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Mechanism of Tau hyperphosphorylation involving lysosomal enzyme asparagine endopeptidase in a mouse model of brain ischemia.

Basurto-Islas, Gustavo, Gu, Jin-hua, Tung, Yunn Chyn, Liu, Fei, Iqbal, Khalid·2018·Journal of Alzheimer’s Disease
DOI 10.3233/jad-170715
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Abstract

Dementias including Alzheimer’s disease (AD) are multifactorial disorders that involve several different etiopathogenic mechanisms. Cerebral ischemia has been suspected in the altered regulation of protein kinases and phosphatases that leads to hyperphosphorylation of tau and further neurofibrillary pathology, a key hallmark of AD and related neurodegenerative diseases. However, the deregulation of these enzymes and their relationship with ischemia and AD remain unclear. Previously, we reported a mechanism by which the lysosomal enzyme asparagine endopeptidase (AEP) is associated with brain acidosis and AD. In this study, we subjected mice to middle cerebral artery occlusion and found that compared with wild type mice, the ischemia-induced brain injury and motor deficit in AEP-knockout mice are reduced, probably because ischemia activates AEP. AEP cleaves inhibitor 2 of protein phosphatase 2A (I 2 PP2A), which translocates from the neuronal nucleus to the cytoplasm and produces hyperphosphorylation of tau through inhibition of PP2A. These findings suggest a possible mechanism of tau pathology associated with ischemia.

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Crossref · 10.3233/jad-170715

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Metadata

Authors
Basurto-Islas, G., Gu, J.-H., Tung, Y. C., Liu, F., & Iqbal, K.
Affiliations
Department of Neurochemistry, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY, USA
Venue
Journal of Alzheimer’s Disease
Publisher
SAGE Publications
Published
2018-04-24
Volume
63
Issue
2
Pages
821-833
ISSN
  • 1387-2877
  • 1875-8908
DOI
10.3233/jad-170715
Cited by
39
References
3
Language
en
Licence
journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)

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