TY - JOUR
T1 - Human fetal tau protein isoform
T2 - Possibilities for Alzheimer's disease treatment
AU - Jovanov-Milošević, Nataša
AU - Petrović, Davor
AU - Sedmak, Goran
AU - Vukšić, Mario
AU - Hof, Patrick R.
AU - Šimić, Goran
N1 - Funding Information:
This work was supported by grant no. 108-1081870-1872 (“Development of cortical connections in man”) and grant no. 108-1081870-1942 (A Phosphorylation of tau proteins in development and Alzheimer's disease”) from the Croatian Ministry of Science Education and Sports of Republic of Croatia , project no. 09/16 (“Detection and tracking of biological markers for early therapeutic intervention in sporadic Alzheimer's disease”) from Croatian Science Foundation, and in part by NIH grant AG05138 .
PY - 2012/8
Y1 - 2012/8
N2 - 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.
AB - 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.
KW - Ageing
KW - Brain development
KW - Deafferentation
KW - Entorhinal cortex lesion
KW - Mild cognitive impairment
KW - Paired helical filaments-PHF
KW - Tau potein kinases
UR - http://www.scopus.com/inward/record.url?scp=84861560498&partnerID=8YFLogxK
U2 - 10.1016/j.biocel.2012.05.001
DO - 10.1016/j.biocel.2012.05.001
M3 - Short survey
AN - SCOPUS:84861560498
SN - 1357-2725
VL - 44
SP - 1290
EP - 1294
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
IS - 8
ER -