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      Copper sulphate impact on the antioxidant defence system of the marine bivalves Cerastoderma edule and Scrobicularia plana

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          Abstract

          Anthropogenic activities, such as agriculture and industrial activities, are a main source of pollution contributing for the degradation of water quality and thus affecting the living organisms of aquatic systems. Copper is widely used at these practices being often released into the aquatic systems and may cause negative effects in its communities. This study proposes to determine the effects of copper in the antioxidant defence system of two size classes (big and small sizes) of Scrobicularia plana and Cerastoderma edule, two marine bivalve species with commercial interest. It was observed the behaviour activity of the organisms during the exposure to copper sulphate (CS) and was determined the enzymatic activities of glutathione-S-transferases (GST), glutathione reductase (GR) and glutathione peroxidase (GPx) (both selenium-dependent (SeGPx) and total (tGPx)) in the muscle tissue (foot). Lipid peroxidation (LPO) was evaluated through thiobarbituric acid reactive substances (TBARS) measurement in the foot. Changes in the behaviour and enzymatic activity were observed. Lipid peroxidation was observed at C. edule and S. plana big and small size classes, respectively, according to TBARS levels. The foot showed to be a good tissue to be used in biochemical analysis to detect the presence of toxicants.

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          Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants.

          The potential of oxygen free radicals and other reactive oxygen species (ROS) to damage tissues and cellular components, called oxidative stress, in biological systems has become a topic of significant interest for environmental toxicology studies. The balance between prooxidant endogenous and exogenous factors (i.e., environmental pollutants) and antioxidant defenses (enzymatic and nonenzymatic) in biological systems can be used to assess toxic effects under stressful environmental conditions, especially oxidative damage induced by different classes of chemical pollutants. The role of these antioxidant systems and their sensitivity can be of great importance in environmental toxicology studies. In the past decade, numerous studies on the effects of oxidative stress caused by some environmental pollutants in terrestrial and aquatic species were published. Increased numbers of agricultural and industrial chemicals are entering the aquatic environment and being taken up into tissues of aquatic organisms. Transition metals, polycyclic aromatic hydrocarbons, organochlorine and organophosphate pesticides, polychlorinated biphenyls, dioxins, and other xenobiotics play important roles in the mechanistic aspects of oxidative damage. Such a diverse array of pollutants stimulate a variety of toxicity mechanisms, such as oxidative damage to membrane lipids, DNA, and proteins and changes to antioxidant enzymes. Although there are considerable gaps in our knowledge of cellular damage, response mechanisms, repair processes, and disease etiology in biological systems, free radical reactions and the production of toxic ROS are known to be responsible for a variety of oxidative damages leading to adverse health effects and diseases. In the past decade, mammalian species were used as models for the study of molecular biomarkers of oxidative stress caused by environmental pollutants to elucidate the mechanisms underlying cellular oxidative damage and to study the adverse effects of some environmental pollutants with oxidative potential in chronic exposure and/or sublethal concentrations. This review summarizes current knowledge and advances in the understanding of such oxidative processes in biological systems. This knowledge is extended to specific applications in aquatic organisms because of their sensitivity to oxidative pollutants, their filtration capacity, and their potential for environmental toxicology studies.
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            Glutathione reductase.

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              Possible mechanisms underlying copper-induced damage in biological membranes leading to cellular toxicity.

              It is generally accepted that copper toxicity is a consequence of the generation of reactive oxygen species (ROS) by copper ions via Fenton or Haber-Weiss reactions. Copper ions display high affinity for thiol and amino groups occurring in proteins. Thus, specialized proteins containing clusters of these groups transport and store copper ions, hampering their potential toxicity. This mechanism, however, may be overwhelmed under copper overloading conditions, in which copper ions may bind to thiol groups occurring in proteins non-related to copper metabolism. In this study, we propose that indiscriminate copper binding may lead to damaging consequences to protein structure, modifying their biological functions. Therefore, we treated liver subcellular membrane fractions, including microsomes, with Cu2+ ions either alone or in the presence of ascorbate (Cu2+/ascorbate); we then assayed both copper-binding to membranes, and microsomal cytochrome P450 oxidative system and GSH-transferase activities. All assayed sub-cellular membrane fractions treated with Cu2+ alone displayed Cu2+-binding, which was significantly increased in the presence of Zn2+, Hg2+, Cd2+, Ag+1 and As3+. Treatment of microsomes with Cu2+ in the microM range decreased the microsomal thiol content; in the presence of ascorbate, Cu2+ added in the nM concentrations range induced a significant microsomal lipoperoxidation; noteworthy, increasing Cu2+ concentration to > or =50 microM led to non-detectable lipoperoxidation levels. On the other hand, microM Cu2+ led to the inhibition of the enzymatic activities tested to the same extent in either presence or absence of ascorbate. We discuss the possible significance of indiscriminate copper binding to thiol proteins as a possible mechanism underlying copper-induced toxicity.
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                Author and article information

                Contributors
                amgoncalves@uc.pt
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                11 November 2019
                11 November 2019
                2019
                : 9
                : 16458
                Affiliations
                [1 ]ISNI 0000000123236065, GRID grid.7311.4, Department of Biology and CESAM, , University of Aveiro, ; 3810-193 Aveiro, Portugal
                [2 ]ISNI 0000 0000 9511 4342, GRID grid.8051.c, MARE - Marine and Environmental Sciences Centre, Department of Life Sciences, Faculty of Sciences and Technology, , University of Coimbra, ; 3004-517 Coimbra, Portugal
                Author information
                http://orcid.org/0000-0002-9326-187X
                http://orcid.org/0000-0002-8611-7183
                Article
                52925
                10.1038/s41598-019-52925-9
                6848077
                31712602
                0145bcbc-31ae-45b9-bb2a-c61b5bc88dc7
                © The Author(s) 2019

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 28 February 2019
                : 23 September 2019
                Funding
                Funded by: FundRef https://doi.org/10.13039/501100001871, Ministry of Education and Science | Fundação para a Ciência e a Tecnologia (Portuguese Science and Technology Foundation);
                Award ID: UID/AMB/50017/2013
                Award ID: SFRH/BPD/112803/2015
                Award ID: UID/AMB/50017/2013
                Award ID: UID/MAR/04292/2019
                Award ID: POCI-01-0145-FEDER-022127
                Award ID: UID/AMB/50017/2013
                Award ID: SFRH/BPD/97210/2013
                Award ID: UID/MAR/04292/2019
                Award ID: POCI-01-0145-FEDER-022127
                Award Recipient :
                Funded by: FundRef https://doi.org/10.13039/501100005727, Universidade de Coimbra (University of Coimbra);
                Award ID: IT057-18-7253
                Award Recipient :
                Categories
                Article
                Custom metadata
                © The Author(s) 2019

                Uncategorized
                enzymes,environmental sciences,biomarkers
                Uncategorized
                enzymes, environmental sciences, biomarkers

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