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Microtubule severing protein expression in Alzheimer's disease animal models
Journal article   Open access   Peer reviewed

Microtubule severing protein expression in Alzheimer's disease animal models

Sara Ansaloni, Robert Nichols, Peter W. Baas and Aleister J. Saunders
Alzheimer's & dementia, v 4(4S Part 23), pp T753-T753
Jul 2008
DOI: https://doi.org/10.1016/j.jalz.2008.05.2347
url
https://doi.org/10.1016/j.jalz.2008.05.2347View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze),  Open

Abstract

Background Alzheimer's disease (AD) is characterized by extensive neuronal death that causes progressive memory loss. Accumulation of Aβ aggregates and neurofibrillary tangles are believed to be responsible for AD-associated neurodegeneration. Aβ is a toxic peptide generated by the enzymatic cleavage of APP which can aggregate inside or outside the neurons. Neurofibrillary tangles are formed when the Tau protein, a microtubule (MT) associated protein, is hyper-phosphorylated. Hyper-phosphorylated Tau cannot bind MTs. Failure of Tau binding to MTs causes destabilization by increased de-polymerization. Potentially, Tau-deprived MTs are also more accessible to severing proteins. In fact, Tau has been shown to protect MTs from severing by katanin and spastin. Methods We hypothesize that levels of katanin and spastin might differ between control and transgenic mouse models of AD. To test this hypothesis we performed Western Blot analysis of cortex and hippocampus tissue isolated from transgenic and control mice. Results We found that katanin levels are decreased in triple transgenic animals. Regulation of katanin levels might be a defense mechanism to avoid further cytoskeleton degeneration. Conclusions This observation is completely new and might indicate targeting of severing proteins as a possible therapeutic strategy for AD.

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