发布时间：

2025-04-30

论文名称：

Phospholipid transfer protein reduces phosphorylation of tau in human neuronal cells.

发表刊物：

J Neurosci Res

摘要：

Tau function is regulated by phosphorylation, and
abnormal tau phosphorylation in neurons is one of the
key processes associated with development of Alzheimer’s
disease and other tauopathies. In this study we
provide evidence that phospholipid transfer protein
(PLTP), one of the main lipid transfer proteins in the
brain, significantly reduces levels of phosphorylated tau
and increases levels of the inactive form of glycogen
synthase kinase-3b (GSK3b) in HCN2 cells. Furthermore,
inhibition of phosphatidylinositol-3 kinase (PI3K)
reversed the PLTP-induced increase in levels of GSK3b
phosphorylated at serine 9 (pGSK3bSer9) and partially
reversed the PLTP-induced reduction in tau phosphorylation.
We provide evidence that the PLTP-induced
changes are not due to activation of Disabled-1 (Dab1),
insofar as PLTP reduced levels of total and phosphorylated
Dab1 in HCN2 cells. We have also shown that inhibition
of tyrosine kinase activity of insulin receptor (IR)
and/or insulin-like growth factor 1 (IGF1) receptor
(IGFR) reverses the PLTP-induced increase in levels of
phosphorylated Akt (pAktThr308 and pAktSer473), suggesting
that PLTP-mediated activation of the PI3K/Akt
pathway is dependent on IR/IGFR receptor tyrosine kinase
activity. Our study suggests that PLTP may be an
important modulator of signal transduction pathways in
human neurons.

合写作者：

Dong W, Albers JJ, Vuletic S

卷号：

2009-87

页面范围：

3176-3185

是否译文：

否

发表时间：

2009-05-06