Developmental expression of glutathione peroxidase, catalase, and manganese superoxide dismutase mRNAs during spermatogenesis in the mouse

Journal of Andrology

Volumn 17, Issue 3, 1996, Pages 256-262

  Gu, Wei ^a   Hecht, Norman B ^a  

^a TUFTS UNIVERSITY   (United States)

Author keywords

Antioxidant enzymes; gene expression; testis; translational regulation

Indexed keywords

CATALASE; GLUTATHIONE PEROXIDASE; MANGANESE;

ANIMAL CELL; ARTICLE; CELL PROTECTION; DNA DAMAGE; DNA PROBE; ENZYME ACTIVITY; MALE; MEIOSIS; MOUSE; NONHUMAN; NORTHERN BLOTTING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; REGENERATION; SPERMATOGENESIS;

ANIMALS; BLOTTING, NORTHERN; CATALASE; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE PEROXIDASE; MALE; MICE; MICE, INBRED STRAINS; POLYRIBOSOMES; RNA, MESSENGER; SPERMATOGENESIS; SPERMATOZOA; SUPEROXIDE DISMUTASE; TESTIS;

EID: 0029998368     PISSN: 01963635     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (49)

1. Aebi M. Catalase in vitro. Methods Enzymol 1984;105:121-126.
2. Aitken RJ, Clarkson JS. Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa. J Reprod Fertil 1987;81:459-469.
3. Aitken RJ, Clarkson JS, Fishel S. Generation of reactive oxygen species, lipid peroxidation and human sperm function. Biol Reprod 1989;40:183-197.
4. Aitken RJ, Irvine DS, Wu FC. Prospective analysis of sperm-oocyte fusion and reactive oxygen species generation as criteria for the diagnosis of infertility. Am J Obstet Gynecol 1991;164:542-551.
5. Alcivar AA, Hake LE, Millette CM, Trasler JM, Hecht NB. Mitochondrial gene expression in male germ cells of the mouse. Dev Biol 1989;135:263-271.
6. Alvarez JG, Storey BT. Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid peroxidation. Gamete Res 1989;23:77-90.
7. Alvarez JG, Storey BT. Evidence for increased lipid peroxidative damage and loss of Superoxide dismutase activity as a model of sublethal cryodamage to human sperm during cryopreservation. J Androl 1992;13:232-241.
8. Alvarez JG, Touchstone JB, Blasco L, Storey BT. Spontaneous lipid peroxidation and production of hydrogen peroxide and Superoxide in human spermatozoa: Superoxide dismutase as major enzyme protectant against oxygen toxicity. J Androl 1987;8:338-348.
9. Ames BN, Shigenaga MK, Hagen TM. Oxidants, antioxidants and the degenerative disease of aging. Proc Natl Acad Sci USA 1993;90:7915-7922.
10. Avraham KB, Schickler M, Sapoznicov D, Yarom R, Groner Y. Down's syndrome: abnormal neuromuscular junction in tongue of transgenic mice with elevated level of human Superoxide dismutase. Cell 1988;54:823-829.
11. Barra D, Schinina ME, Simmaco M, Bannister JV, Bannister WH, Ratillio G, Bossa F. The primary structure of human liver manganese superoxide dismutase. J Biol Chem 1984;259:12595-12601.
12. Bauche F, Fouchard M, Jégou B. Antioxidant system in rat testicular cells. FEBS Lett 1994;349:392-396.
13. Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979;59:527-605.
14. Crow JE How much do you know about spontaneous human mutation rate? Environ Mol Mutagen 1993;21:122-129.
15. Crapo JD, Oury T, Rabouille C, Slot JW, Chang L-Y. Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc Natl Acad Sci USA 1992;89:10404-10409.
16. Davies KJA. Protein damage and degradation by oxygen radicals. J Biol Chem 1987;262:9895-9901.
17. Deng H-X, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung WY, Getzoff ED, Hu P, Herzfeldt B, Roos RP, Warner C, Deng G, Soriano E, Smyth C, Parge HE, Roses AD, Hollewell RA, Pericak-Vouce MA, Siddique T. Amyotrophic lateral sclerosis and structural defects in Cu, Zn Superoxide dismutase. Science 1993;261:1047.
18. Dryja TP, Shizuo M, Petersen R, Rapaport JM, Walton D, Yandell DW. Parental origin of mutations of the retinoblastoma gene. Nature 1989;339:556-558.
19. Elroy-Stein O, Bernstein Y, Groner Y. Overproduction of human superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J 1986;5:615-622.
20. Fridovich I. The biology of oxygen radicals. Science 1978;201:875-880.
21. Griveau JF, Dumont E, Renard P, Callegari JP, Lannou DL. Reactive oxygen species, lipid peroxidation and enzymatic defense systems in human spermatozoa. J Reprod Fertil 1995;103:17-26.
22. Gu W, Hecht NB. Translation of a testis-specific Cu/Zn Superoxide dismutase mRNA (SOD-1) is regulated by a 65 kDa which binds to its 5′ untranslated region. Mol Cell Biol 1996; in press.
23. Gu W, Hermo L, Hecht NB. In male mouse germ cells, copper-zinc superoxide dismutase utilizes alternative promoters that produce multiple transcripts with different translation potential. J Biol Chem 1995a:270:236-243.
24. Gu W, Kwon YH, Oko R, Hermo L, Hecht NB. Poly(A) binding protein is bound to both stored and polysomal mRNAs in the mammalian testis. Mol Reprod Dev 1995b;40:273-285.
25. Harman D. The aging process. Proc Natl Acad Sci USA 1981;78:7124-7128.
26. Harman D. Free radical theory of aging. Mutat Res 1992;275:257-266.
27. Ho Y-S, Crapo JD. Isolation and characterization of complementary DNA encoding human manganese-containing Superoxide dismutase. FEBS Lett 1992;229:256-260.
28. Holland MK, Alvarez JG, Storey BT. Production of Superoxide and activity of Superoxide dismutase in rabbit epididymal spermatozoa. Biol Reprod 1982;27:1109-1118.
29. Hurt J, Hsu J-L, Dougall WC, Visner GA, Burr IM, Nick HS. Multiple mRNA species generated by alternative polyadenylation from the rat manganese Superoxide dismutase gene. Nucleic Acids Res 1992;20:2985-2990.
30. Jeulin C, Soufir JC, Weber P, Laval-Martin D, Calvayrac R. Catalase activity in human spermatozoa and seminal plasma. Gamete Res 1989;24:185-196.
31. Jones PL, Kucera G, Gordon H, Boss JM. Cloning and characterization of the murine manganous Superoxide dismutase-encoding gene. Gene 1995;153:155-161.
32. Jow WW, Schlegel PN, Chicon Z, Philips D, Goldstein M, Bardin CW. Identification and localization of copper-zinc Superoxide dismutase gene expression in rat testicular development. J Androl 1993;14:439-447.
33. Kleene KC. Poly(A) shortening accompanies the activation of five mRNAs during spermatogenesis in the mouse. Development 1989;106:367-373.
34. Kleene KC, Distel RJ, Hecht NB. Translational regulation and deadenylation of a protaraine mRNA during spermatogenesis in the mouse. Dev Biol 1984;105:71-79.
35. Loschen G, Azzi A, Richter C, Flohe L. Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett 1974;42:68-72.
36. Mastuda Y, Seki N, Utsugi-Takeuchi T, Tobari I. X-ray and mitomycin C (MMC)-induced chromosome aberrations in spermatogenic germ cells and the repair capacity of mouse eggs for X-ray and MMC damage. Mutat Res 1989;211:67-75.
37. Menella MR, Jones R. Properties of spermatozoal Superoxide dismutase and lack of involvement of Superoxides in metal ion catalyzed lipid-peroxidation reactions in semen. Biochem J 1980;191:289-297.
38. Nanogaki T, Noda Y, Narimoto K, Shiotani M, Mori T, Matsuda T, Yoshida O. Localization of Cu/Zn-superoxide dismutase in the human male genital organs. Hum Reprod 1992;7:81-85.
39. National Research Council. Health Effects of Exposure to Low Levels of Ionizing Radiation. BEIV V. Washington, DC: National Academy Press; 1990.
40. Peskin AV, Shlyahova L. Cell nuclei generate DNA-nicking Superoxide radicals. FEBS Lett 1986;194:317-321.
41. Petters-Jori C, Vandervoorde A, Baudhuin P Subcellular localization of Superoxide dismutase in rat liver. Biochem J 1975;150:131-139.
42. Robinson BS, Johnson DW, Poulos A. Novel molecular species of sphin-gomyelin containing 2-hydroxylated polyenic very long chain fatty acids in mammalian testes and spermatozoa. J Biol Chem 1992;267:1746-1751.
43. Rosen DR, Siddique T, David P, Figlewicz DA, Sapp P, Donaldson D, Goto JP, Deng H-X, Rahmani Z, Krizus A, McKenna-Yasek D, Cayabyab A, Gaston SM, Berger R, Tanzi E, Halperin JJ, Herzfeldt B, Van der Bergh R, Hong WY, Bird T, Deng G, Mulder DW, Smyth C, Liang NO, Gusella JS, Horvitz HR, Brown RH Jr. Mutations in Cu/ Zn Superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993;362:59-62.
44. Salin ML, Day ED, Crapo JD. Isolation and characterization of a manganese containing Superoxide dismutase for rat liver. Arch Biochem Biophys 1978;187:223-228.
45. Slot J, Geuze H, Freeman B, Crapo JD. Inlracellular localization of the copper-zinc and manganese Superoxide dismutase in rat liver parenchymal cells. J Lab Invest 1986;55:363-371.
46. Stadtman ER. Protein oxidation and aging. Science 1992;257:1220-1224.
47. Van Loon AA, Boer PJ, Van der Schans GP, Mackenbach P, Grootegoed JA, Baan RA, Lohman PHM. Immunochemical detection of DNA damage induction and repair at different cellular stages of spermatogenesis of the hamster after in vitro or in vivo exposure to ionizing radiation. Exp Cell Res 1991;193:303-309.
48. Vogel F, Rathenberg R. Review: spontaneous mutation in man. Adv Hum Genet 1975;5:223-318.
49. Wagner JR, Hu CC, Ames BN. Endogenous oxidative damage of deoxycytidine in DNA. Proc Natl Acad Sci USA 1992;89:3380-3384.