Type of Submission
Poster
Keywords
Netrin-3, immunofluorescence, secretion
Abstract
Tetrahymena thermophila are free-living, unicellular, eukaryotic protozoans that live in a variety of aquatic environments. These organisms interact with their environment by responding to chemorepellents and chemoattractants which direct them toward favorable stimuli, such as food, and away from unfavorable stimuli, such as predators. We have previously described two netrin-like proteins, a netrin-1 like protein, and a netrin-3 like protein, which are secreted from Tetrahymena. Both of these proteins act as chemorepellents, and may allow cells to communicate with each other regarding population density, preventing them from outgrowing the available environmental resources. In our current study, we used antibodies against the N- and C-terminal of netrin-3 to show the distribution of this protein throughout the cell. We find that netrin-3 is highly colocalized with the endoplasmic reticulum and colocalizes with tubulin to a lesser extent. This is to be expected for a protein that is secreted from cells and trafficked on microtubules.
Campus Venue
Stevens Student Center
Location
Cedarville, OH
Start Date
4-12-2017 11:00 AM
End Date
4-12-2017 2:00 PM
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Immunolocalization of a Netrin-3 Like Peptide in Tetrahymena thermophila Using Antibodies Against the N- and C-terminus of the Protein
Cedarville, OH
Tetrahymena thermophila are free-living, unicellular, eukaryotic protozoans that live in a variety of aquatic environments. These organisms interact with their environment by responding to chemorepellents and chemoattractants which direct them toward favorable stimuli, such as food, and away from unfavorable stimuli, such as predators. We have previously described two netrin-like proteins, a netrin-1 like protein, and a netrin-3 like protein, which are secreted from Tetrahymena. Both of these proteins act as chemorepellents, and may allow cells to communicate with each other regarding population density, preventing them from outgrowing the available environmental resources. In our current study, we used antibodies against the N- and C-terminal of netrin-3 to show the distribution of this protein throughout the cell. We find that netrin-3 is highly colocalized with the endoplasmic reticulum and colocalizes with tubulin to a lesser extent. This is to be expected for a protein that is secreted from cells and trafficked on microtubules.
