Browse > Article

Gene Expression Patterns of the Endogenous Antioxidant Enzymes in Linuron-Treated Rat Ventral Prostates after Castration  

Yon, Jung-Min (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungbuk National University)
Lin, Chunmei (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungbuk National University)
Lee, Yoon-Bok (Central Research Institute, Dr. Chung's Food Co. Ltd.)
Lee, Beom-Jun (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungbuk National University)
Yun, Young-Won (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungbuk National University)
Nam, Sang-Yoon (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungbuk National University)
Publication Information
Journal of Embryo Transfer / v.27, no.2, 2012 , pp. 101-105 More about this Journal
Abstract
Linuron is a pesticide with a weak anti-androgenic property, which impacts male reproductive organs. In this study, to clarify whether linuron affects the cellular antioxidant system of ventral prostate, gene expression patterns of the representative antioxidant enzymes such as glutathione peroxidase (GPx), selenoprotein P (SePP), and superoxide dismutase (SOD) were investigated in the rat ventral prostates exposed to linuron using real-time RT-PCR analyses. Sprague-Dawley rats castrated at 6 weeks old were treated with linuron (25, 50, or 100 mg/kg per oral) daily for 10 days after testosterone propionate administration (0.4 mg/kg) subcutaneously. As compared to normal control animals, mRNA levels of phospholipid hydroperoxide GPx (PHGPx), SePP, and Mn SOD significantly increased in the prostates exposed to linuron (25, 50, and 100 mg/kg). However, cytosolic GPx (100 mg/kg) and Cu/Zn SOD (25, 50, and 100 mg/kg) mRNA levels significantly decreased in the ventral prostates. These results indicate that linuron upregulates the expressions of PHGPx, SePP, and Mn SOD mRNAs, but down-regulates the expressions of cytosolic GPx and Cu/Zn SOD in rat prostates, suggesting that linuron may have dual effects in the cellular antioxidant system of prostate.
Keywords
linuron; glutathione peroxidase; selenoprotein; superoxide dismutase; rat ventral prostate;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Muller FL, Lustgarten MS, Jang Y, Richardson A and Van Remmen H. 2007. Trends in oxidative aging theories. Free Radic. Biol. Med. 43:477-503.   DOI   ScienceOn
2 Murakoshi M, Tagawa M, Inada R, Mizokami A, Suzuki M and Watanabe K. 1993. Immunolocalization of glutathioneperoxidase and androgen receptors in the rat dorsolateral prostate. Tokai. J. Exp. Clin. Med. 18:87-94.
3 Nishimura K, Matsumiya K, Tsujimura A, Koga M, Kitamura M and Okuyama A. 2001. Association of selenoprotein P with testosterone production in cultured Leydig cells. Arch. Androl. 47:67-76.   DOI   ScienceOn
4 Pang ST, Dillner K, Wu X, Pousette A, Norstedt G and Flores- Morales A. 2002. Gene expression profiling of androgen deficiency predicts a pathway of prostate apoptosis that involves genes related to oxidative stress. Endocrinology 143: 4897-4906.   DOI   ScienceOn
5 Roy AK, Lavrovsky Y, Song CS, Chen S, Jung MH, Velu NK, Bi BY and Chatterjee B. 1999. Regulation of androgen action. Vitam. Horm. 55:309-352.
6 Shabsigh A, Chang DT, Heitjan DF, Kiss A, Olsson CA, Puchner PJ and Buttyan R. 1998. Rapid reduction in blood flow to the rat ventral prostate gland after castration: preliminary evidence that androgens influence prostate size by regulating blood flow to the prostate gland and prostatic endothelial cell survival. Prostate 36:201-206.   DOI   ScienceOn
7 Sharifi N, Hurt EM, Thomas SB and Farrar WL. 2008. Effects of manganese superoxide dismutase silencing on androgen receptor function and gene regulation: implications for castration- resistant prostate cancer. Clin. Cancer Res. 14:6073-6080.   DOI   ScienceOn
8 Tam NN, Gao Y, Leung YK and Ho SM. 2003. Androgenic regulation of oxidative stress in the rat prostate: involvement of NAD(P)H oxidases and antioxidant defense machinery during prostatic involution and regrowth. Am. J. Pathol. 163: 2513-2522.   DOI   ScienceOn
9 Waller CL, Juma BW, Gray LE Jr and Kelce WR. 1996. Threedimensional quantitative structure-activity relationships for androgen receptor ligands. Toxicol. Appl. Pharmacol. 137: 219-227.   DOI   ScienceOn
10 Weisiger RA and Fridovich I. 1973. Mitochondrial superoxide simutase. Site of synthesis and intramitochondrial localization. J. Biol. Chem. 248:4793-4796.
11 Wolf C Jr, Lambright C, Mann P, Price M, Cooper RL, Ostby J and Gray LE Jr. 1999. Administration of potentially antiandrogenic pesticides (procymidone, linuron, iprodione, chlozolinate, p,p'-DDE, and ketoconazole) and toxic substances (dibutyl- and diethylhexyl phthalate, PCB 169, and ethane dimethane sulphonate) during sexual differentiation produces diverse profiles of reproductive malformations in the male rat. Toxicol. Ind. Health. 15:94-118.
12 Frye CA, Bo E, Calamandrei G, Calza L, Dessi-Fulgheri F, Fernandez M, Fusani L, Kah O, Kajta M, Le Page Y, Patisaul HB, Venerosi A, Wojtowicz AK and Panzica GC. 2012. Endocrine disrupters: a review of some sources, effects, and mechanisms of actions on behaviour and neuroendocrine systems. J. Neuroendocrinol. 24:144-159.   DOI   ScienceOn
13 Agarwal A, Saleh RA and Bedaiwy MA. 2003. Role of reactive oxygen species in the pathophysiology of human reproduction. Fertil. Steril. 79:829-843.   DOI   ScienceOn
14 Burk RF, Hill KE and Motley AK. 2003. Selenoprotein metabolism and function: evidence for more than one function for selenoprotein P. J. Nutr. 133:1517S-1520S.
15 Castellon E, Rioseco H, Rojas J, Royer M, Salas E, Contreras H and Huidobro C. 2005. Glutathione peroxidase activity in cell cultures from different regions of human epididymis. Asian J. Androl. 7:33-37.   DOI   ScienceOn
16 Colborn T, Vom Saal FS and Soto AM. 1993. Developmental effects of endocrine-disrupting chemicals in wildlife and humans. Environ. Health Perspect. 101:378-384.   DOI   ScienceOn
17 Davison SL and Bell R. 2006 Androgen physiology. Semin. Reprod. Med. 24:71-77.   DOI
18 Imai H and Nakagawa Y. 2003. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 34:145-169.   DOI   ScienceOn
19 Jara M, Carballada R and Esponda P. 2004. Age-induced apoptosis in the male genital tract of the mouse. Reproduction 127:359-366.   DOI   ScienceOn
20 Kang IH, Kim HS, Shin JH, Kim TS, Moon HJ, Kim IY, Choi KS, Kil KS, Park YI, Dong MS and Han SY. 2004. Comparison of anti-androgenic activity of flutamide, vinclozolin, procymidone, linuron, and p, p'-DDE in rodent 10-day Hershberger assay. Toxicology 199:145-159.   DOI
21 Lambright C, Ostby J, Bobseine K, Wilson V, Hotchkiss AK, Mann PC and Gray LE Jr. 2000 Cellular and molecular mechanisms of action of linuron: an antiandrogenic herbicide that produces reproductive malformations in male rats. Toxicol. Sci. 56:389-399.   DOI
22 McCord JM and Fridovich I. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-6055.