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crystallin/sHSP is required for mitochondrial function in human ocular tissue
| Title: | aB- crystallin/sHSP is required for mitochondrial function in human ocular tissue. |
 81 views 11 downloads |
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| Name(s): |
McGreal, Rebecca. 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: | 2012 | |
| Publisher: | Florida Atlantic University | |
| Physical Form: | electronic | |
| Extent: | x, 85 p. : ill. (some col.) | |
| Language(s): | English | |
| Summary: | The central premise of this dissertation is that the small heat shock protein (sHSP), (Sa(BB-crystallin is essential for lens and retinal pigmented epithelial (RPE) cell function and oxidative stress defense. To date, the mechanism by which it confers protection is not known. We hypothesize that these functions could occur through its ability to protect mitochondrial function in lens and RPE cells. To test this hypothesis, we examined the expression of (Sa(BB-crystallin/sHSP in lens and RPE cells, we observed its localization in the cells, we examined translocation to the mitochondria in these cells upon oxidative stress treatment, we determined its ability to form complexes with and protect cytochrome c (cyt c) against damage, and we observed its ability to preserve mitochondrial function under oxidative stress conditions in lens and RPE cells. In addition to these studies, we examined the effect of mutations of (Sa(BB-crystallin/sHSP on its cellular localization and translocation patterns under oxidative stress, its in vivo and in vitro chaperone activity, and its ability to protect cyt c against oxidation. Our data demonstrated that (Sa(BB-crystallin/sHSP is expressed at high levels in the mitochondria of lens and RPE cells and specifically translocates to the mitochondria under oxidative stress conditions. We demonstrate that (Sa(BB-crystallin/sHSP complexes with cyt c and protects it against oxidative inactivation. Finally, we demonstrate that (Sa(BB-crystallin/sHSP directly protects mitochondria against oxidative inactivation in lens and RPE cells. Since oxidative stress is a key component of lens cataract formation and age-related macular degeneration (AMD), these data provide a new paradigm for understanding the etiology of these diseases. | |
| Identifier: | 794912752 (oclc), 3342242 (digitool), FADT3342242 (IID), fau:3889 (fedora) | |
| Note(s): |
by Rebecca McGreal. Vita. Thesis (Ph.D.)--Florida Atlantic University, 2012. Includes bibliography. Electronic reproduction. Boca Raton, Fla., 2012. Mode of access: World Wide Web. |
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| Subject(s): |
Mitochondrial pathology Chemical mutagenesis Oxidative stress -- Prevention Cellular signal transduction Eye -- Diseases -- Etiology Molecular chaperones |
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| Persistent Link to This Record: | http://purl.flvc.org/FAU/3342242 | |
| Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
| Host Institution: | FAU |
