PubMed: 26655600

Title
Glycation alter the process of Tau phosphorylation to change Tau isoforms aggregation property.
Journal
Biochimica et biophysica acta
Volume
1862
Issue
None
Pages
192-201
Date
2016-02-01
Authors
Deng Y | Iqbal J | Li L | Liu K | Liu Y | Qin P | Qing H

Evidence c494fa850e

However, granule cells of the dentate gyrus mainly express 3R isoforms, which resist Tau aggregation in AD, but accumulate 3R aggregates in Pick's disease [14]. 3R Tau is a major Tau isoform in laser microdissected Pick bodies [15].

Evidence 5bc641bf18

The results show that 4R2N and 3R2N Tau increase their aggregation extent with glycation while 3R1N decreases aggregation properties with glycation

Evidence be144361a5

Despite 4R1N having no significant change, the same modified 4R2N Tau promotes its aggregation significantly (Fig. 6A, C, E).

Evidence f39fb0d431

Glycation and phosphorylation of both 4R1Nand 4R0NTau reduce its aggregation.

Evidence 14884534e7

On the other hand, the MS analysis shows that in the combined reaction of 4R2N Tau the level of phosphorylation is increased and the level of glycation is decreased.

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.