Atrazine effects on antioxidant status and xenobiotic metabolizing enzymes after oral administration in peripubertal male rat.
Previously, we reported that in vivo applied atrazine from postnatal day 23 to 50 induced strong inhibition of testicular steroidogenesis. Therefore, the aim of the present study was to investigate, in the same experimental model, the oxidative status in androgen-producing testicular interstitial compartment characterized by diminished steroidogenesis. In parallel, we determined activities of antioxidative and cytochrome P450 (CYP) xenobiotic-metabolizing enzymes in liver. To confirm the results on atrazine induced-inhibition of testicular androgenesis, we measured ex vivo production of androgen in Leydig cells. The results revealed decreased activity of antioxidant enzymes, especially glutathione S-transferase (GST), but also glutathione peroxidase (GSH-Px) and catalase (CAT) in testicular interstitial cells, in parallel with strongly diminished ex vivo basal and agonist-stimulated Leydig cell androgenesis. In liver, atrazine increased the activity of GSH-Px, GST, and CYP1A1/2 enzyme, but not lipid peroxidation. These results indicate that atrazine markedly affects both antioxidant status and androgenesis in peripubertal rats.
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia. Electronic address: kristina.pogrmic@dbe.uns.ac.rs.
Kristina
K
Pogrmic-Majkic
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Sonja
S
Kaisarevic
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Svetlana
S
Fa
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Vanja
V
Dakic
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Branka
B
Glisic
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Jelena
J
Hrubik
Laboratory for Ecotoxicology (LECOTOX), Department of Biology and Ecology, University of Novi Sad Faculty of Sciences, 21000 Novi Sad, Serbia.
Radmila
R
Kovacevic
D000284:Administration, Oral; D000818:Animals; D001280:Atrazine / Q000633:toxicity*; D002374:Catalase / Q000378:metabolism; D019363:Cytochrome P-450 CYP1A1 / Q000378:metabolism; D019388:Cytochrome P-450 CYP1A2; D019362:Cytochrome P-450 CYP2B1 / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism; D006540:Herbicides / Q000633:toxicity*; D007985:Leydig Cells / Q000187:drug effects / Q000378:metabolism; D015227:Lipid Peroxidation / Q000187:drug effects; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism; D011627:Puberty; D051381:Rats; D017208:Rats, Wistar; D013739:Testosterone / Q000378:metabolism; D015262:Xenobiotics / Q000378:metabolism
D003580:Cytochromes; D006540:Herbicides; D015262:Xenobiotics; D013739:Testosterone; D002374:Catalase; D005979:Glutathione Peroxidase; C017170:Cyp1a2 protein, rat; D019363:Cytochrome P-450 CYP1A1; D019388:Cytochrome P-450 CYP1A2; D019362:Cytochrome P-450 CYP2B1; D005982:Glutathione Transferase; D001280:Atrazine