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    • Graduate School - MU Theses and Dissertations (MU)
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    • 2008 Dissertations (MU)
    • 2008 MU dissertations - Access restricted to MU
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    Amyloid beta induces cPLA2 activation by an NADPH oxidase-dependent mechanism in neurons

    Shelat, Phullara B., 1978-
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    [PDF] research.pdf.pdf (3.477Mb)
    Date
    2008
    Format
    Thesis
    Metadata
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    Abstract
    [ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] Alzheimer's disease (AD) is a neurodegenerative disorder affecting more than 20 million people worldwide. An increase in production of amyloid beta peptides (A[Beta]) and their aggregation to the oligomeric form is thought to contribute to neurotoxicity in the AD brain. cPLA2 is an enzyme responsible for hydrolysis of fatty acids in the sn-2 position of membrane phospholipids. Substantial attention has been paid to arachidonic acid (AA) because this lipid mediator is not only used for prostanoid synthesis but is also regarded as a retrograde transmitter. cPLA2 has been implicated in the pathogenesis of a number of neurodegenerative diseases including AD. Recent studies provided evidence for the production of reactive oxygen species (ROS) in association with glutamate excitotoxicity and involvement of NMDA receptors in A[Beta]-induced neurotoxicity. This study is focused on elucidating the role of NADPH oxidase, a superoxide producing enzyme, on the signaling pathway leading to cPLA2 activation and AA release in cortical neurons. Results show that A[Beta] and NMDA can produce ROS in neurons via NADPH oxidase and that this pool of ROS is important for ERK1/2 phosphorylation, cPLA2 phosphorylation and subsequent AA release. The study presented here identifies for the first time the importance of the ROS producing enzyme NADPH oxidase in the signaling pathway leading to A[Beta]-induced and NMDA receptor-mediated cPLA2 activation in neurons. This novel mechanism may contribute to a better understanding of the oxidative mechanism underlying the pathogenesis of AD.
    URI
    https://hdl.handle.net/10355/7205
    https://doi.org/10.32469/10355/7205
    Degree
    Ph. D.
    Thesis Department
    Biochemistry (MU)
    Rights
    Access is limited to the campus of the University of Missouri--Columbia.
    Collections
    • 2008 MU dissertations - Access restricted to MU
    • Biochemistry electronic theses and dissertations (MU)
    • Biochemistry electronic theses and dissertations (MU)

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