Master of Science
Dr. Greg Kelly
Nucleoredoxin is a redox sensitive protein recently shown to be involved in the Wnt/β-catenin pathway through binding dishevelled. When Wnt is present, dishevelled prevents a destruction complex from degrading β-catenin. This facilitates the translocation of β-catenin into the nucleus where it binds to TCF-LEF to impart changes in gene expression. This study used mouse F9 cells as a model to examine whether or not nucleoredoxin is involved in augmenting the Wnt/β-catenin signaling required for extraembryonic endoderm differentiation. It was found that nucleoredoxin and three dishevelled isoforms were present in F9 cells. Furthermore, nucleoredoxin was found to bind to dishevelled-2, and when cells were treated with an oxidizing agent this interaction diminished. Lastly, when nucleoredoxin expression was knocked down, F9 cells differentiated into extraembryonic endoderm. Together, the data would indicate that the Wnt/β-catenin signaling pathway obligatory for extraembryonic endoderm differentiation is redox regulated at the level of nucleoredoxin.
Sandieson, Leanne, "Nucleoredoxin and Wnt signaling in F9 cells" (2012). Electronic Thesis and Dissertation Repository. 977.