Evaluation of Massie’s Creek Habitat and Water Quality

In November of 2009, Greene County completed a restoration project on the North Fork of Massie Creek. This project was designed to address “...erosion and water quality concerns, improve drainage, and restore the habitat of NFMC”. The project worked to “...stabilize the stream banks, create riffle/pool habitat, and restore and enhance vegetation along a 2.2-mile long segment of the creek”. The project was finalized with seeding the area in January of 2010. Now four years later we will evaluate the aquatic habitats, macroinvertebrate biodiversity, and water quality in the restored (North Fork) and unrestored (South Fork) segments of Massie’s Creek as well as points after their confluence. We predict that the water quality, macroinvertebreate biodiversity, and aquatic habitats will be of greater quality in the restored North Fork as compared to the other segments. We will be monitoring water quality (light, temperature, and turbidity) at different points along Massie Creek. Additionally, we will use the Ohio EPA’s Qualitative Habitat Evaluation Index to assess habitat quality and macroinvertebrate biodiversity

Evidence for Secretion of a Netrin-1-like Protein by Tetrahymena thermophila

Netrin-1 is a pleiotropic signaling molecule with targets in many mammalian cell types. Though first characterized as a chemotactic signal involved in neuronal guidance during development, netrin-1 has since been found to have a regulatory role in angiogenesis, and is also used as a biomarker in certain cancers. Tetrahymena thermophila are free-living protists that rely on chemotactic signals to find food, as well as to escape predators. Chemoattractants cause the cells to swim faster in the forward direction, while chemorepellents cause ciliary reversal, resulting in movement of the cell away from the noxious stimulus. We have previously found that netrin-1 is a chemorepellent in T. thermophila. More recently, we have detected netrin-1 by ELISA in both whole cell extract and secreted protein samples obtained from T. thermophila. In addition, we have immunolocalized netrin-1 staining to the cytosol of T. thermophila using an anti-netrin-1 antibody. We are currently running Western blots to determine the molecular weight of this protein and compare it to its vertebrate counterparts. Further experimentation is needed to determine the physiological role of this protein in T. thermophila