Human fetal tau protein isoform: possibilities for Alzheimer's disease treatment |
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| Authors: | Jovanov-Milo?evi? Nata?a Petrovi? Davor Sedmak Goran Vuk?i? Mario Hof Patrick R Simi? Goran |
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| Institution: | 1. Department of Laboratory Medicine, Sundsvall County Hospital, Sweden;2. Department of Research and development, Sundsvall County Hospital, Sweden;3. Department of Natural Sciences, Mid Sweden University, Sundsvall, Sweden;1. McKnight Brain Institute, Department of Neurology, University of Florida, Gainesville, FL 32611, USA;2. Department of Neuroscience and Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, FL 32611, USA;3. Genetics Institute, University of Florida, Gainesville, FL 32611, USA |
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| 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. |
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