Suppressing poly(ADP-ribose)polymerase-1 inhibits tau phosphorylation in HEK293/tau441 cells.
- Author:
Qin-Hao CHEN
1
;
Xiao-Mei LIAO
;
Shao-Hui WANG
Author Information
1. College of Life Science, Huazhong Normal University, Wuhan 430079, China.
- Publication Type:Journal Article
- MeSH:
Benzamides;
pharmacology;
Depression, Chemical;
Glycogen Synthase Kinase 3;
metabolism;
HEK293 Cells;
Humans;
Phosphorylation;
Poly (ADP-Ribose) Polymerase-1;
Poly(ADP-ribose) Polymerase Inhibitors;
Poly(ADP-ribose) Polymerases;
metabolism;
tau Proteins;
metabolism
- From:
Acta Physiologica Sinica
2011;63(6):511-516
- CountryChina
- Language:Chinese
-
Abstract:
The study aimed to investigate the effect of inhibition of poly(ADP-ribose) polymerase-1 (PARP-1) activity on tau phosphorylation in HEK293/tau441 cells and its mechanism. HEK293/tau441 cells were treated with 3-aminobenzamide (3-AB), a PARP-1 inhibitor, at different doses (0.5, 1, 2, 4 mmol/L). After 24 h, the cell morphology was observed under phase contrast microscope, tau phosphorylation level in different sites (tau-1, tau-5, Thr231) and the activity of glycogen synthase kinase 3 (GSK-3) were detected by Western blotting. The results showed: (1) 3-AB at different doses failed to change the morphology of cells; (2) The 3-AB-induced decrease in activity of PARP-1 resulted in increase of unphosphorylation level in tau-1(Ser195/198/199/202) sites; (3) The phosphorylation of tau was decreased in Thr231 site, while the total tau was slightly changed after 3-AB treatment; (4) With the increased phosphorylation of GSK-3 at Ser9 site, the activity of GSK-3 was decreased after 3-AB treatment. The results suggest that the inhibition of PARP-1 by 3-AB could decrease tau phosphorylation in HEK293/tau441 cells probably through decreasing GSK-3 activity.
