Transfection with GSK-3? in vivo induces tau hyperphosphorylation at PHF-1 sites*
- VernacularTitle:在体转染GSK-3?引起tau蛋白在PHF-1位点的过度磷酸化(英文)
- Author:
Honglian LI
;
Shaohui WANG
;
Xiaomei LIAO
;
Xiaochuan WANG
;
Qun WANG
;
Jianzhi WANG
- Publication Type:Journal Article
- Keywords:
Glycogen synthase kinase 3;
Tau proteins;
Hyperphosphorylation
- From:
Chinese Journal of Pathophysiology
1986;0(03):-
- CountryChina
- Language:Chinese
-
Abstract:
AIM: To probe into tau hyperphosphorylation at PHF-1 sites induced by glycogen synthase kinase-3? (GSK-3?) in vivo. METHODS: Twenty-one rats were randomly allocated to three groups as follows: GSK-3? transfection group, vector group and control group; 0.1 ?g/3 ?L GSK-3?-HA plasmid or vector was injected bilaterally into cerebrum of the rats respectively, rats without injection were controls. Western blotting and immunohistochemical staining of cortex were carried out to detect the expression of GSK-3?-HA plasmid and tau phosphorylation using phosphorylation-dependent tau antibody PHF-1. RESULTS: After transfection with GSK-3?-HA for 48 h, GSK-3?-HA was expressed in GSK-3? transfection group; and hyperphosphorylated tau at PHF-1 sites accumulated in neurons in the transfected areas. The hyperphosphorylated tau colocalized largely with GSK-3? expressed by the transfected GSK-3? plasmid. CONCLUSIONS: Transfection with GSK-3? in vivo can induce tau hyperphosphorylation involving the pathogenesis of neurodegenerative disorders. These data further prove that GSK-3? is a key kinase to induce tau hyperphosphorylation and may be a therapeutic target for tauopathy-related neurodegenerative diseases.
