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Methionine sulfoxide reductase A (MsrA) and aging in the anoxia-tolerant freshwater turtle (Trachemys scripta)

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Date Issued:
2010
Summary:
The enzyme Methionine sulfoxide reductase A (MsrA) repairs oxidized proteins, and may act as a scavenger of reactive oxygen species (ROS), making it a potential therapeutic target for age-related neurodegenerative diseases. The anoxia-tolerant turtle offers a unique model to observe the effects of oxidative stress on a system that maintains neuronal function following anoxia and reoxygenation, and that ages without senescence. MsrA is present in both the mitochondria and cytosol, with protein levels increasing respectively 3- and 4-fold over 4 hours of anoxia, and remaining 2-fold higher than basal upon reoxygenation. MsrA was knocked down in neuronally-enriched cell cultures via RNAi transfection. Propidium iodide staining showed no significant cell death during anoxia, but this increased 7-fold upon reoxygenation, suggesting a role for MsrA in ROS suppression during reperfusion. This is the first report in any system of MsrA transcript and protein levels being regulated by oxygen levels.
Title: Methionine sulfoxide reductase A (MsrA) and aging in the anoxia-tolerant freshwater turtle (Trachemys scripta).
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Name(s): Bruce, Lynsey Erin.
Charles E. Schmidt College of Science
Department of Biological Sciences
Type of Resource: text
Genre: Electronic Thesis Or Dissertation
Date Issued: 2010
Publisher: Florida Atlantic University
Physical Form: electronic
Extent: vi, 7-52 p. : ill.
Language(s): English
Summary: The enzyme Methionine sulfoxide reductase A (MsrA) repairs oxidized proteins, and may act as a scavenger of reactive oxygen species (ROS), making it a potential therapeutic target for age-related neurodegenerative diseases. The anoxia-tolerant turtle offers a unique model to observe the effects of oxidative stress on a system that maintains neuronal function following anoxia and reoxygenation, and that ages without senescence. MsrA is present in both the mitochondria and cytosol, with protein levels increasing respectively 3- and 4-fold over 4 hours of anoxia, and remaining 2-fold higher than basal upon reoxygenation. MsrA was knocked down in neuronally-enriched cell cultures via RNAi transfection. Propidium iodide staining showed no significant cell death during anoxia, but this increased 7-fold upon reoxygenation, suggesting a role for MsrA in ROS suppression during reperfusion. This is the first report in any system of MsrA transcript and protein levels being regulated by oxygen levels.
Identifier: 650308601 (oclc), 2683139 (digitool), FADT2683139 (IID), fau:3497 (fedora)
Note(s): by Lynsey Erin Bruce.
Thesis (M.S.)--Florida Atlantic University, 2010.
Includes bibliography.
Electronic reproduction. Boca Raton, Fla., 2010. Mode of access: World Wide Web.
Subject(s): Oxidation-reduction reaction
Proteins -- Chemical modification
Turtles -- Physiology
Oxygen -- Physiological effect
Aging -- Molecular aspects
Persistent Link to This Record: http://purl.flvc.org/FAU/2683139
Use and Reproduction: http://rightsstatements.org/vocab/InC/1.0/
Host Institution: FAU