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Int J Biochem Cell Biol. 2012 Aug;44(8):1290-4. doi: 10.1016/j.biocel.2012.05.001. Epub 2012 May 15.

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

Author information

  • 1Croatian Institute for Brain Research, University of Zagreb School of Medicine, Šalata 12, 10000 Zagreb, Croatia. njovanov@hiim.hr

Abstract

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.

Copyright © 2012 Elsevier Ltd. All rights reserved.

PMID:
22595282
[PubMed - indexed for MEDLINE]
PMCID:
PMC3572194
Free PMC Article

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