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Article
Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila
International Journal of Peptides
  • Heather G. Kuruvilla, Cedarville University
  • Bradley Schmidt, Cedarville University
  • Stephanie E. Song, Cedarville University
  • Marian A. Bhajjan, Cedarville University
  • Matthew S. Merical, Cedarville University
  • Caleb Alley, Cedarville University
  • Christopher Griffin, Cedarville University
  • David Yoder, Cedarville University
  • Josephine Hein, Cedarville University
  • Daniel B. Kohl, Cedarville University
  • Cambria R. Puffenberger, Cedarville University
  • David C. Petroff, Cedarville University
  • Elise Newcomer, Cedarville University
  • Kortney Good, Cedarville University
  • Graham Heston, Cedarville University
  • Anna O. Hurtubise, Cedarville University
Document Type
Article
Publication Date
2-4-2016
DOI
http://dx.doi.org/10.1155/2016/7142868
Keywords
  • Netrin-1,
  • chemorepellents
Abstract

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 i s 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.

Article Number
7142868
Citation Information
Heather G. Kuruvilla, Bradley Schmidt, Stephanie E. Song, Marian A. Bhajjan, et al.. "Netrin-1 Peptide Is a Chemorepellent in Tetrahymena thermophila" International Journal of Peptides Vol. 2016 (2016) p. 1 - 7
Available at: http://works.bepress.com/heather_kuruvilla/63/