Neuron‐glia interactions: Molecular basis of alzheimer's disease and applications of neuroproteomics.
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| Title: | Neuron‐glia interactions: Molecular basis of alzheimer's disease and applications of neuroproteomics. |
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| Authors: | Ibrahim, Abdallah Mohammad (AUTHOR), Pottoo, Faheem Hyder (AUTHOR), Dahiya, Ekta Singh (AUTHOR), Khan, Firdos Alam (AUTHOR), Kumar, J. B. Senthil (AUTHOR) |
| Source: | European Journal of Neuroscience. Jul2020, Vol. 52 Issue 2, p2931-2943. 13p. 2 Diagrams, 2 Charts, 1 Graph. |
| Subjects: | Alzheimer's disease, Molecular interactions, Mass spectrometry, Cognition disorders, Neuroglia, Vascular dementia, Senile dementia |
| Abstract: | Neurodegenerative disorders present with progressive and irreversible degeneration of the neurons. Alzheimer's disease (AD) is one of the most common neurodegenerative disorders affecting 50 million people worldwide (2017), expected to be doubled every 20 years. Primarily affected by age, AD is the cause for old‐age dementia, progressive memory loss, dysfunctional thoughts, confusion, cognitive impairment and personality changes. Neuroglia formerly understood as "glue" of the brain neurons consists of macroglia (astrocytes and oligodendrocyte), microglia and progenitors NG2‐glia, and constitute a large fraction of the mammalian brain. The primary functions of glial cells are to provide neurons with metabolic and structural support in the healthy brain; however, they attain a "reactive" state from the "resting" state upon challenged with a pathological insult such as a neurodegenerative cascade. Failure or defects in their homoeostatic functions (i.e. concentration of ions, neurotransmitters) ultimately jeopardize neurons with excitotoxicity and oxidative stress. Moreover, the most common clinical outcome of AD is the cognitive impairment and memory loss, which are attributed mainly by the accumulation of Aβ. Failure of glial cells to remove the Aβ toxic proteins accelerates the AD progression. The rapidly emerging proteomic techniques such as mass spectrometry (MS), cross‐linking mass spectrometry, hydrogen deuterium trade mass spectrometry, protein foot printing and 2‐DGE combined with LC–MS/MS present wide array of possibilities for the identification of differentially expressed proteins in AD. [ABSTRACT FROM AUTHOR] |
| Copyright of European Journal of Neuroscience is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Psychology and Behavioral Sciences Collection |
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| Abstract: | Neurodegenerative disorders present with progressive and irreversible degeneration of the neurons. Alzheimer's disease (AD) is one of the most common neurodegenerative disorders affecting 50 million people worldwide (2017), expected to be doubled every 20 years. Primarily affected by age, AD is the cause for old‐age dementia, progressive memory loss, dysfunctional thoughts, confusion, cognitive impairment and personality changes. Neuroglia formerly understood as "glue" of the brain neurons consists of macroglia (astrocytes and oligodendrocyte), microglia and progenitors NG2‐glia, and constitute a large fraction of the mammalian brain. The primary functions of glial cells are to provide neurons with metabolic and structural support in the healthy brain; however, they attain a "reactive" state from the "resting" state upon challenged with a pathological insult such as a neurodegenerative cascade. Failure or defects in their homoeostatic functions (i.e. concentration of ions, neurotransmitters) ultimately jeopardize neurons with excitotoxicity and oxidative stress. Moreover, the most common clinical outcome of AD is the cognitive impairment and memory loss, which are attributed mainly by the accumulation of Aβ. Failure of glial cells to remove the Aβ toxic proteins accelerates the AD progression. The rapidly emerging proteomic techniques such as mass spectrometry (MS), cross‐linking mass spectrometry, hydrogen deuterium trade mass spectrometry, protein foot printing and 2‐DGE combined with LC–MS/MS present wide array of possibilities for the identification of differentially expressed proteins in AD. [ABSTRACT FROM AUTHOR] |
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| ISSN: | 0953816X |
| DOI: | 10.1111/ejn.14838 |
