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Reactive Oxygen Species and Antioxidants in Luteal Cell Demise

  • Chapter
Cell Death in Reproductive Physiology

Part of the book series: Proceedings in the Serono Symposia USA Series ((SERONOSYMP))

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Abstract

The corpus luteum is the end-differentiated state of the primordial follicle and one of the major endocrine substructures of the ovary. The formation and involution of the corpus luteum occurs by processes that are regulated by endocrine, paracrine, and intracrine agents of the pituitary, the uterus (in nonprimates), the ovary, and the immune system. The physiological role of the corpus luteum is the secretion of products necessary for the establishment and maintenance of pregnancy. The more prominent luteal products are progesterone, estrogens, androgens, and peptides such as relaxin and oxytocin. Other products include inhibin and its family members, eicosanoids, cytokines, growth factors, and oxygen radicals. It is now evident that the historical perspective of the corpus luteum as an organ of progesterone and estradiol secretion governed solely by feedback regulation of luteinizing hormone (LH) is inadequate. In this chapter, we offer one view of corpus luteum regression and its regulation based on recent findings of this lab and others using the pseudopregnant rat model.

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References

  1. Aune TM, Thomas EL. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur J Biochem 1977; 80: 209–14.

    Article  PubMed  CAS  Google Scholar 

  2. Test ST, Weiss J. The generation of utilization of chlorinated oxidants by human neutrophile. Adv Free Rad Biol Med 1986; 2: 91–116.

    Article  CAS  Google Scholar 

  3. Uehara K, Hori K, Nakano M, Koga S. Highly sensitive chemiluminescence method for determining myeloperoxidase in human polymorphonuclear leukocytes. Anal Biochem 1991; 199: 191–6.

    Article  PubMed  CAS  Google Scholar 

  4. Palmer RMJ, Ferrige AG, Moncada S. Nitric oxide accounts for the biological activity of endothelium-derived relaxing factor. Nature 1987; 327: 524–6.

    Article  PubMed  CAS  Google Scholar 

  5. Schmidt HHW, Warner TD, Ishii K, Sheng H, Murad F. Insulin secretion from pancreatic B cells caused by L-arginine-derived nitrogen oxides. Science 1992; 255: 721–3.

    Article  PubMed  CAS  Google Scholar 

  6. Floris R, Piersma SR, Yang G, Jones P, Wever R. Interaction of myeloperoxidase with peroxynitrite. A comparison with lactoperoxidase, horseradish peroxidase and cata-lase. Eur J Biochem 1993; 215: 767–75.

    Article  PubMed  CAS  Google Scholar 

  7. Stelmaszynska T, Kukovetz E, Egger G, Schaur RJ. Possible involvement of myeloperoxidase in lipid peroxidation. Int J Biochem 1992; 24: 121–8.

    Article  PubMed  CAS  Google Scholar 

  8. Wiedau-Pazos M, Goto JJ, Rabizadeh S, et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996; 271: 515–8.

    Article  PubMed  CAS  Google Scholar 

  9. Gryglewski RJ, Palmer RM, Moncada S. Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor. Nature 1986; 320: 454–6.

    Article  PubMed  CAS  Google Scholar 

  10. Marklund S, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974; 47: 469–74.

    Article  PubMed  CAS  Google Scholar 

  11. Schuman EM, Madison DV. A requirement for the intracellular messenger nitric oxide in long-term potentiation. Science 1991; 254: 1503–6.

    Article  PubMed  CAS  Google Scholar 

  12. Halliwell B, Gutteridge JMC. Free radicals in biology and medicine. Oxford: Oxford University Press, 1989.

    Google Scholar 

  13. Morel F, Doussiere J, Vignais PV. The superoxide-generating oxidase of phagocytic cells. Eur J Biochem 1991; 201: 523–46.

    Article  PubMed  CAS  Google Scholar 

  14. Nunez J, Pommier J. Formation of thyroid hormones. Vitamins and hormones 1982; 39: 175–229.

    Article  PubMed  CAS  Google Scholar 

  15. Zweier JL, Kuppusamy P, Lutty GA. Measurement of endothelial cell free radical generation: evidence for a central mechanism of free radical injury in postischemic tissues. Proc Nail Acad Sci USA 1988; 85: 4046–50.

    Article  CAS  Google Scholar 

  16. Dupuy C, Virion A, Ohayon R, Kaniewski J, Deme D, Pommier J. Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane. J Biol Chem 1991; 266: 3739–43.

    PubMed  CAS  Google Scholar 

  17. Maly F-E. The B lymphocyte: a newly recognized source of reactive oxygen species with immunoregulatory potential. Free Rad Res Comm 1990; 8: 143–8.

    Article  CAS  Google Scholar 

  18. Meier B, Cross AR, Hancock JT, Kaup FJ, Jones OTG. Identification of a superoxide-generating NADPH oxidase system in human fibroblasts. Biochem J 1991; 275: 241–5.

    PubMed  CAS  Google Scholar 

  19. Krieger-Brauer HI, Kather H. Human fat cells possess a plasma membrane-bound H2O2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase. J Clin Invest 1992; 89: 1006–13.

    Article  PubMed  CAS  Google Scholar 

  20. Alvarez JG, Touchstone JC, 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. JAndrol 1987; 8: 338–48.

    CAS  Google Scholar 

  21. Aitken RJ, Clarkson JS, Fishel S. Generation of reactive oxygen species, lipid peroxidation, and human sperm function. Biol Reprod 1989; 40: 183–97.

    Article  Google Scholar 

  22. Shapiro BM. The control of oxidant stress at fertilization. Science 1991; 252: 533–6.

    Article  PubMed  CAS  Google Scholar 

  23. Sawada M, Carlson JC. Superoxide radical production in plasma membrane samples from regressing corpora lutea. Can J Physiol Pharmacol 1989; 67: 465–71.

    Article  PubMed  CAS  Google Scholar 

  24. Sawada M, Carlson JC. Studies on the mechanism controlling generation of superoxide radical in luteinized rat ovaries during regression. Endocrinology 1994; 135: 1645–50.

    Article  PubMed  CAS  Google Scholar 

  25. Riley JCM, Behrman HR. In vivo generation of hydrogen peroxide in the rat corpus luteum during luteolysis. Endocrinology 1991; 128: 1749–53.

    Article  PubMed  CAS  Google Scholar 

  26. Sawada M, Carlson JC. Association of lipid peroxidation during luteal regression in the rat and natural aging in the rotifer. Exp Gerontol 1985; 20: 179–86.

    Article  PubMed  CAS  Google Scholar 

  27. Aten RF, Duarte KM, Behrman HR. Regulation of ovarian antioxidant vitamins, reduced glutathione, and lipid peroxidation by luteinizing hormone and prostaglandin Fen. Biol Reprod 1992; 46: 401–7.

    Article  PubMed  CAS  Google Scholar 

  28. Sugino M, Nakamura Y, Takeda O, Ishimatsu M, Kato H. Changes in activities of superoxide dismutase and lipid peroxide in corpus luteum during pregnancy in rats. J Reprod Fertil 1993; 97: 347–51.

    Article  PubMed  CAS  Google Scholar 

  29. Bucco RA, Melner МН, Gordon DS, Leers-Sucheta S, Ong DE. Inducible expression of cellular retinoic acid-binding protein II in rat ovary: gonadotropin regulation during luteal development. Endocrinology 1995; 136: 2730–40.

    Article  PubMed  CAS  Google Scholar 

  30. Bulmer D. The histochemistry of ovarian macrophages in the rat. J Anat Lond 1964; 98: 313–9.

    CAS  Google Scholar 

  31. Kirsch TM, Friedman AC, Vogel RL, Flickinger GL. Macrophages in corpora lutea of mice: characterization and effects on steroid secretion. Biol Reprod 1981; 25: 629–38.

    Article  PubMed  CAS  Google Scholar 

  32. Adams EC, Hertig AT. Studies on the human corpus luteum. I. Observations on the ultrastructure of development and regression of the luteal cells during the menstrual cycle. J Cell Biol 1969; 41: 696–715.

    Article  PubMed  CAS  Google Scholar 

  33. Bagavandoss P, Wiggins RC, Kunkel SL, Remick DG, Keyes PL. Tumor necrosis factor production and accumulation of inflammatory cells in the corpus luteum of pseudopregnancy and pregnancy in rabbits. Biol Reprod 1990; 42: 367–76.

    Article  PubMed  CAS  Google Scholar 

  34. Murdoch WJ. Treatment of sheep with prostaglandin F2a enhances production of a luteal chemoattractant for eosinophils. Am J Reprod Immunol 1987; 15: 52–6.

    CAS  Google Scholar 

  35. Pepperell JR, Wolcott K, Behrman HR. Luteolytic effect of neutrophils in rat luteal cells. Endocrinology 1992; 130: 1001–8.

    Article  PubMed  CAS  Google Scholar 

  36. Musicki B, Kodaman PH, Aten RF, Behrman HR. Endocrine regulation of ascorbic acid transport and secretion in luteal cells. Biol Reprod 1996; 54: 399–406.

    Article  PubMed  CAS  Google Scholar 

  37. Wright K, Luborsky-Moore JL, Behrman HR. Specific binding of prostaglandin F2a to membranes of rat corpora lutea. Mol Cell Endocrinol 1979; 13: 25–34.

    Article  PubMed  CAS  Google Scholar 

  38. Wright K, Pang CY, Behrman HR. Luteal membrane binding to PGF2a and sensitivity of corpora lutea to PGF2a induced luteolysis in pseudopregnant rats. Endocrinology 1980; 106: 1333–7.

    Article  PubMed  CAS  Google Scholar 

  39. Steadman LE, Murdock WJ. Production of leukotriene B4 by luteal tissue of sheep treated with prostaglandin F2 alpha. Prostaglandins 1988; 36: 741–5.

    Article  PubMed  CAS  Google Scholar 

  40. Visner GA, Dougall WC, Wilson JM, Burr IA, Nick HS. Regulation of manganese superoxide dismutase by lipopolysaccharide, interleukin-1, and tumor necrosis factor. J Biol Chem 1990; 265: 2856–64.

    PubMed  CAS  Google Scholar 

  41. Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979; 59: 527–605.

    PubMed  CAS  Google Scholar 

  42. Meister A, Anderson ME. Glutathione. Annu Rev Biochem 1983; 52: 711–60.

    Article  PubMed  CAS  Google Scholar 

  43. Prabir KD. Tissue distribution of constitutive and induced soluble peroxidase in the rat. Eur J Biochem 1992; 206: 59–67.

    Article  Google Scholar 

  44. Edwards SW, Nurcombe HL, Hart CA. Oxidative inactivation of myeloperoxidase released from human neutrophils. Biochem J 1987; 245: 925–8.

    PubMed  CAS  Google Scholar 

  45. Arnao MB, Acosta М, del Rio JA, Garcia-Canovas F. Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agent. Biochim Biophys Acta 1990; 1038: 85–9.

    Article  PubMed  CAS  Google Scholar 

  46. Kolodecik TR, Aten RF, Behrman HR. Interaction of ascorbic acid or thiocyanate with peroxidase blocks the action of hydrogen peroxide in rat luteal cells. Biol Reprod 1994; 50 (Suppl 1): 152.

    Google Scholar 

  47. Rose RC. Transport of ascorbic acid and other water-soluble vitamins. Biochim Biophys Acta 1988; 947: 335–66.

    Article  PubMed  CAS  Google Scholar 

  48. Stansfield DA, Flint AP. The entry of ascorbic acid into the corpus luteum in vivo and in vitro and the effect of luteinizing hormone. J Endocrinol 1967; 39: 27–35.

    Article  PubMed  CAS  Google Scholar 

  49. Levine M, Morita K. Ascorbic acid in endocrine systems. Vitamins and hormones. Vol. 42. New York: Academic Press, Inc., 1985: 1–64.

    Google Scholar 

  50. Grollman AP, Lehninger AL. Enzymic synthesis of L-ascorbic acid in different animal species. Arch Biochem Biophys 1957; 69: 458–67.

    Article  PubMed  CAS  Google Scholar 

  51. Behrman HR, Preston SL, Aten RF, Rinaudo P, Zreik T. Hormone induction of ascorbic acid transport in immature granulosa cells. Endocrinology 1996; 137: 4316–21.

    Article  PubMed  CAS  Google Scholar 

  52. Drevon CA. Absorption, transport and metabolism of vitamin E. Free Rad Res Comm 1991; 14: 229–46.

    Article  CAS  Google Scholar 

  53. Packer L. Protective role of vitamin E in biological systems. Am J Clin Nutr 1991; 53: 10505–55.

    Google Scholar 

  54. Traber MG, Kayden HJ. Vitamin E is delivered to cells via the high affinity receptor for low-density lipoprotein. Am J Clin Nutr 1984; 40: 747–51.

    CAS  Google Scholar 

  55. Aten RF, Kolodecik TR, Behrman HR. Ovarian vitamin E accumulation: evidence for a role of lipoproteins. Endocrinology 1994; 135: 533–9.

    CAS  Google Scholar 

  56. Yuting C, Rongliang Z, Zhongjian J, Yong J. Flavonoids as superoxide scavengers and antioxidants. Free Rad Biol Med 1990; 9: 19–21.

    Article  Google Scholar 

  57. Bendich A, Olson JA. Biological actions of carotenoids. FASEB J 1989; 3: 1927–32.

    PubMed  CAS  Google Scholar 

  58. Krinsky NI. Antioxidant functions of carotenoids. Free Rad Biol Med 1989; 7: 617–35.

    Article  PubMed  CAS  Google Scholar 

  59. Behrman HR, Preston SL. Luteolytic actions of peroxide in rat ovarian cells. Endocrinology 1989; 124: 2895–900.

    Article  PubMed  CAS  Google Scholar 

  60. Margolin Y, Aten RF, Behrman HR. Antigonadotropic and antisteroidogenic actions of peroxide in rat granulosa cells. Endocrinology 1990; 127: 245–50.

    Article  PubMed  CAS  Google Scholar 

  61. Gatzuli E, Aten RF, Behrman HR. Inhibition of gonadotropin action and progester-one synthesis by xanthine oxidase in rat luteal cells. Endocrinology 1991; 128: 2253–8.

    Article  PubMed  CAS  Google Scholar 

  62. Endo T, Aten RF, Leykin L, Behrman HR. Hydrogen peroxide evokes antisteroidogenic and antigonadotropic actions in human granulosa lutein cells. J Clin Endocrinol Metab 1993; 76: 337–42.

    Article  PubMed  CAS  Google Scholar 

  63. Kodaman PH, Aten RF, Behrman HR. Lipid hydroperoxides evoke antigonadotropic and antisteroidogenic activity in rat luteal cells. Endocrinology 1994; 135: 2723–30.

    Article  PubMed  CAS  Google Scholar 

  64. Wu XM, Sawada M, Carlson JC. Stimulation of phospholipase A2 by xanthine oxidase in the rat corpus luteum. Biol Reprod 1992; 47: 1053–8.

    Article  PubMed  CAS  Google Scholar 

  65. Wu X, Yao K, Carlson J. Plasma membrane changes in the rat corpus luteum induced by oxygen radical generation. Endocrinology 1993; 133: 491–5.

    Article  PubMed  CAS  Google Scholar 

  66. Musicki B, Behrman HR. Metal chelators reverse the action of hydrogen peroxide in rat luteal cells. Mol Cell Endocr 1993; 92: 215–20.

    Article  CAS  Google Scholar 

  67. Musicki B, Aten RF, Behrman HR. Inhibition of protein synthesis and hormone-sensitive steroidogenesis in response to hydrogen peroxide in rat luteal cells. Endocrinology 1994; 134: 588–95.

    Article  PubMed  CAS  Google Scholar 

  68. Soodak LK, Macdonald GJ, Behrman HR. Luteolysis is linked to LH-induced depletion of ATP in vivo. Endocrinology 1988; 122: 187–93.

    Article  PubMed  CAS  Google Scholar 

  69. Behrman HR, Aten RF. Evidence that hydrogen peroxide blocks hormone-sensitive cholestrol transport into mitochondria of rat luteal cells. Endocrinology 1991; 128: 2958–66.

    Article  PubMed  CAS  Google Scholar 

  70. Stocco DM, Wells 3, Clark BJ. The effects of hydrogen peroxide on steroidogenesis in mouse Leydig tumor cells. Endocrinology 1993; 133: 2827–32.

    Article  PubMed  CAS  Google Scholar 

  71. Hall PF. Trophic stimulation of steroidogenesis: in search of the elusive trigger. Rec Prog Horm Res 1985; 41: 1–39.

    PubMed  CAS  Google Scholar 

  72. Garren LD, Ney RL, Davis WW. Studies on the role of protein synthesis in the regulation of corticosterone production by adrenocorticotropic hormone in vivo. Proc Nat! Acad Sci USA 1965; 53: 1443–50.

    Article  CAS  Google Scholar 

  73. Toaff ME, Schleyer H, Strauss JF III. Metabolism of 25-hydroxycholesterol by rat luteal mitochondria and dispersed cells. Endocrinology 1982; 111: 1785–90.

    Article  PubMed  CAS  Google Scholar 

  74. Clark BJ, Wells J, King SR, Stocco DM. The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. J Biol Chem 1994; 269: 28314–22.

    PubMed  CAS  Google Scholar 

  75. King SR, Ronen-Fuhrmann T, Timberg R, Clark BJ, Orly J, Stocco DM. Steroid production after in vitro transcription, translation, and mitochondrial processing of protein products of complementary deoxyribonucleic acid for steroidogenic acute regulatory protein. Endocrinology 1995; 136: 5165–76.

    Article  PubMed  CAS  Google Scholar 

  76. Becker J, Mezger V, Courgeon A-M, Best-Belpomme М. Hydrogen peroxide activates immediate binding of a Drosophilafactor to DNA heat-shock regulatory element in vivo and in vitro. Eur J Biochem 1990; 189: 553–8.

    Article  PubMed  CAS  Google Scholar 

  77. Bruce JL, Price BD, Coleman CN, Calderwood SK. Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins. Cancer Res 1993; 53: 12–15.

    PubMed  CAS  Google Scholar 

  78. Donati YRA, Slosman DO, Polla BS. Oxidative injury and the heat shock response. Biochem Pharm 1990; 40: 2571–7.

    Article  PubMed  CAS  Google Scholar 

  79. Healy AM, Mariethoz E, Pizurki L, Polla BS. Heat shock proteins in cellular defense mechanisms and immunity. Ann NY Acad Sci 1992; 663: 319–30.

    Article  PubMed  CAS  Google Scholar 

  80. Heufelder AE, Wenzel BE, Bahn R. Methimazole and propylthiouracil inhibit the oxygen free radial-induced expression of a 72 kilodalton heat shock protein in Graves’ retroocular fibroblasts. J Clin Endocrinol Metab 1992; 74: 737–42.

    Article  PubMed  CAS  Google Scholar 

  81. Koizumi T, Negishi M, Ichikawa A. Activation of heat shock transcription factors by Л 12-prostaglandin J2 and its inhibition by intracellular glutathione. Biochem Pharmacol 1993; 45: 2457–64.

    Article  PubMed  CAS  Google Scholar 

  82. Santoro MG, Garaci E, Amici C. Prostaglandins with antiproliferative activity induce the synthesis of a heat shock protein in human cells. Proc Nat ’ Acad Sci USA 1989; 86: 8407–11.

    Article  CAS  Google Scholar 

  83. Nowak TS, Jr. Synthesis of heat shock/stress proteins during cellular injury. Ann NY Acad Sci 1993; 679: 142–56.

    Article  PubMed  CAS  Google Scholar 

  84. Welch WJ. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 1992; 72: 1063–81.

    PubMed  CAS  Google Scholar 

  85. Behrman HR, Riley JCM, Aten RF. Reactive oxygen species and ovarian function. In: Adashi E, Leung P, eds. The ovary. New York: Raven Press, 1993: 455–71.

    Google Scholar 

  86. Sender Baum M, Rosberg S. A phorbol ester, phorbol 12-myristate 13-acetate, and a calcium ionophore, А23187, can mimic the luteolytic effect of prostaglandin F2a in isolated rat luteal cells. Endocrinology 1987; 120: 1019–26.

    Article  Google Scholar 

  87. Musicki B, Aten RF, Behrman HR. The antigonadotropic actions of PGF2a and phorbol ester are mediated by separate processes in rat luteal cells. Endocrinology 1990; 126: 1388–95.

    Article  PubMed  CAS  Google Scholar 

  88. Dorflinger LJ, Albert PJ, Williams AT, Behrman HR. Calcium is an inhibitor of luteinizing hormone-sensitive adenylate cyclase in the luteal cell. Endocrinology 1984; 114: 1208–15.

    Article  PubMed  CAS  Google Scholar 

  89. Welch WJ, Kang HS, Beckmann RP, Mizzen LA. Response of mammalian cells to metabolic stress: changes in cell physiology and structure/function of stress proteins. Curr Top Microbiol Immunol 1991; 167: 31–55.

    Article  PubMed  CAS  Google Scholar 

  90. Craig EA. Chaperones: helpers along the pathways to protein folding. Science 1993; 260: 1902–4.

    Article  PubMed  CAS  Google Scholar 

  91. Norwich AL, Willison KR. Protein folding in the cell: functions of two families of molecular chaperone, hsp60, and TF55–TCP1. Phil Trans R Soc Lond B 1993; 339: 57–70.

    Google Scholar 

  92. McKay DB. Structure and mechanism of 70-kDa heat-shock-related proteins. Adv Protein Chem 1993; 44: 67–98.

    Article  PubMed  CAS  Google Scholar 

  93. Aquino DA, Brosnan CF. Heat-shock proteins and immunopathology. In: Brosnan CF, ed. Heat shock proteins and gamma-delta T cells. Vol. 53. Basel: Karger, 1992: 1–16.

    Chapter  Google Scholar 

  94. Hartl FU, Martin J. Protein folding in the cell: the role of molecular chaperones Hsp 70 and Hsp 60. Annu Rev Biophys Biomol Struct 1992; 21: 293–322.

    Article  PubMed  CAS  Google Scholar 

  95. Winfield JB, Jarjour WN. Stress proteins, autoimmunity, and autoimmune disease. Curr Top Microbiol Immunol 1991; 167: 161–89.

    Article  PubMed  CAS  Google Scholar 

  96. Ben-Ze’ev A, Amsterdam A. Regulation of heat shock protein synthesis by gonadotropins in cultured granulosa cells. Endocrinology 1989; 124: 2584–94.

    Article  PubMed  Google Scholar 

  97. Li X, Warren DW, Gregoire J, Pedersen RC, Lee AS. The rat 78000 dalton glucose regulated protein [GRP78] as a precursor for the rat steroidogenesis-activator polypeptide [SAP]: the sap coding sequence is homologous with the terminal end of GRP78. Mol Endocrinol 1989; 3: 1944–52.

    Article  PubMed  CAS  Google Scholar 

  98. Neupert W, Hart! F-U, Craig EA, Pfanner N. How do polypeptides cross the mitochondrial membranes? Cell 1990; 63: 447–50.

    Article  PubMed  CAS  Google Scholar 

  99. Tenniswood MP, Guenette RS, Lakins J, Mooibroek M, Wong P, Welsh J. Active cell death in hormone-dependent tissues. Cancer Metastasis Rev 1992; 11: 197–220.

    Article  PubMed  CAS  Google Scholar 

  100. Saw KD, Murphy SP, Morimoto RI. Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mot Cell Biol 1993; 13: 1392–407.

    Google Scholar 

  101. Morimoto RI, Sarge KD, Abravaya K. Transcriptional regulation of heat shock genes. J Biol Chem 1992; 267: 21987–90.

    PubMed  CAS  Google Scholar 

  102. Benjamin IJ, Kroger B, Williams RS. Activation of the heat shock transcription factor by hypoxia in mammalian cells. Proc Nat! Acad Sci USA 1990; 87: 6263–7.

    Article  CAS  Google Scholar 

  103. Shibahara S, Muller RM, Taguchi H. Transcriptional control of rat here oxygenase by heat shock. J Biol Chem 1987; 262: 12889–92.

    PubMed  CAS  Google Scholar 

  104. Colotta F, Polentarutti N, Staffico M, Fincato G, Mantovani A. Heat shock induces the transcriptional activation of c-fos protooncogene. Biochem Biophys Res Commun 1990; 168: 1013–9.

    Article  PubMed  CAS  Google Scholar 

  105. Khanna A, Aten RF, Behrman HR. Heat shock protein induction blocks hormone-sensitive steroidogenesis in rat luteal cells. Steroids 1994; 59: 4–9.

    Article  PubMed  CAS  Google Scholar 

  106. Thomas JP, Dorflinger LJ, Behrman HR. Mechanism of the rapid antigonadotropic action of prostaglandins in cultured luteual cells. Proc Nat! Acad Sci USA 1978; 75: 1344–8.

    Article  CAS  Google Scholar 

  107. Jordan AW. Effects of prostaglandin F2a treatment on LH and dibutyryl cyclic AMP-stimulated progesterone secretion by isolated rat luteal cells. Biol Reprod 1981; 25: 327–31.

    Article  PubMed  CAS  Google Scholar 

  108. Khanna A, Aten RF, Behrman HR. Physiological and pharmacological inhibitors of luteinizing hormone-dependent steroidogenesis induce heat shock protein-70 in rat luteal cells. Endocrinology 1995; 136: 1775–81.

    Article  PubMed  CAS  Google Scholar 

  109. McPherson LA, Van Kirk EA, Murdoch WJ. Localization of stress protein-70 in avine corpora lutea during prostaglandin-induced luteolysis. Prostaglandins 1993; 46: 433–40.

    Article  PubMed  CAS  Google Scholar 

  110. Khanna A, Aten RF, Behrman HR. Heat shock protein-70 induction mediates luteal regression in the rat. Mo! Endocrinol 1995; 9: 1431–40.

    CAS  Google Scholar 

  111. Wang F, Riley JCM, Behrman HR Immunosuppressive glucocorticoid blocks extrauterine luteolysins in the rat. Biol Reprod 1993; 49: 66–75.

    Article  PubMed  CAS  Google Scholar 

  112. Malven PV. Hypophysial regulation of luteolysis in the rat. In: McKerns KW, ed. The gonads. New York: Meredith Corporation, 1969: 367–82.

    Google Scholar 

  113. Long JA, Evans HM. The oestrous cycle in the rat. Memoirs Univ Calif 1922; 6: 1–148.

    Google Scholar 

  114. Smith PE. Hypophysectomy and a replacement therapy in the rat. Am J Anat 1930; 45: 205–73.

    Article  Google Scholar 

  115. Astwood EB, Greep RO. A corpus luteum-stimulating substance in the rat placenta. Proc Soc Exp Biol Med 1958; 38: 713–6.

    Google Scholar 

  116. Malven PV, Sawyer CH. A luteolytic action of prolactin in hypophysectomized rats. Endocrinology 1966; 79: 268–74.

    Article  PubMed  CAS  Google Scholar 

  117. Corner GW. The histological dating of the human corpus luteum of menstruation. Am J Anat 1956; 98: 377–401.

    Article  PubMed  Google Scholar 

  118. Kerr JFR, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26: 239–57.

    Article  PubMed  CAS  Google Scholar 

  119. Wyllie AH, Kerr JFR, Currie AR. Cell death: the significance of apoptosis. Int Rev Cytol 1980; 68: 251–306.

    Article  PubMed  CAS  Google Scholar 

  120. Azmi TI, O’Shea JD. Mechanism of deletion of endothelial cells during regression of the corpus luteum. Lab Invest 1984; 51: 206–17.

    PubMed  CAS  Google Scholar 

  121. Juengel JL, Garverick HA, Johnson AL, Youngquist RS, Smith MF. Apoptosis during luteal regression in cattle. Endocrinology 1993; 132: 249–54.

    Article  PubMed  CAS  Google Scholar 

  122. Endo T, Aten RF, Wang F, Behrman HR. Coordinate induction and activation of metalloproteinase and ascorbate depletion in structural luteolysis. Endocrinology 1993; 133: 690–8.

    Article  PubMed  CAS  Google Scholar 

  123. Fairchild DL, Pate JL. Modulation of bovine luteal cell synthetic capacity by interferon-gamma. Biol Reprod 1991; 44: 357–63.

    Article  PubMed  CAS  Google Scholar 

  124. Desclin L. Observations sur la structure des ovaires chez des rats soumis a l’influence de la prolactine Annal D’Endocrinol 1949; 10: 1–18.

    CAS  Google Scholar 

  125. Greenwald GS, Rothchild I. Formation and maintenance of corpora lutea in laboratory animals. JAnim Sci (Suppl 1) 1968; 27: 139–62.

    Google Scholar 

  126. Macdonald GJ, Greep RO. Prolactin-induced morphological luteal regression unaffected by LH. Proc Soc Exp Biol Med 1969; 131: 905–7.

    PubMed  CAS  Google Scholar 

  127. Grinwich DL, Hichens M, Behrman HR. Control of the LH receptor by prolactin and prostaglandin F2a in rat corpora lutea. Biol Reprod 1976; 14: 212–8.

    Article  PubMed  CAS  Google Scholar 

  128. Behrman HR, Grinwich DL, Hichens М, Macdonald GJ. Effect of hypophysectomy, prolactin, and prostaglandin F2a on gonadotropin binding in vivo and in vitro in the corpus luteum. Endocrinology 1978; 103: 349–57.

    Article  PubMed  CAS  Google Scholar 

  129. Sanchez-Criado JE, Ochiai K, Rothchild I. Indomethacin treatment prevents prolactin-induced luteolysis in the rat. J Endocrinol 1987; 112: 317–22.

    Article  PubMed  CAS  Google Scholar 

  130. Woessner JF, Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 1991; 5: 2145–54.

    PubMed  CAS  Google Scholar 

  131. Shimizu Y, Shaw S. Lymphocyte interactions with extracellular matrix. FASEB J 1991; 5: 2292–9.

    PubMed  CAS  Google Scholar 

  132. Springer TA. Adhesion receptors of the immune system. Nature 1990; 346: 425–34.

    Article  PubMed  CAS  Google Scholar 

  133. Tinker D, Rucker RB. Role of selected nutrients in synthesis, accumulation, and chemical modification of connective tissue proteins. Physiol Rev 1985; 65: 607–57.

    PubMed  CAS  Google Scholar 

  134. Kucharz E. The collagens: biochemistry and pathophysiology. New York: Springer-Verlag, 1992: 430.

    Book  Google Scholar 

  135. Geesin JC, Darr D, Kaufman R, Murad S, Pinnell SR. Ascorbic acid specifically increases type I and type III procollagen messenger RNA levels in human skin fibro-b asts. J Invest Dermatol 1988; 90: 420–4.

    Article  PubMed  CAS  Google Scholar 

  136. Aten RF, Kolodecik TR, Behrman HR. A cell adhesion receptor antiserum abolishes, wheras laminin and fibronectin glycoprotein components of extracellular matrix promote, luteinization of cultured rat granulosa cells. Endocrinology 1995;136:1753–8

    Google Scholar 

  137. Boudreau N, Syrrpson CJ, Werb Z, Bissell MJ. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 1995; 267: 891–3.

    Article  PubMed  CAS  Google Scholar 

  138. Franceschi RT. The role of ascorbic acid in mesenchymal differentiation. Nutrition Rev 1992; 50: 65–70.

    Article  CAS  Google Scholar 

  139. Padh H. Cellular functions of ascorbic acid. Biochem Cell Biol 1990; 68: 1166–73.

    Article  PubMed  CAS  Google Scholar 

  140. Cullen EI, May V, Eipper BA. Transport and stability of ascorbic acid in pituitary cultures. Mol Cell Endocrinol 1986; 48: 239–50.

    Article  PubMed  CAS  Google Scholar 

  141. Finn FM, Johns PA. Ascorbic acid transport by isolated bovine adrenal cortical cells. Endocrinology 1980; 106: 811–7.

    Article  PubMed  CAS  Google Scholar 

  142. Oikarinen A. Dermal connective tissue modulated by pharmacologic agents. Int J Derm 1992; 31: 149–56.

    Article  PubMed  CAS  Google Scholar 

  143. Nomura S, Hogan BLM, Wills AJ, Heath JK, Edwards DR. Developmental expression of tissue inhibitor of metalloproteinase (TIMP) RNA. Development 1989; 105: 575–83.

    PubMed  CAS  Google Scholar 

  144. Tanaka T, Andoh N, Takeya T. Sato E. Differential screening of ovarian cDNA libraries detected the expression of porcine collagenase inhibitor gene in functional corpora lutea. Mol Cell Endocrinol 1992; 83: 65–71.

    Article  PubMed  CAS  Google Scholar 

  145. Malven PV, Cousar GJ, Row EH. Structural luteolysis in hypophysectomized rats. Emer J Physiol 1969; 216: 421–4.

    CAS  Google Scholar 

  146. Mann JS, Kinkey MS, Edwards DR, Curry TЕ Jr. Hormonal regulation of matrix metalloproteinase inhibitors in rat granulosa cells and ovaries. Endocrinology 1991; 128: 1825–32.

    Article  PubMed  CAS  Google Scholar 

  147. Reich R, Daphna-Iden D, Chun SY, et al. Preovulatory changes in ovarian expression of collagenases and tissue metalloproteinase inhibitor messenger ribonucleic acid: role of eicosanoids. Endocrinology 1991; 129: 1869–75.

    Article  PubMed  CAS  Google Scholar 

  148. Gaddy-Kurten D, Hickey GJ, Fey GH, Gauldie J, Richards JS. Hormonal regulation and tissue-specific localization of a2-macroglobulin in rat ovarian follicles and corpora lutea. Endocrinology 1989; 125: 2985–95.

    Article  PubMed  CAS  Google Scholar 

  149. Caldwell BV, Behrman HR. Prostaglandins in reproductive processes. Med Clin N/A 1981; 65: 927–35.

    CAS  Google Scholar 

  150. Behrman HR, Caldwell BV. Role of prostaglandins in reproductive processes. In: Greep RP, ed. Reproductive physiology. Medical and Technical Publishing Co. Ltd, 1973.

    Google Scholar 

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Authors
  1. Harold R. Behrman
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  2. Raymond F. Aten
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  3. Pinar Kodaman
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  4. Tony G. Zreik
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  5. Paolo Rinaudo
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Editor information

Editors and Affiliations

  1. Vincent Center for Reproductive Biology, Massachusetts General Hospital, Boston, MA, 02114, USA

    Jonathan L. Tilly Ph.D.

  2. Center for Research on Reproduction and Women’s Health, University of Pennsylvania School of Medicine, Philadelphia, PA, 19104, USA

    Jerome F. Strauss III M.D., Ph.D.

  3. W. Alton Jones Cell Science Center, Lake Placid, NY, 12946, USA

    Martin Tenniswood Ph.D.

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© 1997 Springer Science+Business Media New York

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Behrman, H.R., Aten, R.F., Kodaman, P., Zreik, T.G., Rinaudo, P. (1997). Reactive Oxygen Species and Antioxidants in Luteal Cell Demise. In: Tilly, J.L., Strauss, J.F., Tenniswood, M. (eds) Cell Death in Reproductive Physiology. Proceedings in the Serono Symposia USA Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-1944-6_13

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  • DOI: https://doi.org/10.1007/978-1-4612-1944-6_13

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-7351-6

  • Online ISBN: 978-1-4612-1944-6

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