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Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
Netrin-1 is a highly conserved, pleiotropic signaling molecule that can serve as a neuronal chemorepellent during vertebrate development. In vertebrates, chemorepellent signaling is mediated through the tyrosine kinase, src-1, and the tyrosine phosphatase, shp-2. Tetrahymena thermophila has been use...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4830718/ https://www.ncbi.nlm.nih.gov/pubmed/27123011 http://dx.doi.org/10.1155/2016/7142868 |
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author | Kuruvilla, Heather Schmidt, Bradley Song, Stephanie Bhajjan, Marian Merical, Matthew Alley, Caleb Griffin, Christopher Yoder, David Hein, Josephine Kohl, Daniel Puffenberger, Cambria Petroff, David Newcomer, Elise Good, Kortney Heston, Graham Hurtubise, Anna |
author_facet | Kuruvilla, Heather Schmidt, Bradley Song, Stephanie Bhajjan, Marian Merical, Matthew Alley, Caleb Griffin, Christopher Yoder, David Hein, Josephine Kohl, Daniel Puffenberger, Cambria Petroff, David Newcomer, Elise Good, Kortney Heston, Graham Hurtubise, Anna |
author_sort | Kuruvilla, Heather |
collection | PubMed |
description | Netrin-1 is a highly conserved, pleiotropic signaling molecule that can serve as a neuronal chemorepellent during vertebrate development. In vertebrates, chemorepellent signaling is mediated through the tyrosine kinase, src-1, and the tyrosine phosphatase, shp-2. Tetrahymena thermophila has been used as a model system for chemorepellent signaling because its avoidance response is easily characterized under a light microscope. Our experiments showed that netrin-1 peptide is a chemorepellent in T. thermophila at micromolar concentrations. T. thermophila adapts to netrin-1 over a time course of about 10 minutes. Netrin-adapted cells still avoid GTP, PACAP-38, and nociceptin, suggesting that netrin does not use the same signaling machinery as any of these other repellents. Avoidance of netrin-1 peptide was effectively eliminated by the addition of the tyrosine kinase inhibitor, genistein, to the assay buffer; however, immunostaining using an anti-phosphotyrosine antibody showed similar fluorescence levels in control and netrin-1 exposed cells, suggesting that tyrosine phosphorylation is not required for signaling to occur. In addition, ELISA indicates that a netrin-like peptide is present in both whole cell extract and secreted protein obtained from Tetrahymena thermophila. Further study will be required in order to fully elucidate the signaling mechanism of netrin-1 peptide in this organism. |
format | Online Article Text |
id | pubmed-4830718 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-48307182016-04-27 Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila Kuruvilla, Heather Schmidt, Bradley Song, Stephanie Bhajjan, Marian Merical, Matthew Alley, Caleb Griffin, Christopher Yoder, David Hein, Josephine Kohl, Daniel Puffenberger, Cambria Petroff, David Newcomer, Elise Good, Kortney Heston, Graham Hurtubise, Anna Int J Pept Research Article Netrin-1 is a highly conserved, pleiotropic signaling molecule that can serve as a neuronal chemorepellent during vertebrate development. In vertebrates, chemorepellent signaling is mediated through the tyrosine kinase, src-1, and the tyrosine phosphatase, shp-2. Tetrahymena thermophila has been used as a model system for chemorepellent signaling because its avoidance response is easily characterized under a light microscope. Our experiments showed that netrin-1 peptide is a chemorepellent in T. thermophila at micromolar concentrations. T. thermophila adapts to netrin-1 over a time course of about 10 minutes. Netrin-adapted cells still avoid GTP, PACAP-38, and nociceptin, suggesting that netrin does not use the same signaling machinery as any of these other repellents. Avoidance of netrin-1 peptide was effectively eliminated by the addition of the tyrosine kinase inhibitor, genistein, to the assay buffer; however, immunostaining using an anti-phosphotyrosine antibody showed similar fluorescence levels in control and netrin-1 exposed cells, suggesting that tyrosine phosphorylation is not required for signaling to occur. In addition, ELISA indicates that a netrin-like peptide is present in both whole cell extract and secreted protein obtained from Tetrahymena thermophila. Further study will be required in order to fully elucidate the signaling mechanism of netrin-1 peptide in this organism. Hindawi Publishing Corporation 2016 2016-03-31 /pmc/articles/PMC4830718/ /pubmed/27123011 http://dx.doi.org/10.1155/2016/7142868 Text en Copyright © 2016 Heather Kuruvilla et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Kuruvilla, Heather Schmidt, Bradley Song, Stephanie Bhajjan, Marian Merical, Matthew Alley, Caleb Griffin, Christopher Yoder, David Hein, Josephine Kohl, Daniel Puffenberger, Cambria Petroff, David Newcomer, Elise Good, Kortney Heston, Graham Hurtubise, Anna Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila |
title | Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
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title_full | Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
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title_fullStr | Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
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title_full_unstemmed | Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
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title_short | Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
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title_sort | netrin-1 peptide is a chemorepellent in tetrahymena thermophila |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4830718/ https://www.ncbi.nlm.nih.gov/pubmed/27123011 http://dx.doi.org/10.1155/2016/7142868 |
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