Human fetal tau protein isoform: Possibilities for Alzheimer's disease treatment

Nataša Jovanov-Milošević, Davor Petrović, Goran Sedmak, Mario Vukšić, Patrick R. Hof, Goran Šimić

Research output: Contribution to journalShort surveypeer-review

27 Scopus citations


While early 1990s reports showed the phosphorylation pattern of fetal tau protein to be similar to that of tau in paired helical filaments (PHF) in Alzheimer's disease (AD), neither the molecular mechanisms of the transient developmental hyperphosphorylation of tau nor reactivation of the fetal plasticity due to re-expression of fetal protein kinases in the aging and AD human brain have been sufficiently investigated. Here, we summarize the current knowledge on fetal tau, adding new data on the specific patterns of tau protein and mRNA expression in the developing human brain as well as on change in tau phosphorylation in the perforant pathway after entorhinal cortex lesion in mice. As fetal tau isoform does not form PHF even in a highly phosphorylated state, understanding its expression and post-translational modifications represents an important avenue for future research towards the development of AD treatment and prevention.

Original languageEnglish
Pages (from-to)1290-1294
Number of pages5
JournalInternational Journal of Biochemistry and Cell Biology
Issue number8
StatePublished - Aug 2012


  • Ageing
  • Brain development
  • Deafferentation
  • Entorhinal cortex lesion
  • Mild cognitive impairment
  • Paired helical filaments-PHF
  • Tau potein kinases


Dive into the research topics of 'Human fetal tau protein isoform: Possibilities for Alzheimer's disease treatment'. Together they form a unique fingerprint.

Cite this