Antioxidant superoxide dismutase - a review: its function, regulation in the testis, and role in male fertility☆

References

1. • Fridovich I.
   The biology of oxygen radicals.
   Science. 1978; 201: 875-880
   View in Article

   • Google Scholar
2. • McCord J.M.
   Human disease, free radicals, and the oxidant/antioxidant balance.
   Clin Biochem. 1993; 26: 351-357
   View in Article

   • Google Scholar
3. • Papas A.M.
   Determinants of antioxidant status in humans.
   Lipids. 1996; 31: S77-S82
   View in Article

   • Google Scholar
4. • Setchell B.P.
   • Waites G.M.H.
   The blood-testis barrier.
   in: Hamilton D.W. Greep R.O. Handbook of physiology. Vol 5. Williams & Wilkens, Baltimore, MD1989: 143-172
   View in Article

   • Google Scholar
5. • de Kretser D.M.
   • Kerr J.B.
   The cytology of the testis.
   in: Knobil E. Neill J. The physiology of reproduction. Vol 1. Raven Press, New York1988: 837-932
   View in Article

   • Google Scholar
6. • Adams J.D.
   • Odunze I.N.
   Oxygen free radicals and Parkinson’s disease.
   Free Radic Biol Med. 1991; 10: 161-169
   View in Article

   • Google Scholar

7. Jacob RA, Burri BJ. Oxidative damage and defense. Am J Clin Nutr 1006;63:985S–90S.

   View in Article

   • Google Scholar
8. • Multhaup G.
   • Ruppert T.
   • Schlicksupp A.
   • et al.
   Reactive oxygen species and Alzheimer’s disease.
   Biochem Pharmacol. 1997; 54: 533-539
   View in Article

   • Google Scholar
9. • Halliwell B.
   Antioxidants in human health and disease.
   Ann Rev Nutr. 1996; 16: 33-50
   View in Article

   • Google Scholar
10. • Halliwell B.
    Antioxidants.
    in: Sies H. Antioxidants in disease mechanisms and therapy. Vol. 38. Academic Press, New York1997: 3-20
    View in Article

    • Google Scholar
11. • Fridovich I.
    Biological effects of the superoxide radical.
    Arch Biochem Biophys. 1986; 15: 1-11
    View in Article

    • Google Scholar
12. • McCord J.M.
    • Fridovich I.
    Superoxide dismutase.
    Free Radic Biol Med. 1988; 5: 363-369
    View in Article

    • Google Scholar
13. • Groves J.T.
    Peroxynitrite.
    Curr Opin Chem Biol. 1999; 3: 226-235
    View in Article

    • Google Scholar
14. • Springall D.R.
    Nitric oxide—friend or foe.
    J Pathol. 1995; 175: 165-166
    View in Article

    • Google Scholar
15. • Huang E.P.
    Nitric oxide.
    Curr Biol. 1999; 28: R42
    View in Article

    • Google Scholar
16. • Groves J.T.
    • Wang C.C.Y.
    Nitric oxide synthase.
    Curr Opin Chem Biol. 2000; 4: 687-695
    View in Article

    • Google Scholar
17. • Radi R.
    • Beckman J.S.
    • Bush K.M.
    • Freeman B.A.
    Peroxynitrite-induced membrane lipid peroxidation.
    Arch Biochem Biophys. 1991; 288: 481-487
    View in Article

    • Google Scholar
18. • Van Poppel G.
    • van den Berg H.
    Vitamins and cancer.
    Cancer Lett. 1997; 114: 195-202
    View in Article

    • Google Scholar
19. • Lee I.M.
    Antioxidant vitamins in the prevention of cancer.
    Proc Assoc Am Physicians. 1999; 111: 10-15
    View in Article

    • Google Scholar
20. • Li D.
    • Devaraj S.
    • Fuller C.
    • Bucala R.
    • Jialal I.
    Effect of α-tocopherol on LDL oxidation and glycation.
    J Lipid Res. 1996; 37: 1978-1986
    View in Article

    • Google Scholar
21. • Stampfer M.J.
    • Hennekens C.H.
    • Manson J.E.
    • Colditz G.A.
    • Rosner B.
    • Willett W.C.
    Vitamin E consumption and the risk of coronary disease in women.
    N Eng J Med. 1993; 328: 1444-1449
    View in Article

    • Google Scholar
22. • Rimm E.R.
    • Stampfer M.J.
    • Ascherio A.
    • Giovannucci E.
    • Colditz G.A.
    • Willet W.C.
    Vitamin E consumption and the risk of coronary heart disease in men.
    N Eng J Med. 1993; 328: 1450-1456
    View in Article

    • Google Scholar
23. • Traber M.G.
    • Packer L.
    Vitamin E.
    Am J Clin Nutr. 1995; 62: 1501S-1509S
    View in Article

    • Google Scholar
24. • Palmer H.J.
    • Paulson K.E.
    Reactive oxygen species and antioxidants in signal transduction and gene expression.
    Nutr Rev. 1997; 55: 353-361
    View in Article

    • Google Scholar
25. • Carlberg C.
    Lipid soluble vitamins in gene regulation.
    Biofactors. 1999; 10: 91-97
    View in Article

    • Google Scholar
26. • Gopalakrishna R.
    • Jaken S.
    Protein kinase C signaling and oxidative stress.
    Free Radic Biol Med. 2000; 28: 1349-1361
    View in Article

    • Google Scholar
27. • Wu S.H.
    • Oldfield J.E.
    • Whanger P.D.
    • Weswig P.H.
    Effect of selenium, vitamin E, and antioxidants on testicular function in rats.
    Biol Reprod. 1973; 8: 625-629
    View in Article

    • Google Scholar
28. • Bensoussan K.
    • Morales C.R.
    • Hermo L.
    Vitamin E deficiency causes incomplete spermatogenesis and affects the structural differentiation of epithelial cells of the epididymis in the rat.
    J Androl. 1998; 19: 266-288
    View in Article

    • Google Scholar
29. • Brigelius-Flohe R.
    • Traber M.G.
    Vitamin E.
    FASEB J. 1999; 13: 1145-1155
    View in Article

    • Google Scholar
30. • Raha S.
    • Robinson B.H.
    Mitochondria, oxygen free radicals, disease, and aging.
    Trends Biochem Sci. 2000; 25: 502-508
    View in Article

    • Google Scholar
31. • Marklund S.L.
    Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species.
    Biochem J. 1984; 222: 649-655
    View in Article

    • Google Scholar
32. • Marklund S.L.
    Extracellular superoxide dismutase in human tissues and human cell lines.
    Clin Invest. 1984; 74: 1398-1403
    View in Article

    • Google Scholar

33. Oury TD, Day BJ, Crapo JD. Extracellular superoxide dismutase in vessels and airways of humans and baboons. Free Radic Biol Med 20:957–65.

    View in Article

    • Google Scholar
34. • Sandstrom J.
    • Karlsson K.
    • Edlund A.
    • Marklund S.L.
    The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity.
    J Biol Chem. 1992; 267: 18205-18209
    View in Article

    • Google Scholar
35. • Willems J.
    • Zwijsen A.
    • Slegers H.
    • et al.
    Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma.
    J Biol Chem. 1993; : 14614-14621
    View in Article

    • Google Scholar
36. • Carlsson L.M.
    • Marklund S.L.
    • Edlund T.
    The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid.
    Proc Natl Acad Sci USA. 1996; 93: 5219-5222
    View in Article

    • Google Scholar
37. • Karlsson K.
    • Marklund S.L.
    Extracellular superoxide dismutase in the vascular system of mammals.
    Biochem J. 1988; 255: 223-228
    View in Article

    • Google Scholar
38. • Mruk D.
    • Cheng C.H.
    • Cheng Y.H.
    • et al.
    Rat testicular extracellular superoxide dismutase.
    Biol Reprod. 1998; 59: 298-308
    View in Article

    • Google Scholar
39. • Petrone W.F.
    • English D.K.
    • Wong K.
    • McCord J.M.
    Free radicals and inflammation.
    Proc Natl Acad Sci USA. 1980; 77: 1159-1163
    View in Article

    • Google Scholar
40. • Folz R.J.
    • Abushamaa A.M.
    • Suliman H.B.
    Extracellular superoxide dismutase in the airways of transgenic mice reduces inflammation and attenuates lung toxicity following hyperoxia.
    J Clin Invest. 1999; 103: 1055-1066
    View in Article

    • Google Scholar
41. • Mruk D.D.
    • Cheng C.Y.
    In vitro regulation of extracellular superoxide dismutase in Sertoli cells.
    Life Sci. 2000; 67: 133-145
    View in Article

    • Google Scholar
42. • Silvestrini B.
    • Guglielmotti A.
    • Saso L.
    • Cheng C.Y.
    Changes in concanavalin A-reactive proteins in inflammatory disorders.
    Clin Chem. 1989; 35: 2207-2211
    View in Article

    • Google Scholar
43. • Hensley K.
    • Robinson K.A.
    • Gabbita S.P.
    • Salsman S.
    • Floyd R.A.
    Reactive oxygen species, cell signaling, and cell injury.
    Free Radic Biol Med. 2000; 28: 1456-1462
    View in Article

    • Google Scholar
44. • Miller M.J.
    • McNeill H.
    • Mullane K.M.
    • Caravella S.J.
    • Clark D.A.
    SOD prevents damage and attenuates eicosanoid release in a rabbit model of necrotizing enterocolitis.
    Am J Physiol. 1988; 255: G556-G565
    View in Article

    • Google Scholar
45. • Emerit J.
    • Pelletier S.
    • Tosoni-Verilgnue D.
    • Mollet M.
    Phase II trial of copper/zinc superoxide dismutase (CuZn SOD) in treatment of Crohn’s disease.
    Free Radic Biol Med. 1989; 7: 145-149
    View in Article

    • Google Scholar
46. • Peltola V.
    • Huhtaniemi I.
    • Ahotupa M.
    Antioxidant enzyme activity in the maturing rat testis.
    J Androl. 1991; 13: 450-455
    View in Article

    • Google Scholar
47. • Jow W.W.
    • Schlegel P.N.
    • Cichon Z.
    • Phillips D.
    • Goldstein M.
    • Bardin C.W.
    Identification and localization of copper-zinc superoxide dismutase gene expression in rat testicular development.
    J Androl. 1993; 14: 439-447
    View in Article

    • Google Scholar
48. • Bauche F.
    • Fouchard M.H.
    • Jegou B.
    Antioxidant system in the rat testicular cells.
    FEBS Lett. 1993; 349: 392-396
    View in Article

    • Google Scholar
49. • Gu W.
    • Morales C.
    • Hecht N.B.
    In male mouse germ cells, copper-zinc superoxide dismutase utilizes alternative promoters that produce multiple transcripts with different translation potential.
    J Biol Chem. 1995; 270: 236-243
    View in Article

    • Google Scholar
50. • Perry A.C.F.
    • Jones R.
    • Hall L.
    Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression.
    Biochem J. 1993; 293: 21-25
    View in Article

    • Google Scholar
51. • Arivandan G.R.
    • Pineau C.P.
    • Bardin C.W.
    • Cheng C.Y.
    Ability of trypsin in mimicking germ cell factors that affect Sertoli cell secretory function.
    J Cell Physiol. 1996; 168: 123-133
    View in Article

    • Google Scholar
52. • Arivandan G.R.
    • Mruk D.
    • Lee W.M.
    • Cheng C.Y.
    Identification, isolation, and characterization of a 41-kilodalton protein from rat germ cell-conditioned medium exhibiting concentration-dependent dual biological activities.
    Endocrinology. 1997; 138: 3259-3268
    View in Article

    • Google Scholar
53. • Marklund S.L.
    Superoxide dismutase in human tissues, cells, and extracellular fluids.
    in: Johnson J.E. Walford R. Harman D. Miguel J. Free radicals, aging, and degenerative diseases. 1st ed. Alan R Liss, New York1986: 509-526
    View in Article

    • Google Scholar
54. • Marklund S.L.
    • Holme E.
    • Hellner L.
    Superoxide dismutase in extracellular fluids.
    Clin Chem Acta. 1982; 126: 41-51
    View in Article

    • Google Scholar
55. • Folz R.J.
    • Guan J.
    • Seldin M.F.
    • Oury T.D.
    • Enghild J.J.
    • Crapo J.D.
    Mouse extracellular superoxide dismutase.
    Am J Respir Cell Mol Biol. 1997; 17: 393-403
    View in Article

    • Google Scholar
56. • Peltola V.
    • Parvinen M.
    • Huhtaniemi I.
    • Kulmala J.
    • Ahotupa M.
    Comparison of effects of 0.5 and 3.0 Gy X-irradiation on lipid peroxidation and antioxidant enzyme function in rat testis and liver.
    J Androl. 1993; 14: 267-274
    View in Article

    • Google Scholar
57. • Russell L.D.
    • Tallon-Doran M.
    • Weber J.E.
    • Wong V.
    • Peterson R.N.
    Three-dimensional reconstruction of a rat stage V Sertoli cell.
    Am J Anat. 1983; 167: 181-192
    View in Article

    • Google Scholar
58. • Weber J.E.
    • Russell L.D.
    • Wong V.
    • Peterson R.N.
    Three-dimensional reconstruction of a rat stage V Sertoli cell.
    Am J Anat. 1983; 167: 163-179
    View in Article

    • Google Scholar
59. • Wong V.
    • Russell L.D.
    Three-dimensional reconstruction of a rat V Sertoli cell.
    Am J Anat. 1983; 167: 143-161
    View in Article

    • Google Scholar
60. • Li J.C.H.
    • Samy E.T.
    • Grima J.
    • Chung S.S.W.
    • Mruk D.
    • Lee W.M.
    • Silvestrini B.
    • Cheng C.Y.
    Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis.
    J Cell Physiol. 2000; 185: 366-385
    View in Article

    • Google Scholar
61. • Oury T.D.
    • Chang L.Y.
    • Marklund S.L.
    • Day B.J.
    • Crapo J.D.
    Immunocytochemical localization of extracellular superoxide dismutase in human lung.
    Lab Invest. 1994; 70: 889-898
    View in Article

    • Google Scholar
62. • Siwik D.A.
    • Pagano P.J.
    • Colucci W.S.
    Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts.
    Am J Physiol Cell Physiol. 2001; 280: C53-C60
    View in Article

    • Google Scholar
63. • Marklund S.L.
    Regulation by cytokines of extracellular superoxide dismutase and other superoxide dismutase isoenzymes in fibroblasts.
    J Biol Chem. 1992; 267: 6696-6701
    View in Article

    • Google Scholar
64. • Rao R.K.
    • Baker R.D.
    • Baker S.S.
    • Gupta A.
    • Holycross M.
    Oxidant-induced disruption of intestinal epithelial barrier function.
    Am J Physiol Gastrointest Liver Physiol. 1997; 273: G812-G823
    View in Article

    • Google Scholar
65. • Hecht D.
    • Zick Y.
    Selective inhibition of protein tyrosine phosphatase activities by H₂O₂ and vanadate in vitro.
    Biochem Biophys Res Commun. 1992; 188: 773-779
    View in Article

    • Google Scholar
66. • Heffetz D.
    • Bushkin H.
    • Dror R.
    • Zick Y.
    The insulinomimetic agents H₂O₂ and vanadate stimulate protein tyrosine phosphorylation in intact cells.
    J Biol Chem. 1990; 265: 2896-2902
    View in Article

    • Google Scholar
67. • Rao R.K.
    • Li L.
    • Baker R.D.
    • Baker S.S.
    • Gupta A.
    Glutathione oxidation and PTPase inhibition by hydrogen peroxide in Caco-2 cell monolayer.
    Am J Physiol Gastrointest Liver Physiol. 2000; 279: G332-G340
    View in Article

    • Google Scholar
68. • Lagrange P.
    • Romero I.A.
    • Minn A.
    • Revest P.A.
    Transendothelial permeability changes induced by free radicals in an in vitro model of the blood-brain barrier.
    Free Radic Biol Med. 1999; 27: 667-672
    View in Article

    • Google Scholar
69. • Olson L.
    • Ayer-LeLievre C.
    • Ebendal T.
    • Seiger A.
    Nerve growth factor-like immunoreactivities in rodent salivary glands and testis.
    Cell Tissue Res. 1987; 248: 275-286
    View in Article

    • Google Scholar
70. • Parvinen M.
    • Pelto-Huikko M.
    • Soder O.
    • et al.
    Expression of β-nerve growth factor and its receptor in rat seminiferous epithelium.
    J Cell Biol. 1992; 117: 629-641
    View in Article

    • Google Scholar
71. • Dejucq N.
    • Dugast I.
    • Ruffault A.
    • Van der Meide P.H.
    • Jegou B.
    Interferon-α and -γ expression in the rat testis.
    Endocrinology. 1995; 136: 4925-4931
    View in Article

    • Google Scholar
72. • Wang J.E.
    • Josefsen G.M.
    • Hansson V.
    • Haugen T.B.
    Residual bodies and IL-1α stimulate expression of mRNA for IL-1α and IL-1 receptor type I in cultured rat Sertoli cells.
    Mol Cell Endocrinol. 1998; 137: 139-144
    View in Article

    • Google Scholar
73. • Sunderesan M.
    • Yu Z.X.
    • Ferrans V.J.
    • Irani K.
    • Finkel T.
    Requirement for generation of H₂O₂ for PDGF signal transduction.
    Science. 1995; 270: 296-299
    View in Article

    • Google Scholar
74. • Bae Y.S.
    • Kang S.W.
    • Seo M.S.
    • Baines I.C.
    • Tekle E.
    • Chock P.B.
    • Rhee S.G.
    Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation.
    J Biol Chem. 1997; 272: 217-221
    View in Article

    • Google Scholar
75. • Lee S.R.
    • Kwon K.S.
    • Kim S.R.
    • Rhee S.G.
    Reversible inactivation of protein tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor.
    J Biol Chem. 1998; 273: 15366-15372
    View in Article

    • Google Scholar