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      Effect of Sterigmatocystin or Aflatoxin Contaminated Feed on Lipid Peroxidation and Glutathione Redox System and Expression of Glutathione Redox System Regulatory Genes in Broiler Chicken

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          Abstract

          Authors studied the effect of sterigmatocystin from infected corn (STC), purified sterigmatocystin (PSTC), and aflatoxin B1 from infected corn (AFB 1) on lipid peroxidation and glutathione redox parameters, including the expression of their encoding genes in a sub-chronic (14 days) trial. A total of 144 three-week-old cockerels was divided into four experimental groups ( n = 36 in each). Control feed was contaminated with STC or PSTC (1590 µg STC/kg or 1570.5 µg STC/kg feed), or with AFB 1 (149.1 µg AFB 1/kg feed). Six birds from each group were sampled at day 1, 2, 3, 7 and 14 of mycotoxin exposure. As parameters of lipid peroxidation, conjugated dienes (CD) and trienes (CT) were measured in the liver, while malondialdehyde (MDA) concentration was determined in blood plasma, red blood cell hemolysate and liver. Reduced glutathione (GSH) concentration and glutathione peroxidase (GPx) activity were determined in the same samples, and expression of glutathione peroxidase 4 ( GPX4), glutathione synthetase ( GSS) and glutathione reductase ( GSR) genes was measured by RT-PCR in the liver. STC, PSTC or AFB 1 caused a slight, but not significant, increase in CD and CT levels; however, in the case of MDA, no increase was found in the liver. Glutathione redox system was activated in the liver by AFB 1, but less markedly by STC/PSTC. PSTC and AFB 1 resulted in a higher expression of GPX4, while GSS expression was down-regulated by AFB 1 on day 1, but up-regulated by STC on day 2 and by both mycotoxins on day 7. However, on day 14, GSS expression was down-regulated by PSTC. Expression of GSR was low on day 1 in AFB 1 and PSTC groups, but later it was up-regulated by AFB 1. The observed changes regarding gene expression strengthen the hypothesis that the mild oxidative stress, caused by the applied STC doses, activates the glutathione redox system of broiler chickens.

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          An accurate and rapid method for the determination of proteins in small amounts of blood serum and plasma.

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            The selenium deficiency disease exudative diathesis in chicks is associated with downregulation of seven common selenoprotein genes in liver and muscle.

            Fast-growing broiler chicks are susceptible to Se deficiency diseases including exudative diathesis (ED). Our objective was to determine if ED could be induced by feeding a current, practical diet and if the incidence was related to selenogenome expression in liver and muscle of chicks. Four groups of day-old broiler chicks (n = 60/group) were fed a corn-soy basal diet (BD; 14 μg Se/kg; produced in the Se-deficient area of Sichuan, China and not supplemented with Se or vitamin E), the BD and all-rac-α-tocopheryl acetate at 50 mg/kg and Se (as sodium selenite) at 0.3 mg/kg, or both of these nutrients for 6 wk. A high incidence of ED and mortality of chicks were induced by the BD. The incidences and mortality were completely prevented by supplemental dietary Se but were only partially decreased by supplemental α-tocopherol acetate. Dietary Se deficiency decreased (P < 0.05) mRNA levels of 7 common selenoprotein genes (Gpx1, Gpx4, Sepw1, Sepn1, Sepp1, Selo, and Selk) in muscle and liver. Whereas supplementing α-tocopherol acetate enhanced (P < 0.05) only the muscle Sepx1 mRNA level, it actually decreased (P < 0.05) hepatic Gpx1, Seli, Txnrd1, and Txnrd2 mRNA levels. In conclusion, dietary Se protected chicks from the Se deficiency disease ED, probably by upregulating selenoprotein genes coding for oxidation- and/or lesion-protective proteins. The protection by vitamin E might be mediated via selenoproteins not assayed in this study and/or Se-independent mechanisms. The inverse relationship between hepatic expression of 4 redox-related selenoprotein genes and vitamin E status revealed a novel interaction between Se and vitamin E in vivo.
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              Efficacy of turmeric (Curcuma longa), containing a known level of curcumin, and a hydrated sodium calcium aluminosilicate to ameliorate the adverse effects of aflatoxin in broiler chicks.

              A 3-wk feeding study was conducted to evaluate the efficacy of turmeric (Curcuma longa) powder (TMP), containing a known level of curcumin, and a hydrated sodium calcium aluminosilicate (HSCAS; Improved Milbond-TX, IMTX, an adsorbent, Milwhite Inc., Houston, TX) to ameliorate the adverse effects of aflatoxin B(1) (AFB(1)) in broiler chicks. Four pen replicates of 5 chicks each were assigned to each of 7 dietary treatments, which included the basal diet not containing TMP, HSCAS, or AFB(1) (control); basal diet supplemented with 0.5% food grade TMP that contained 1.48% total curcuminoids (74 mg/kg); basal diet supplemented with 0.5% HSCAS; basal diet supplemented with 1.0 mg/kg AFB(1); basal diet supplemented with 0.5% TMP and 1.0 mg/kg AFB(1); basal diet supplemented with 0.5% HSCAS and 1.0 mg/kgAFB(1); and basal diet supplemented with 0.5% TMP, 0.5% HSCAS, and 1.0 mg/kg AFB(1). The addition of TMP to the AFB(1) diet significantly (P < 0.05) improved the weight gain of chicks, and the addition of HSCAS to the AFB(1) diet significantly (P < 0.05) improved feed intake and weight gain, and reduced relative liver weight. The addition of TMP or HSCAS and TMP with HSCAS ameliorated the adverse effects of AFB(1) on some of the serum chemistry parameters (total protein, albumin, cholesterol, calcium). Further, decreased antioxidant functions in terms of level of peroxides, superoxide dismutase activity, and total antioxidant concentration in liver homogenate due to AFB1 were also alleviated by the inclusion of TMP, HSCAS, or both. The reduction in the severity of hepatic microscopic lesions due to supplementation of the AFB(1) diet with TMP and HSCAS demonstrated the protective action of the antioxidant and adsorbent used in the present study.
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                Author and article information

                Journal
                Antioxidants (Basel)
                Antioxidants (Basel)
                antioxidants
                Antioxidants
                MDPI
                2076-3921
                28 June 2019
                July 2019
                : 8
                : 7
                : 201
                Affiliations
                [1 ]Department of Nutrition, Szent István University, H-2100 Gödöllő, Hungary
                [2 ]Mycotoxins in the Food Chain Research Group, Hungarian Academy of Sciences–Kaposvár University–Szent István University, H-7400 Kaposvár, Hungary
                [3 ]Department of Environmental and Applied Microbiology, Agro-Environmental Research Institute, National Agricultural Research and Innovation Centre (NARIC), H-1022 Budapest, Hungary
                [4 ]Department of Microbiology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Hungary
                Author notes
                Author information
                https://orcid.org/0000-0002-9435-4568
                https://orcid.org/0000-0003-1651-4623
                https://orcid.org/0000-0003-2323-833X
                Article
                antioxidants-08-00201
                10.3390/antiox8070201
                6680631
                31261801
                adf2013e-9884-4b4e-907f-31299d1e2322
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 01 June 2019
                : 26 June 2019
                Categories
                Article

                sterigmatocystin,broiler chicken,antioxidant defense system,glutathione peroxidase,gene expression

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