Jul 10, 2018

Prion-Like Propagation of Post-Translationally Modified Tau in Alzheimer's Disease: A Hypothesis

Journal of Molecular Neuroscience : MN
Shweta Kishor Sonawane, Subashchandrabose Chinnathambi

Abstract

The microtubule-associated protein Tau plays a key role in the neuropathology of Alzheimer's disease by forming intracellular neurofibrillary tangles. Tau in the normal physiological condition helps stabilize microtubules and transport. Tau aggregates due to various gene mutations, intracellular insults and abnormal post-translational modifications, phosphorylation being the most important one. Other modifications which alter the function of Tau protein are glycation, nitration, acetylation, methylation, oxidation, etc. In addition to forming intracellular aggregates, Tau pathology might spread in a prion-like manner as revealed by several in vitro and in vivo studies. The possible mechanism of Tau spread can be via bulk endocytosis of misfolded Tau species. The recent studies elucidating this mechanism have mainly focussed on the aggregation and spread of repeat domain of Tau in the cell culture models. Further studies are needed to elucidate the prion-like propagation property of full-length Tau and its aggregates in a more intense manner in vitro as well as in vivo conditions. Varied post-translational modifications can have discrete effects on aggregation propensity of Tau as well as its propagation. Here, we review the pri...Continue Reading

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Mentioned in this Paper

Study
Familial Alzheimer Disease (FAD)
In Vivo
Endocytosis
Protein Methylation
Glycate
Neurofibrillary Degeneration (Morphologic Abnormality)
Post-Translational Protein Processing
Protoplasm
Aggregation

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