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《医学前沿(英文)》 >> 2008年 第2卷 第3期 doi: 10.1007/s11684-008-0044-8

Effect of inhibiting tyrosine kinase Src expression on protein phosphatase 2A and tau phosphorylation

1.Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology; Karolinska Institutet, KI-Alzheimer Disease Research Center (KI-ADRC); 2.Clinical Laboratory of Union Hospital, Tongji Medical College, Huazhong University of Science and Technology; 3.Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology; 4.Karolinska Institutet, KI-Alzheimer Disease Research Center (KI-ADRC);

发布日期: 2008-09-05

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摘要

The aim of this study is to investigate the effect of tyrosine kinase Src on Tyrosine 307(Y307) phosphorylation, protein phosphatase 2A (PP2A) activity, and on tau phosphorylation. Specific Src siRNA was transfected into cultured mouse neuroblastoma N2a cells to inhibit the expression of Src protein, and the phosphorylation levels of PP2A Y307 and tau at different sites, as well as PP2A activity were detected at different time points after siRNA transfection. Twelve hours after siRNA transfection, the protein level of Src was dramatically decreased, with decreased PP2A Y307 phosphorylation. However, the total PP2A protein level was also decreased, together with a decreased PP2A activity. Tau was hyperphosphorylated at the Ser198/199/202 sites. Multiple factors may be involved in the cellular regulation of PP2A activity. Inhibiting Src expression could induce inactivation of PP2A and tau hyperphosphorylation.

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