Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy.

ABSTRACT:

Aim

Tau protein is a prominent component of paired helical filaments in Alzheimer's disease (AD) and other tauopathies. While the abnormal phosphorylation of tau on serine and threonine has been well established in the disease process, its phosphorylation on tyrosine has only recently been described. We previously showed that the Src family non-receptor tyrosine kinases (SFKs) Fyn and Src phosphorylate tau on Tyr18 and that phospho-Tyr18-tau was present in AD brain. In this study, we have investigated the appearance of phospho-Tyr18-tau, activated SFK and proliferating cell nuclear antigen (PCNA) during disease progression in a mouse model of human tauopathy.

Methods

We have used JNPL3, which expresses human tau with P301L mutation, and antibodies specific for phospho-Tyr18-

SUBMITTER: Bhaskar K 

PROVIDER: S-EPMC2939304 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature