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Date of Award
Bachelor of Science (BS)
Department of Biology
To maintain viability, cells must resolve misfolded protein stress; the inability to do so often triggers cell death, most notably in neurons during neurodegenerative disease. The NAC is a highly conserved translational chaperone essential for protein folding and localization to organelles throughout the cell. In C. elegans, depletion of the NAC initiates misfolded protein stress specifically in the endoplasmic reticulum, inducing a response that upregulates the HSP-4 chaperone in an attempt to prevent cell death. This upregulation is robust but not uniform, and deficient in regions containing neurons. We are characterizing this non-uniform stress response to determine if HSP-4 upregulation is cell-specific and correlates with survival. Additionally, there is evidence that the NAC may function in engaging premature and/or atypical differentiation under stress conditions. We’ve developed a protocol that characterizes the differentiation patterns and stress responses in NAC-depleted C. elegans. Our results indicate that NAC-depleted C. elegans have altered gut cell differentiation patterns when compared to control treatments. Furthermore, control studies were conducted to determine baseline patterns of HSP-4 expression in relation to the location of gut cells. Future studies will investigate differentiation patterns of muscle and neuronal cells in NAC-depleted C. elegans as well as characterizing the upregulation of HSP-4 in gut, muscle, and neuronal cells within NAC-depleted C. elegans.
Matson, Courtney A. and Wallace, Erin N., "Characterization of Cell-type Specific Responses in C. elegans Experiencing Misfolded Protein Stress: How Do Some Cells Save Themselves While Others Die?" (2015). Senior Honors Projects, 2010-current. 44.