Upregulation of Glutathion S-Transferase mu 1 in Bovine Cystic Follicles

  • Kang, Da-Won (Department of Physiology, Institute of Health Sciences, Gyeongsang National University School of Medicine) ;
  • Kim, Chang-Woon (Department of Physiology, Institute of Health Sciences, Gyeongsang National University School of Medicine) ;
  • Han, Jae-Hee (Department of Physiology, Institute of Health Sciences, Gyeongsang National University School of Medicine)
  • Received : 2010.11.09
  • Accepted : 2010.11.30
  • Published : 2010.12.31

Abstract

Follicular cystic follicles (FCFs) show delayed regression with persistent follicle growth. However, the mechanism by which follicles are persistently grown remains unclear. Glutathione S-transferases (GSTs) are drug-metabolizing and detoxification enzymes that are involved in the intracellular transport and metabolism of steroid hormones. In this study, a proteomic analysis was performed to identify whether GST expression is changed in bovine FCFs and to predict the interactions between GST and other proteins. Normal follicles and FCFs were classified based on their sizes (5 to 10 mm and 25 mm). In bovine follicles, GST mu 1 (GSTM1) was detected as a differentially expressed protein (DEP) and significantly up-regulated in FCFs compared to normal follicles (p<0.05). Consistent with the proteomic results, semi-quantitative PCR data and western blot analysis revealed an up-regulation of GSTM1 in FCFs. Expression levels of aromatase and dehydrogenase proteins were changed in FCFs. These results show that the up-regulation of GSTM1 that is observed in bovine FCFs is likely to be responsible for the persistent follicle growth in FCFs as the activity of aromatase and the dehydrogenases.

Keywords

References

  1. Boyer TD. 1989. The glutathione S-transferases: an update. Hepatology 9:486-496. https://doi.org/10.1002/hep.1840090324
  2. Cho SG, Lee YH, Park HS, Ryoo K, Kang KW, Park J, Eom SJ, Kim MJ, Chang TS, Choi SY, Shim J, Kim Y, Dong MS, Lee MJ, Kim SG, Ichijo Hand Choi EJ. 2001. Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1. J. Biol. Chem. 276:12749-12755. https://doi.org/10.1074/jbc.M005561200
  3. Choe C, Cho YW, Kim CW, Son DS, Han J and Kang D. 2010. Identification of differentially expressed genes in bovine follicular cystic ovaries. Korean J. Physiol. Pharmacol. 14:265-272. https://doi.org/10.4196/kjpp.2010.14.5.265
  4. Douglas KT. 1987. Mechanism of action of glutathione-dependent enzymes. Adv. Enzymol. Relat. Areas. Mol. Biol. 59:103-167.
  5. Haas S, Pierl C, Harth V, Pesch B, Rabstein S, Bruning T, Ko Y, Hamann U, Justenhoven C, Brauch H and Fischer HP. 2006. Expression of xenobiotic and steroid hormone metabolizing enzymes in human breast carcinomas. Int. J. Cancer 119:1785-1791. https://doi.org/10.1002/ijc.21915
  6. Hauptmann S, Denkert C, Koch I, Petersen S, Schluns K, Reles A, Dietel M and Petersen I. 2002. Genetic alterations in epithelial ovarian tumors analyzed by comparative genomic hybridization. Hum. Pathol. 33:632-641. https://doi.org/10.1053/hupa.2002.124913
  7. Hirvonen A, Husgafvel-Pursiainen K, Anttila Sand Vainio H. 1993. The GSTM1 null genotype as a potential risk modifier for squamous cell carcinoma of the lung. Carcinogenesis 14:1479-1481. https://doi.org/10.1093/carcin/14.7.1479
  8. Hokaiwado N, Takeshita F, Naiki-Ito A, Asamoto M, Ochiya T and Shirai T. 2008. Glutathione S-transferase Pi mediates proliferation of androgen-independent prostate cancer cells. Carcinogenesis 29:1134-1138. https://doi.org/10.1093/carcin/bgn097
  9. Isobe N and Yoshimura Y. 2007. Deficient proliferation and apoptosis in the granulosa and theca interna cells of the bovine cystic follicle. J. Reprod. Dev. 53:1119-1124. https://doi.org/10.1262/jrd.19041
  10. Kesler DJ, Elmore RG, Brown EM and Garverick HA. 1981. Gonadotropin releasing hormone treatment of dairy cows with ovarian cysts. I. Gross ovarian morphology and endocrinology. Theriogenology 16:207-217. https://doi.org/10.1016/0093-691X(81)90103-5
  11. Osterberg L, Akeson M, Levan K, Partheen K, Zetterqvist BM, Brannstrom M and Horvath G. 2006. Genetic alterations of serous borderline tumors of the ovary compared to stage I serous ovarian carcinomas. Cancer Genet. Cytogenet. 167:103-108. https://doi.org/10.1016/j.cancergencyto.2006.01.009
  12. Rahilly M, Carder PJ, al Nafussi A and Harrison DJ. 1991. Distribution of glutathione S-transferase isoenzymes in human ovary. J. Reprod. Fertil. 93:303-311. https://doi.org/10.1530/jrf.0.0930303
  13. Somyoonsap P, Tani A, Charoenpanich J, Minami T, Kimbara K and Kawai F. 2008. Involvement of PEG-carboxylate dehydrogenase and glutathione S-transferase in PEG metabolism by Sphingopyxis macrogoltabida strain 103. Appl. Microbiol. Biotechnol. 81:473-484. https://doi.org/10.1007/s00253-008-1635-7
  14. Tan H, Zhong Y and Pan Z. 2009. Autocrine regulation of cell proliferation by estrogen receptor-alpha in estrogen receptor-alpha-positive breast cancer cell lines. BMC Cancer 9:31. https://doi.org/10.1186/1471-2407-9-31
  15. Yang Y, Parsons KK, Chi L, Malakauskas SM and Le TH. 2009. Glutathione S-transferase-microl regulates vascular smooth muscle cell proliferation, migration, and oxidative stress. Hypertension 54:1360-1368. https://doi.org/10.1161/HYPERTENSIONAHA.109.139428
  16. Zhong S, Wyllie AH, Barnes D, Wolf CR and Spurr NK. 1993. Relationship between the GSTM1 genetic polymorphism and susceptibility to bladder, breast and colon cancer. Carcinogenesis 14:1821-1824. https://doi.org/10.1093/carcin/14.9.1821