Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells
- 20 November 1995
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 375 (3) , 243-248
- https://doi.org/10.1016/0014-5793(95)01221-y
Abstract
The axonal microtubule‐associated protein, tau, is thought to play an important role in axonal growth and in the establishment of neuronal polarity. In adult human brain there are six alternatively spliced tau isoforms, which have different microtubule binding affinities in vitro. The tubulin‐tau interaction is further modified by phosphorylation of tau and, compared to adult brain tau, both foetal brain tau and paired helical filament (PHF) tau, characteristic of Alzheimer's disease, are hyperphosphorylated. In vivo both the expression of tau isoforms and their phosphorylation states are developmentally regulated. In order to establish the correlation between the expression of tau isoforms and their pattern of phosphorylation, we have characterised these two features in several in vitro models of neuronal differentiation, including the human neuroblastoma cell lines, SK‐N‐SH, SH‐SY5Y and IMR32 cells, rat PC12 cells and primary rat cortical neurones. Sensitive RT‐PCR analysis revealed a different complement of tau isoforms in the different cell lines and neuritogenesis was associated mainly with an increase in the overall tau protein level with no apparent phosphorylation changes. A switch in tau isoform expression occurred only at the terminal stages of neuronal development, when it may be important in reinforcing the previously established axonal cytoarchitecture.Keywords
This publication has 33 references indexed in Scilit:
- Abnormally phosphorylated tau in SY5Y human neuroblastoma cellsFEBS Letters, 1995
- τ Phosphorylation in Human, Primate, and Rat Brain: Evidence that a Pool of τ Is Highly Phosphorylated In Vivo and Is Rapidly Dephosphorylated In VitroJournal of Neurochemistry, 1994
- Developmental Changes in τ Phosphorylation: Fetal τ Is Transiently Phosphorylated in a Manner Similar to Paired Helical Filament‐τ Characteristic of Alzheimer's DiseaseJournal of Neurochemistry, 1993
- Okadaic Acid Induces Early Changes in Microtubule‐Associated Protein 2 and γ Phosphorylation Prior to Neurodegeneration in Cultured Cortical NeuronsJournal of Neurochemistry, 1993
- Abnormal tau phosphorylation at Ser396 in alzheimer's disease recapitulates development and contributes to reduced microtubule bindingNeuron, 1993
- τ Protein Kinase II Is Involved in the Regulation of the Normal Phosphorylation State of τ ProteinJournal of Neurochemistry, 1993
- Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tauFEBS Letters, 1992
- Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinaseNeuroscience Letters, 1992
- Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's diseaseFEBS Letters, 1992
- Developmentally regulated expression of specific tau sequencesPublished by Elsevier ,1989