EGCG, a green tea polyphenol, as a modulator of the in vitro methylglyoxal-induced tau glycation and its effect on the reduction of advanced glycation end products in neuroblastoma cells

Source: Correspondence with – Subashchandrabose Chinnathambi – [email protected]

Oncotarget released “Epigallocatechin-3-gallate modulates tau post-translational modifications and cytoskeletal network“Who reported that the chemical modulators of Tau-PTMs, such as kinase inhibitors and antibody-based therapeutics, have been developed, but natural compounds as modulators of Tau-PTMs have not been explored much.

These authors applied biophysical and biochemical techniques such as fluorescence kinetics, oligomerization analysis, and transmission electron microscopy to study the influence of EGCG on tau glycation in vitro.

EGCG inhibited the methylglyoxal-induced tau glycation in vitro.

EGCG strongly inhibited the MG-induced formation of advanced glycation end products in neuroblastoma cells and also modulated the localization of AT100 phosphorylated tau in the cells.

They report EGCG, a polyphenol from green tea, as a modulator of in vitro Methylglyoxal-induced tau glycation and its influence on the reduction of advanced glycation end products in neuroblastoma cells.

EGCG, a green tea polyphenol, acts as a modulator of in vitro Methylglyoxal-induced tau glycation and its influence on the reduction of advanced glycation end products in neuroblastoma cells.

Dr. Subashchandrabose Chinnathambi from the CSIR-National Chemical Laboratory and the Academy of Scientific and Innovative Research said: “Tau is a microtubule-associated protein that supports neuronal function [1, 2] and tau neurofibrillary tangles is one of the important characteristic pathologies in AD.

The clearance of hyperphosphorylated tau is decreased by PTMs such as glycation, nitration, and polyamination, while glycosylation and dephosphorylation prevent tau hyperphosphorylation.

In contrast to phosphorylation, glycation is a non-enzymatic PTM that occurs between reducing sugars and proteins, lipids, etc. Glycation is triggered at high blood sugar levels due to its metabolism via the polyol pathway, which converts sugars into highly reactive intermediates such as methylglyoxal, gloxal, etc. Glycation involves multi-step reactions, including complex rearrangements that form advanced glycation end products.

In addition, the tau glycation is modulated in an isoform-dependent manner and the glycation together with the phosphorylation increases the tendency of full-length tau to aggregate.

In this study, they demonstrate the effect of EGCG in inhibiting tau glycation in vitro and global glycation in neuroblastoma cells.

The Chinnathambi Research Team concluded in his Oncotarget“> Research shows that similar studies have reported a decrease in MG-induced AGE formation in neuro2a by AG.

The decrease in AGEs and ROS by EGCG has already been shown in previous studies on Nrf2-dependent signaling pathways in different cell types.

The exact mechanism by which AGEs formation is inhibited in mouse neuroblastoma cells is unclear, but it could be due to the deletion of carbonyls formed by EGCG during glycation.

EGCG has been found to reduce the glycation of elements of the cytoskeleton such as actin and tubulin.

Reduced glycation was accompanied by resumed tubulin assembly and increased actin extension, thereby improving neuronal structural integrity.

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DOI – https: //doi.Organization/10.18632 /onkoziel.27963

Full text – https: //www.onkoziel.com /Items/27963 /Text/

Correspondence – Subashchandrabose Chinnathambi – [email protected]

keywords
Alzheimer’s disease,
Tau protein,
Tau PTMs,
Tau glycation,
Inhibition of tau glycation

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