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Oxidative stress induces transient O-GlcNAc elevation and tau dephosphorylation in SH-SY5Y cells.
- Source :
-
Journal of cellular and molecular medicine [J Cell Mol Med] 2016 Dec; Vol. 20 (12), pp. 2269-2277. Date of Electronic Publication: 2016 Jul 26. - Publication Year :
- 2016
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Abstract
- O-linked β-N-acetlyglucosamine or O-GlcNAc modification is a dynamic post-translational modification occurring on the Ser/Thr residues of many intracellular proteins. The chronic imbalance between phosphorylation and O-GlcNAc on tau protein is considered as one of the main hallmarks of Alzheimer's disease. In recent years, many studies also showed that O-GlcNAc levels can elevate upon acute stress and suggested that this might facilitate cell survival. However, many consider chronic stress, including oxidative damage as a major risk factor in the development of the disease. In this study, using the neuronal cell line SH-SY5Y we investigated the dynamic nature of O-GlcNAc after treatment with 0.5 mM H <subscript>2</subscript> O <subscript>2</subscript> for 30 min. to induce oxidative stress. We found that overall O-GlcNAc quickly increased and reached peak level at around 2 hrs post-stress, then returned to baseline levels after about 24 hrs. Interestingly, we also found that tau protein phosphorylation at site S262 showed parallel, whereas at S199 and PHF1 sites showed inverse dynamic to O-Glycosylation. In conclusion, our results show that temporary elevation in O-GlcNAc modification after H <subscript>2</subscript> O <subscript>2</subscript> -induced oxidative stress is detectable in cells of neuronal origin. Furthermore, oxidative stress changes the dynamic balance between O-GlcNAc and phosphorylation on tau proteins.<br /> (© 2016 The Authors. Journal of Cellular and Molecular Medicine published by John Wiley & Sons Ltd and Foundation for Cellular and Molecular Medicine.)
- Subjects :
- Cell Line, Tumor
Cell Survival drug effects
Fluorescent Antibody Technique
Glycosylation drug effects
Humans
Hydrogen Peroxide toxicity
N-Acetylglucosaminyltransferases genetics
N-Acetylglucosaminyltransferases metabolism
Nitrogenous Group Transferases genetics
Nitrogenous Group Transferases metabolism
Phosphorylation drug effects
RNA, Messenger genetics
RNA, Messenger metabolism
Real-Time Polymerase Chain Reaction
Time Factors
Acetylglucosamine metabolism
Oxidative Stress drug effects
tau Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1582-4934
- Volume :
- 20
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Journal of cellular and molecular medicine
- Publication Type :
- Academic Journal
- Accession number :
- 27456536
- Full Text :
- https://doi.org/10.1111/jcmm.12910