple the processes of Tau phosphorylation and aggregation in vitro using recombinant non-phosphorylated Tau.
Synergistic effect of tanshinone IIA and mesenchymal stem cells on preventing learning and memory deficits via anti-apoptosis, attenuating tau phosphorylation and enhancing the activity of central cholinergic system in vascular dementia
2017, Neuroscience LettersCitation Excerpt :Previous reports demonstrated that hyperphosphorylation of tau in neuron was involved in neuronal death during many neurodegenerative diseases, and related to cognitive dysfunction in dementia [21]. GSK 3β was found to play a critical role in regulating the phosphorylation of tau [22]. Our data demonstrated that the treatment with 4-VO induced a significant reduction of GSK 3β phosphorylation, and thus contributed to a significant increase in the level of tau phosphorylation as compared to the sham group (Fig. 3A–D, P < 0.01).
Cellular models of aggregation-dependent template-directed proteolysis to characterize Tau aggregation inhibitors for treatment of Alzheimer disease
2015, Journal of Biological ChemistryCitation Excerpt :The difference between MTC and LMTM was not statistically significant (p = 0.29), but LMTB had lower potency than MTC (p < 0.0001). Stable cellular expression of the Tau aggregation domain of the PHF core in eukaryotic cells is difficult due to its inherent toxicity using a number of different vectors and cell lines (25–27) and is insufficient alone to induce aggregation (28). We were able to solve this problem initially by targeting the localization of the truncated Tau fragment to the membrane of the endoplasmic reticulum (ER), using a fusion protein comprising an 18-amino acid signal sequence (SS) (17) at the N terminus of the Tau fragment.
Tau phosphorylation in human brain: Relationship to behavioral disturbance in dementia
2012, Neurobiology of AgingCitation Excerpt :Glycogen synthase kinase-3β (GSK-3β) has been proposed to be one of the major protein kinases regulating tau phosphorylation and has been reported to be overactivated in brain samples from AD patients (Leroy et al., 2007). When GSK-3β phosphorylation is reduced, its kinase activity is increased, and this can lead to a direct increase in tau phosphorylation (Baum et al., 1995). On the basis of previous studies, we therefore hypothesized that the extent of tau phosphorylation in frontal cortex (BA9) but not parietal cortex (BA39) would be related to agitation/aggression.
Elevated tauopathy and alpha-synuclein pathology in postmortem Parkinson's disease brains with and without dementia
2010, Experimental NeurologyCitation Excerpt :Moreover, we found that upon oxidative stress by MPTP or MPP+, α-Syn induced p-Tau formation through specific activation and recruitment of p-GSK-3β, activated by autophosphorylation at Tyr216 (Kozikowski et al., 2006; Duka et al., 2009). GSK-3β is a proline-directed serine/threonine kinase, ubiquitously expressed in mammalian tissues, and epitopes phosphorylated by GSK-3β are among the pathological phosphorylation sites of Tau seen in NFTs and paired helical filaments (PHFs) of Alzheimer's disease, and GSK-3β is a major kinase implicated in Tau hyperphosphorylation (Baum et al., 1995). To examine the clinical relevance of our previous findings, the current studies were undertaken, and these are the first neurochemical examination of the α-Syn/p-Tau/GSK-3β pathway in human postmortem striata and IFG from PD and PD with dementia (PDD).