Department
Sciences & Mathematics
Format of Presentation
Oral Presentation
Research Category
STEM
Description
Cystic fibrosis is a common genetic disease that is caused by a mutation in the plasma membrane protein CFTR, which stands for Cystic Fibrosis Transmembrane-conductance Regulator. When this membrane protein is mutated, it impairs its chloride ion channel function, blocking the movement of chloride ions that travel in and out of the cell. Previous studies have demonstrated that the most prevalent CFTR mutation, ∆F508-CFTR, can be partially reversed using small molecules (Heda and Marino, BBRC, 271:659-664, 2000). In this study, I have investigated the effects of several triazole compounds known to bind and transport chloride ions in cultured cells, on the expression and function of ∆F508-CFTR. To determine the impact of triazole compounds on CFTR expression, human airway epithelial cells expressing ∆F508-CFTR were treated with various triazole compounds at 27°C for 60 hours. The plasma membrane expression of CFTR was analyzed by immunoblotting with R3194, an anti-CFTR antibody, followed by the detection of the CFTR-specific signal using chemiluminescence. By comparing the results to the control group treated with the vehicle alone (DMSO or ethanol), I observed that these triazole compounds increased the expression of the immature form of CFTR protein in a concentration-dependent manner. This increase in CFTR-protein expression after treatment with triazole suggests that these compounds have the potential to be used as therapeutic agents in the treatment of Cystic Fibrosis.
Recommended Citation
Taylor, Maggie, "UPREGULATION OF THE PREDOMINANT CYSTIC FIBROSIS CAUSING MUTATION DF508-CFTR BY TRIAZOLE COMPOUNDS IN EPITHELIAL CELLS" (2024). Undergraduate Research Conference. 2.
https://athenacommons.muw.edu/urc/2024/oral-presentations-ii/2
Included in
UPREGULATION OF THE PREDOMINANT CYSTIC FIBROSIS CAUSING MUTATION DF508-CFTR BY TRIAZOLE COMPOUNDS IN EPITHELIAL CELLS
Cystic fibrosis is a common genetic disease that is caused by a mutation in the plasma membrane protein CFTR, which stands for Cystic Fibrosis Transmembrane-conductance Regulator. When this membrane protein is mutated, it impairs its chloride ion channel function, blocking the movement of chloride ions that travel in and out of the cell. Previous studies have demonstrated that the most prevalent CFTR mutation, ∆F508-CFTR, can be partially reversed using small molecules (Heda and Marino, BBRC, 271:659-664, 2000). In this study, I have investigated the effects of several triazole compounds known to bind and transport chloride ions in cultured cells, on the expression and function of ∆F508-CFTR. To determine the impact of triazole compounds on CFTR expression, human airway epithelial cells expressing ∆F508-CFTR were treated with various triazole compounds at 27°C for 60 hours. The plasma membrane expression of CFTR was analyzed by immunoblotting with R3194, an anti-CFTR antibody, followed by the detection of the CFTR-specific signal using chemiluminescence. By comparing the results to the control group treated with the vehicle alone (DMSO or ethanol), I observed that these triazole compounds increased the expression of the immature form of CFTR protein in a concentration-dependent manner. This increase in CFTR-protein expression after treatment with triazole suggests that these compounds have the potential to be used as therapeutic agents in the treatment of Cystic Fibrosis.