Journal or Publishing Institution: Journal of Proteomics
Study: https://www.sciencedirect.com/science/article/pii/S1874391913003242
Author(s): Arruda, S.C., Barbosa, H.S., Azevedo, R.A. and Arruda, M.A.
Article Type: Peer Reviewed Study
Record ID: 2389
Abstract: This work evaluates the activity of a few key enzymes involved in combating reactive oxygen species (ROS), such as ascorbate peroxidase (EC 1.11.1.11), catalase (EC 1.11.1.6), glutathione reductase (EC 1.6.4.2), and superoxide dismutase (EC 1.15.1.1), as well as the concentration of malondialdehyde and hydrogen peroxide in transgenic and non-transgenic soybean leaves. Additionally, differential protein species from leaves of both genotypes were evaluated by applying a regulation factor of ≥ 1.8 to further corroborate the hypothesis that genetic modification itself can be a stress factor for these plants. For this task, transgenic soybean plants were obtained from seeds modified with the cp4EPSPS gene. The results revealed higher activities of all evaluated enzymes in transgenic than in non-transgenic soybean leaves (ranging from 13.8 to 70.1%), as well as higher concentrations of malondialdehyde and hydrogen peroxide in transgenic soybean leaves, clearly indicating a condition of oxidative stress established in the transgenic genotype. Additionally, 47 proteins were differentially abundant when comparing the leaves of both plants, with 26 species accurately identified, including the protein involved in the genetic modification (CP4EPSPS). From these results, it is possible to conclude that the plant is searching for a new equilibrium to maintain its metabolism because the stress condition is being maintained within levels that can be tolerated by the plant.
Keywords: Soybean, Genetically modified organisms, cp4EPSPS, 2-D DIGE, Mass spectrometry, Oxidative stress
Citation: Arruda, S.C., Barbosa, H.S., Azevedo, R.A. and Arruda, M.A., 2013. Comparative studies focusing on transgenic through cp4EPSPS gene and non-transgenic soybean plants: an analysis of protein species and enzymes. Journal of Proteomics, 93, pp.107-116.