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Full-Text Articles in Systems Biology
Multi-Behavioral Endpoint Testing Of An 87-Chemical Compound Library In Freshwater Planarians, S. Zhang, D. Hagstrom, P. Hayes, A. Graham, Eva-Maria S. Collins
Multi-Behavioral Endpoint Testing Of An 87-Chemical Compound Library In Freshwater Planarians, S. Zhang, D. Hagstrom, P. Hayes, A. Graham, Eva-Maria S. Collins
Biology Faculty Works
There is an increased recognition in the field of toxicology of the value of medium-to-high-throughput screening methods using in vitro and alternative animal models. We have previously introduced the asexual freshwater planarian Dugesia japonica as a new alternative animal model and proposed that it is particularly well-suited for the study of developmental neurotoxicology. In this paper, we discuss how we have expanded and automated our screening methodology to allow for fast screening of multiple behavioral endpoints, developmental toxicity, and mortality. Using an 87-compound library provided by the National Toxicology Program (NTP), consisting of known and suspected neurotoxicants, including drugs, flame …
Planarian Cholinesterase: Molecular And Functional Characterization Of An Evolutionarily Ancient Enzyme To Study Organophosphorus Pesticide Toxicity, D. Hagstrom, S. Zhang, A. Ho, E. S. Tsai, Z. Radić, A. Jahromi, K. J. Kaj, Y. He, P. Taylor, Eva-Maria S. Collins
Planarian Cholinesterase: Molecular And Functional Characterization Of An Evolutionarily Ancient Enzyme To Study Organophosphorus Pesticide Toxicity, D. Hagstrom, S. Zhang, A. Ho, E. S. Tsai, Z. Radić, A. Jahromi, K. J. Kaj, Y. He, P. Taylor, Eva-Maria S. Collins
Biology Faculty Works
The asexual freshwater planarian Dugesia japonica has emerged as a medium-throughput alternative animal model for neurotoxicology. We have previously shown that D. japonica are sensitive to organophosphorus pesticides (OPs) and characterized the in vitro inhibition profile of planarian cholinesterase (DjChE) activity using irreversible and reversible inhibitors. We found that DjChE has intermediate features of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Here, we identify two candidate genes (Djche1 and Djche2) responsible for DjChE activity. Sequence alignment and structural homology modeling with representative vertebrate AChE and BChE sequences confirmed our structural predictions, and show that both DjChE enzymes have intermediate sized catalytic gorges …