Shinobu C. Fujita

TL;DR: The results demonstrate that the activation of TPKI/GSK3β and cdk5 is not necessary to obtain hyperphosphorylated tau in vivo, and indicate that inhibition of PP2A is likely the dominant factor in inducing tau hyperph phosphorylation in the starved mouse, overriding the inhibition of key tau kinases.

TL;DR: This study demonstrates that the cholesterol release is mediated by endogenously synthesized and secreted apoE isoforms and clarify the mechanism underlying this isoform-dependent cholesterol release, and provides a new insight into the issue concerning the putative alteration of apolipoprotein E-related cholesterol metabolism in Alzheimer's disease.

TL;DR: Results indicate that the new splice isoform has a different function, and it is indicated that TPKI2/GSK3β2 occurs predominantly in the neuronal soma, while TPKI1/GSk3β1 is found both in the soma and processes.

TL;DR: Findings indicate that τ is one of the physiological substrates of TPKI and suggest that the enzyme plays an important role in the growth of axons during development of the brain.

TL;DR: Food deprivation of mice for 1 to 3 days progressively enhanced tau hyperphosphorylation in the hippocampus, to a lesser extent in the cerebral cortex, but the effect was least in the cerebellum, in correspondence with the regional selectivity of tauopathy in Alzheimer's disease.