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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fu, Wen Jhamandas, Jack H. Shi, Diya Westaway, David |
| Description | Author Affiliation: Fu W ( From the Division of Neurology, Department of Medicine, Institute of Neuroscience and Mental Health, University of Alberta, Edmonton, Alberta T6G 2S2, Canada.); Shi D ( From the Division of Neurology, Department of Medicine, Institute of Neuroscience and Mental Health, University of Alberta, Edmonton, Alberta T6G 2S2, Canada.); Westaway D ( From the Division of Neurology, Department of Medicine, Institute of Neuroscience and Mental Health, University of Alberta, Edmonton, Alberta T6G 2S2, Canada Department of Biochemistry, and.); Jhamandas JH ( From the Division of Neurology, Department of Medicine, Institute of Neuroscience and Mental Health, University of Alberta, Edmonton, Alberta T6G 2S2, Canada jack.jhamandas@ualberta.ca.) |
| Abstract | Alzheimer disease (AD) is characterized neuropathologically by synaptic disruption, neuronal loss, and deposition of amyloid ß (Aß) protein in brain structures that are critical for memory and cognition. There is increasing appreciation, however, that astrocytes, which are the major non-neuronal glial cells, may play an important role in AD pathogenesis. Unlike neurons, astrocytes are resistant to Aß cytotoxicity, which may, in part, be related to their greater reliance on glycolytic metabolism. Here we show that, in cultures of human fetal astrocytes, pharmacological inhibition or molecular down-regulation of a main enzymatic regulator of glycolysis, 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase (PFKFB3), results in increased accumulation of Aß within and around astrocytes and greater vulnerability of these cells to Aß toxicity. We further investigated age-dependent changes in PFKFB3 and astrocytes in AD transgenic mice (TgCRND8) that overexpress human Aß. Using a combination of Western blotting and immunohistochemistry, we identified an increase in glial fibrillary acidic protein expression in astrocytes that paralleled the escalation of the Aß plaque burden in TgCRND8 mice in an age-dependent manner. Furthermore, PFKFB3 expression also demonstrated an increase in these mice, although at a later age (9 months) than GFAP and Aß. Immunohistochemical staining showed significant reactive astrogliosis surrounding Aß plaques with increased PFKFB3 activity in 12-month-old TgCRND8 mice, an age when AD pathology and behavioral deficits are fully manifested. These studies shed light on the unique bioenergetic mechanisms within astrocytes that may contribute to the development of AD pathology. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 20 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-05-15 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alzheimer Disease Metabolism Amyloid Beta-Peptides Astrocytes Energy Metabolism Phosphofructokinase-2 Aging Genetics Pathology Physiopathology Animals Behavior, Animal Gene Expression Regulation Glial Fibrillary Acidic Protein Mice Mice, Transgenic Nerve Tissue Proteins Biosynthesis Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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