| Alzheimer's disease-specific tau phosphorylation is induced by herpes simplex virus type 1. | |
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MedLine Citation:
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PMID: 19221424 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Neurofibrillary tangles are one of the main neuropathological features of Alzheimer's disease (AD) and are composed of abnormally phosphorylated forms of a microtubule-associated protein called tau. What causes this abnormal phosphorylation is unknown. Our previous studies have implicated herpes simplex virus type 1 (HSV1) as an etiological agent in AD, and so we investigated whether infection with this virus induces AD-like tau phosphorylation. Here we demonstrate that HSV1 causes tau phosphorylation at several sites, including serine 202, threonine 212, serine 214, serine 396 and serine 404. In addition, we have elucidated the mechanism involved by showing that the virus induces glycogen synthase kinase 3beta and protein kinase A, the enzymes that cause phosphorylation at these sites. Our data clearly reveal the importance of HSV1 in AD-type tau phosphorylation, and support the case that the virus is a cause of the disease. Together with our previous data, our results point to the use of antiviral agents to slow the progression of the disease. |
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Authors:
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Matthew A Wozniak; Alison L Frost; Ruth F Itzhaki |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of Alzheimer's disease : JAD Volume: 16 ISSN: 1387-2877 ISO Abbreviation: J. Alzheimers Dis. Publication Date: 2009 |
Date Detail:
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Created Date: 2009-02-17 Completed Date: 2009-06-17 Revised Date: 2010-10-22 |
Medline Journal Info:
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Nlm Unique ID: 9814863 Medline TA: J Alzheimers Dis Country: Netherlands |
Other Details:
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Languages: eng Pagination: 341-50 Citation Subset: IM |
Affiliation:
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Faculty of Life Sciences, The University of Manchester, Manchester, UK. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Line, Tumor Enzyme-Linked Immunosorbent Assay / methods Glycogen Synthase Kinase 3 / metabolism Herpesvirus 1, Human / physiology* Humans Infection Neuroblastoma / metabolism, virology Phosphorylation Serine / metabolism Threonine / metabolism tau Proteins / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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//Biotechnology and Biological Sciences Research Council |
| Chemical | |
Reg. No./Substance:
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0/tau Proteins; 56-45-1/Serine; 72-19-5/Threonine; EC 2.7.11.26/Glycogen Synthase Kinase 3 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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