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Methionine sulfoxide reductase A (MsrA) and aging in the anoxia-tolerant freshwater turtle (Trachemys scripta)
- 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 |
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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. |
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Subject(s): |
Oxidation-reduction reaction Proteins -- Chemical modification Turtles -- Physiology Oxygen -- Physiological effect Aging -- Molecular aspects |
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Persistent Link to This Record: | http://purl.flvc.org/FAU/2683139 | |
Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
Host Institution: | FAU |