PubMed: 26095350

Title
Ribosylation triggering Alzheimer's disease-like Tau hyperphosphorylation via activation of CaMKII.
Journal
Aging cell
Volume
14
Issue
None
Pages
754-63
Date
2015-10-01
Authors
Han C | He R | Liu Y | Su T | Wang Y | Wei Y | Wu B

Evidence 958f465de1

Here, we show for the first time that the administration of D-ribose, the most active glycator among monosaccharides, produces high levels of advanced glycation end products (AGEs) and, importantly, triggers hyperphosphorylation of Tau in the brain of C57BL/6 mouse and neuroblastoma N2a cells.

Evidence 569789dfe3

The treatment of 10 mM D-ribose for 24 h resulted in a significant increase in active form of CaMKII (p-Thr286/287), yet simultaneously in a decrease in inactive form of CaMKII (p-Thr305/306) phosphorylation (Fig. 4e). The enzyme activity assay supported this result.

Evidence 714b87df54

Thus, our results suggest that Tau hyperphosphorylation was a result of ribosylated AGEs, rather than due to a direct reaction involving D-ribose.

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