Trichostatin A enhances catalase activity in Drosophila melanogasterap56f

ECSU Author/Contributor (non-ECSU co-authors, if there are any, appear on document)
Ronald H. Blackmon, Professor (Creator)
Gary Harmon, Professor (Creator)
Elizabeth City State University (ECSU )
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Abstract: In an aerobic environment, catalase plays an important role in the defense of cells and organisms against the toxic effects of oxygen. Possible consequences of the production of reactive oxygen species (ROS) from the metabolism of oxygen include damage to biological macromolecules such as lipids, proteins, and nucleic acids. The detrimental effects on cellular metabolism can result in the loss of viability. Catalase, an antioxidant enzyme, prevents the accumulation of hydrogen peroxide, a reactive oxygen species, by catalyzing conversion of the substrate to water and molecular oxygen. In this inquiry, the role of an epigenetic agent on catalase levels was investigated to ascertain the potential of this approach for bolstering antioxidant defense systems in aerobic organisms. Trichostatin A (TSA) is a histone deacetylase inhibitor that targets the class I and class II histone deacetylases (HDAC) and histones H3 and H4 (Huidobro et al., 2013). Eukaryotic DNA is arranged into chromatin in which histone components of nucleosomes can be regulated by reversible acetylation. Histone acetylation is regulated by histone acetyltransferases and histone deacetylases (HDACs), which play important roles in transcription, DNA replication, and cell cycle progression (Benayoun et al., 2015). Trichostatin A, which inhibits HDAC, has been shown to stop cell cycling, induce differentiation, and reverse morphological changes seen in the cell cycle arrest (Santos et al., 2018). In this study, the activity of catalase in response to TSA was determined in four-day old adult flies of a mutant Drosophila melanogaster strain.

Additional Information

Language: English
Date: 2021
aerobic environment, defense cells, ROS, Eukaryotic DNA

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