Glycogen synthase kinase-3β-mediated tau phosphorylation in cultured cell lines

Chris Wing Cheung Lee, Kwok Fai Lau, Christopher C.J. Miller, Pang Chui Shaw

Research output: Contribution to journalArticlepeer-review

59 Scopus citations


To study further the role of glycogen synthase kinase-3β on tau phosphorylation, glycogen synthase kinase-3β and tau expression vectors were co-transfected into CHO-K1, COS-7 and SH-SY5Y cell. Tau phosphorylation was assessed by phosphorylation-dependent antibodies AT-8, AT-180, AT-270 and PHF-1. The AT-270 and AT-8 epitopes were consistently phosphorylated by glycogen synthase kinase-3β in the three cell lines. Phosphorylation on AT-180 epitope was significant in CHO-K1 and SH-SY5Y cells while PHF-1 epitope was hyper-phosphorylated only in SH-SY5Y cells. We also found that lithium induces phosphorylation of the serine 9 residue of glycogen synthase kinase-3β together with inhibition of tau phosphorylation on PHF-1 epitope in all the three cell lines. This suggests a novel mechanism whereby lithium-mediated inhibition of GSK-3β activity influences tau phosphorylation.

Original languageEnglish (US)
Pages (from-to)257-260
Number of pages4
Issue number2
StatePublished - Feb 10 2003


  • Alzheimer's disease
  • CHO-K1
  • COS-7
  • Glycogen synthase kinase-3 beta
  • SH-SY5Y
  • Tau phosphorylation

ASJC Scopus subject areas

  • General Neuroscience


Dive into the research topics of 'Glycogen synthase kinase-3β-mediated tau phosphorylation in cultured cell lines'. Together they form a unique fingerprint.

Cite this