02674nas a2200229   4500008004100000022001400041245007900055210006900134260000900203300001200212490000800224520191600232653002402148653001002172653001402182653002402196653002402220653002002244100003402264700003602298856011002334       2020                        eng d  a0306-452200aG-protein coupled receptors and tau-different roles in alzheimer's disease0 aGprotein coupled receptors and taudifferent roles in alzheimers   cJUL   a198-2140 v4383 a<p>Post-translational modification of Tau, a microtubule-associated protein in the neuronal cell, plays a major role in Alzheimer's disease. Tau is an axonal protein expressed in mature neurons that promote the self-assembly of tubulin into microtubules and its stabilization in neurons. Phosphorylation of Tau makes it prone to aggregation at the intra-neuronal region leading to impaired neurotransmission and dementia. Tau aggregates undergo trans-cellular propagation by the release of fibrillar species into the extra-cellular environment from damaged and infected neurons that can be internalized by neighbouring neuronal and glia cells and promotes aggregation in healthy cells. G-protein coupled receptors, the largest group of seven transmembrane receptors, are involved in neuronal signal transduction in response to various signals such as hormones and neurotransmitters. In Alzheimer's disease, GPCRs are involved in phosphorylation of Tau through various downstream kinases such as GSK-3b, CDK-5 and ERKs signalling cascade. Several neuronal GPCRs that are involved in Tau phosphorylation are elaborated in this review. The astrocytic GPCR, Tau phosphorylation mediated by CaS receptors and its propagation by exosomes are also elaborated. In the microglia, the extra-cellular Tau binding to a chemokine GPCR, CX3CR1 triggers its internalization, whereas Tau phosphorylation at specific sites decreases its binding affinity to this receptor. Here we highlight the role of GPCRs in Tau phosphorylation and Tau interaction in different cells of the nervous system. Hence, the role of GPCRs are attaining more attention in the therapeutic field of Alzheimer's disease. Specific agonists/antagonists and allosteric modulators could be the potential target for therapy against GPCR-mediated Tau phosphorylation in Alzheimer's disease. (C) 2020 IBRO. Published by Elsevier Ltd. All rights reserved.</p>
10aAlzheimer's disease10aGPCRs10amicroglia10aTau internalization10aTau phosphorylation10aTau propagation1 aChidambaram, Hariharakrishnan1 aChinnathambi, Subashchandrabose  uhttps://library.ncl.res.in/content/g-protein-coupled-receptors-and-tau-different-roles-alzheimers-disease02240nas a2200277   4500008004100000022001400041245007900055210006900134260000800203300001100211490000800222520137500230653002001605653001501625653000901640653002201649653001101671653002001682653002401702100001801726700002101744700002301765700002701788700003601815856011101851       2023                        eng d  a0141-813000aBacopa monnieri reduces Tau aggregation and Tau-mediated toxicity in cells0 aBacopa monnieri reduces Tau aggregation and Taumediated toxicity  cAPR  a1231710 v2343 a<p>
	Alzheimer's disease is a neurodegenerative disease characterized by progressive memory loss and behavioral impairments. In the present study, the ethanolic extract of Bacopa monnieri was studied for its potency to inhibit Tau aggregation and rescuing of the viability of Tau-stressed cells. Bacopa monnieri was observed to inhibit the Tau aggregation in vitro. The cells exposed to Bacopa monnieri were also observed to have a low level of ROS and caspase-3 activity. The immunoblot and immunofluorescence analysis showed that Bacopa monnieri acts as an antioxidant and restored the Nrf2 levels in Neuro2a cells. Bacopa monnieri treatment to Neuro2a cells was observed to reduce the phospho-Tau load in formaldehyde-stressed cells. Furthermore, the treatment of Bacopa monnieri reduced the phosphorylation of GSK-3 beta in formaldehyde-stressed cells. Ran and NUP358 are the key proteins involved in nuclear transport. It was observed that formaldehyde treatment impaired the nuclear transport by missorting the NUP358 arrangement in Neuro2a cells. On the contrary, Bacopa monnieri treatment restored the NUP358 arrangement in cells. The overall results of the present study suggested that Bacopa monnieri could be considered a potent herb against Tau phosphorylation and Tau aggregation, which projects it as a promising formulation for Alzheimer's disease.</p>
10aBacopa monnieri10aGSK-3 beta10aNrf210aNuclear transport10aNUP35810aTau Aggregation10aTau phosphorylation1 aDubey, Tushar1 aKushwaha, Preeti1 aThulasiram, H., V.1 aChandrashekar, Madhura1 aChinnathambi, Subashchandrabose  uhttps://library.ncl.res.in/content/bacopa-monnieri-reduces-tau-aggregation-and-tau-mediated-toxicity-cells