Table of Contents Author Guidelines Submit a Manuscript
PPAR Research
Volume 2008, Article ID 758562, 9 pages
http://dx.doi.org/10.1155/2008/758562
Review Article

Placental Implications of Peroxisome Proliferator-Activated Receptors in Gestation and Parturition

1Université d'Auvergne, JE 2447, ARDEMO, Clermont-Ferrand 63000, France
2INSERM, U.384, Laboratoire de Biochimie, Faculté de Médecine, Clermont-Ferrand 63000, France
3CHU Clermont-Ferrand, Maternité, Hôtel-Dieu, Clermont-Ferrand 63000, France

Received 4 June 2007; Revised 13 August 2007; Accepted 26 October 2007

Academic Editor: Pascal Froment

Copyright © 2008 Valerie Borel et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. W. T. Schaiff, Y. Barak, and Y. Sadovsky, “The pleiotropic function of PPAR γ in the placenta,” Molecular and Cellular Endocrinology, vol. 249, no. 1-2, pp. 10–15, 2006. View at Publisher · View at Google Scholar · View at PubMed
  2. P. Froment, F. Gizard, D. Defever, B. Staels, J. Dupont, and P. Monget, “Peroxisome proliferator-activated receptors in reproductive tissues: from gametogenesis to parturition,” Journal of Endocrinology, vol. 189, no. 2, pp. 199–209, 2006. View at Publisher · View at Google Scholar · View at PubMed
  3. T. Fournier, V. Tsatsaris, K. Handschuh, and D. Evain-Brion, “PPARs and the placenta,” Placenta, vol. 28, no. 2-3, pp. 65–76, 2007. View at Publisher · View at Google Scholar · View at PubMed
  4. I. Issemann and S. Green, “Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators,” Nature, vol. 347, no. 6294, pp. 645–650, 1990. View at Publisher · View at Google Scholar · View at PubMed
  5. L. Michalik, B. Desvergne, C. Dreyer, M. Gavillet, R. N. Laurini, and W. Wahli, “PPAR expression and function during vertebrate development,” International Journal of Developmental Biology, vol. 46, no. 1, pp. 105–114, 2002.
  6. L. Fajas, D. Auboeuf, and E. Raspe et al., “The organization, promoter analysis, and expression of the human PPARγ gene,” The Journal of Biological Chemistry, vol. 272, no. 30, pp. 18779–18789, 1997. View at Publisher · View at Google Scholar
  7. P. Escher and W. Wahli, “Peroxisome proliferator-activated receptors: insight into multiple cellular functions,” Mutation Research, vol. 448, no. 2, pp. 121–138, 2000. View at Publisher · View at Google Scholar
  8. B. Desvergne and W. Wahli, “Peroxisome proliferator-activated receptors: nuclear control of metabolism,” Endocrine Reviews, vol. 20, no. 5, pp. 649–688, 1999. View at Publisher · View at Google Scholar
  9. V. Y. Ng, Y. Huang, L. M. Reddy, J. R. Falck, E. T. Lin, and D. L. Kroetz, “Cytochrome P450 eicosanoids are activators of peroxisome proliferator-activated receptor α,” Drug Metabolism and Disposition, vol. 35, no. 7, pp. 1126–1134, 2007. View at Publisher · View at Google Scholar · View at PubMed
  10. P. Escher, O. Braissant, S. Basu-Modak, L. Michalik, W. Wahli, and B. Desvergne, “Rat PPARs: quantitative analysis in adult rat tissues and regulation in fasting and refeeding,” Endocrinology, vol. 142, no. 10, pp. 4195–4202, 2001. View at Publisher · View at Google Scholar
  11. Q. Wang, H. Fujii, and G. T. Knipp, “Expression of PPAR and RXR isoforms in the developing rat and human term placentas,” Placenta, vol. 23, no. 8-9, pp. 661–671, 2002. View at Publisher · View at Google Scholar
  12. E. B. E. Berry, R. Eykholt, R. J. A. Helliwell, R. S. Gilmour, M. D. Mitchell, and K. W. Marvin, “Peroxisome proliferator-activated receptor isoform expression changes in human gestational tissues with labor at term,” Molecular Pharmacology, vol. 64, no. 6, pp. 1586–1590, 2003. View at Publisher · View at Google Scholar · View at PubMed
  13. B. E. Schwarz, F. M. Schultz, P. C. Macdonald, and J. M. Johnston, “Initiation of human parturition. III. fetal membrane content of prostaglandin E2 and F2α precursor,” Obstetrics and Gynecology, vol. 46, no. 5, pp. 564–568, 1975.
  14. J. R. Okita, P. C. MacDonald, and J. M. Johnston, “Mobilization of arachidonic acid from specific glycerophospholipids of human fetal membranes during early labor,” Journal of Biological Chemistry, vol. 257, no. 23, pp. 14029–14034, 1982.
  15. M. D. Mitchell, D. L. Kraemer, and D. M. Strickland, “The human placenta: a major source of prostaglandin D2,” Prostaglandins Leukotrienes and Medicine, vol. 8, no. 4, pp. 383–387, 1982. View at Publisher · View at Google Scholar
  16. R. J. Helliwell, J. A. Keelan, and K. W. Marvin et al., “Gestational age-dependent up-regulation of prostaglandin D synthase (PGDS) and production of PGDS-derived antiinflammatory prostaglandins in human placenta,” Journal of Clinical Endocrinology & Metabolism, vol. 91, no. 2, pp. 597–606, 2006. View at Publisher · View at Google Scholar · View at PubMed
  17. L. L. Waite, E. C. Person, Y. Zhou, K. H. Lim, T. S. Scanlan, and R. N. Taylor, “Placental peroxisome proliferator-activated receptor-γ is up-regulated by pregnancy serum,” Journal of Clinical Endocrinology & Metabolism, vol. 85, no. 10, pp. 3808–3814, 2000. View at Publisher · View at Google Scholar
  18. H. Li, X. Z. Ruan, and S. H. Powis et al., “EPA and DHA reduce LPS-induced inflammation responses in HK-2 cells: evidence for a PPAR-γ-dependent mechanism,” Kidney International, vol. 67, no. 3, pp. 867–874, 2005. View at Publisher · View at Google Scholar · View at PubMed
  19. A. De Paulis, A. Ciccarelli, I. Marinò, G. De Crescenzo, D. Marinò, and G. Marone, “Human synovial mast cells: II. heterogeneity of the pharmacologic effects of antiinflammatory and immunosuppressive drugs,” Arthritis and Rheumatism, vol. 40, no. 3, pp. 469–478, 1997. View at Publisher · View at Google Scholar
  20. H. Fahmi, J. A. Di Battista, J. P. Pelletier, F. Mineau, P. Ranger, and J. Martel-Pelletier, “Peroxisome proliferator-activated receptor γ activators inhibit interleukin-1β-induced nitric oxide and matrix metalloproteinase 13 production in human chondrocytes,” Arthritis & Rheumatism, vol. 44, no. 3, pp. 595–607, 2001. View at Publisher · View at Google Scholar
  21. Y. Barak, M. C. Nelson, and E. S. Ong et al., “PPAR γ is required for placental, cardiac, and adipose tissue development,” Molecular Cell, vol. 4, no. 4, pp. 585–595, 1999. View at Publisher · View at Google Scholar
  22. V. Sapin, L. Blanchon, A. F. Serre, D. Lemery, B. Dastugue, and S. J. Ward, “Use of transgenic mice model for understanding the placentation: towards clinical applications in human obstetrical pathologies?,” Transgenic Research, vol. 10, no. 5, pp. 377–398, 2001. View at Publisher · View at Google Scholar
  23. P. Antonson, G. U. Schuster, and L. Wang et al., “Inactivation of the nuclear receptor coactivator RAP250 in mice results in placental vascular dysfunction,” Molecular and Cellular Biology, vol. 23, no. 4, pp. 1260–1268, 2003. View at Publisher · View at Google Scholar
  24. Y. Zhu, C. Qi, Y. Jia, J. S. Nye, M. S. Rao, and J. K. Reddy, “Deletion of PBP/PARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality,” Journal of Biological Chemistry, vol. 275, no. 20, pp. 14779–14782, 2000. View at Publisher · View at Google Scholar · View at PubMed
  25. Y.-J. Zhu, S. E. Crawford, and V. Stellmach et al., “Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development,” Journal of Biological Chemistry, vol. 278, no. 3, pp. 1986–1990, 2003. View at Publisher · View at Google Scholar · View at PubMed
  26. Y. Barak, D. Liao, and W. He et al., “Effects of peroxisome proliferator-activated receptor δ on placentation, adiposity, and colorectal cancer,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 1, pp. 303–308, 2002. View at Publisher · View at Google Scholar · View at PubMed
  27. W. T. Schaiff, F. F. Knapp Jr., Y. Barak, T. Biron-Shental, D. M. Nelson, and Y. Sadovsky, “Ligand-activated PPARγ alters placental morphology and placental fatty acid uptake in mice,” Endocrinology, vol. 148, no. 8, pp. 3625–3634, 2007. View at Publisher · View at Google Scholar
  28. W. T. Schaiff, I. Bildirici, M. Cheong, P. L. Chern, D. M. Nelson, and Y. Sadovsky, “Peroxisome proliferator-activated receptor-γ and retinoid X receptor signaling regulate fatty acid uptake by primary human placental trophoblasts,” Journal of Clinical Endocrinology and Metabolism, vol. 90, no. 7, pp. 4267–4275, 2005. View at Publisher · View at Google Scholar · View at PubMed
  29. I. Bildirici, C.-R. Roh, W. T. Schaiff, B. M. Lewkowski, D. M. Nelson, and Y. Sadovsky, “The lipid droplet-associated protein adipophilin is expressed in human trophoblasts and is regulated by peroxisomal proliferator-activated receptor-γ/Retinoid X Receptor,” Journal of Clinical Endocrinology and Metabolism, vol. 88, no. 12, pp. 6056–6062, 2003. View at Publisher · View at Google Scholar
  30. A. K. Duttaroy, “Fetal growth and development: roles of fatty acid transport proteins and nuclear transcription factors in human placenta,” Indian Journal of Experimental Biology, vol. 42, no. 8, pp. 747–757, 2004.
  31. M. Lappas, K. Yee, M. Permezel, and G. E. Rice, “Lipopolysaccharide and TNF-α activate the nuclear factor kappa B pathway in the human placental JEG-3 cells,” Placenta, vol. 27, no. 6-7, pp. 568–575, 2006. View at Publisher · View at Google Scholar · View at PubMed
  32. D. A. Kniss, “Cyclooxygenases in reproductive medicine and biology,” Journal of the Society for Gynecologic Investigation, vol. 6, no. 6, pp. 285–292, 1999. View at Publisher · View at Google Scholar
  33. M. Lappas, M. Permezel, H. M. Georgiou, and G. E. Rice, “Regulation of proinflammatory cytokines in human gestational tissues by peroxisome proliferator-activated receptor-γ: effect of 15-deoxy-Δ12,14-PGJ2 and troglitazone,” Journal of Clinical Endocrinology & Metabolism, vol. 87, no. 10, pp. 4667–4672, 2002. View at Publisher · View at Google Scholar
  34. W. E. Ackerman, X. L. Zhang, B. H. Rovin, and D. A. Kniss, “Modulation of cytokine-induced cyclooxygenase 2 expression by PPARG ligands through NFκB signal disruption in human WISH and amnion cells,” Biology of reproduction, vol. 73, no. 3, pp. 527–535, 2005. View at Publisher · View at Google Scholar · View at PubMed
  35. E. B. Berry, J. A. Keelan, R. J. Helliwell, R. S. Gilmour, and M. D. Mitchell, “Nanomolar and micromolar effects of 15-deoxy- Δ12,14-prostaglandin J2 on amnion-derived wish epithelial cells: differential roles of peroxisome proliferator-activated receptors γ and δ and nuclear factor κB,” Molecular Pharmacology, vol. 68, no. 1, pp. 169–178, 2005. View at Publisher · View at Google Scholar · View at PubMed
  36. M. Lappas and G. E. Rice, “Phospholipase A2 isozymes in pregnancy and parturition,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 70, no. 2, pp. 87–100, 2004. View at Publisher · View at Google Scholar
  37. M. Lappas, M. Permezel, and G. E. Rice, “Leptin and adiponectin stimulate the release of proinflammatory cytokines and prostaglandins from human placenta and maternal adipose tissue via nuclear factor-κB, peroxisomal proliferator-activated receptor-γ and extracellularly regulated kinase 1/2,” Endocrinology, vol. 146, no. 8, pp. 3334–3342, 2005. View at Publisher · View at Google Scholar · View at PubMed
  38. L. R. Dunn-Albanese, W. E. Ackerman, Y. Xie, J. D. Iams, and D. A. Kniss, “Reciprocal expression of peroxisome proliferator-activated receptor-γ and cyclooxygenase-2 in human term parturition,” American Journal of Obstetrics and Gynecology, vol. 190, no. 3, pp. 809–816, 2004. View at Publisher · View at Google Scholar · View at PubMed
  39. T. M. Lindstrom and P. R. Bennett, “15-Deoxy-Δ12,14-prostaglandin J2 inhibits interleukin-1β-induced nuclear factor-κb in human amnion and myometrial cells: mechanisms and implications,” Journal of Clinical Endocrinology & Metabolism, vol. 90, no. 6, pp. 3534–3543, 2005. View at Publisher · View at Google Scholar · View at PubMed
  40. L. Capparuccia, D. Marzioni, and A. Giordano et al., “PPARγ expression in normal human placenta, hydatidiform mole and choriocarcinoma,” Molecular Human Reproduction, vol. 8, no. 6, pp. 574–579, 2002. View at Publisher · View at Google Scholar
  41. J. M. Roberts, R. N. Taylor, T. J. Musci, G. M. Rodgers, C. A. Hubel, and M. K. McLaughlin, “Preeclampsia: an endothelial cell disorder,” American Journal of Obstetrics and Gynecology, vol. 161, no. 5, pp. 1200–1204, 1989.
  42. D. Ware Branch, M. D. Mitchell, E. Miller, W. Palinski, and J. L. Witztum, “Pre-eclampsia and serum antibodies to oxidised low-density lipoprotein,” Lancet, vol. 343, no. 8898, pp. 645–646, 1994. View at Publisher · View at Google Scholar
  43. R. D. Johnson, K. L. Polakoski, X. Huang, Y. Sadovsky, and D. M. Nelson, “The release of 15-hydroxyeicosatetraenoic acid by human placental trophoblast is increased in preeclampsia,” American Journal of Obstetrics and Gynecology, vol. 178, no. 1 part 1, pp. 54–58, 1998. View at Publisher · View at Google Scholar
  44. R. L. Schild, W. T. Schaiff, M. G. Carlson, E. J. Cronbach, D. M. Nelson, and Y. Sadovsky, “The activity of PPAR γ in primary human trophoblasts is enhanced by oxidized lipids,” Journal of Clinical Endocrinology and Metabolism, vol. 87, no. 3, pp. 1105–1110, 2002. View at Publisher · View at Google Scholar
  45. T. Fournier, L. Pavan, and A. Tarrade et al., “The role of PPAR-γ/RXR-α heterodimers in the regulation of human trophoblast invasion,” Annals of the New York Academy of Sciences, vol. 973, pp. 26–30, 2002.
  46. J. A. Keelan, T. A. Sato, K. W. Marvin, J. Lander, R. S. Gilmour, and M. D. Mitchell, “15-Deoxy-Δ12,14-prostaglandin J2, a ligand for peroxisome proliferator-activated receptor-γ, induces apoptosis in JEG3 choriocarcinoma cells,” Biochemical and Biophysical Research Communications, vol. 262, no. 3, pp. 579–585, 1999. View at Publisher · View at Google Scholar · View at PubMed
  47. J. Keelan, R. Helliwell, and B. Nijmeijer et al., “15-Δ12,14-prostaglandin J2-induced apoptosis in amnion-like WISH cells,” Prostaglandins and Other Lipid Mediators, vol. 66, no. 4, pp. 265–282, 2001. View at Publisher · View at Google Scholar
  48. S.-Q. Kuang, L. Liao, and H. Zhang et al., “Deletion of the cancer-amplified coactivator AIB3 results in defective placentation and embryonic lethality,” Journal of Biological Chemistry, vol. 277, no. 47, pp. 45356–45360, 2002. View at Publisher · View at Google Scholar · View at PubMed
  49. K. Nadra, S. I. Anghel, and E. Joye et al., “Differentiation of trophoblast giant cells and their metabolic functions are dependent on peroxisome proliferator-activated receptor β/δ,” Molecular and Cellular Biology, vol. 26, no. 8, pp. 3266–3281, 2006. View at Publisher · View at Google Scholar · View at PubMed
  50. L. Julan, H. Guan, J. P. Van Beek, and K. Yang, “Peroxisome proliferator-activated receptor δ suppresses 11β-hydroxysteroid dehydrogenase type 2 gene expression in human placental trophoblast cells,” Endocrinology, vol. 146, no. 3, pp. 1482–1490, 2005. View at Publisher · View at Google Scholar · View at PubMed
  51. Y. Xu, T. J. Cook, and G. T. Knipp, “Effects of di-(2-ethylhexyl)-phthalate (DEHP) and its metabolites on fatty acid homeostasis regulating proteins in rat placental HRP-1 trophoblast cells,” Toxicological Sciences , vol. 84, no. 2, pp. 287–300, 2005. View at Publisher · View at Google Scholar · View at PubMed
  52. E. Capobianco, A. Jawerbaum, V. White, C. Pustovrh, D. Sinner, and E. T. Gonzalez, “Elevated levels of endothelin-1 and prostaglandin E2 and their effect on nitric oxide generation in placental tissue from neonatal streptozotocin-induced diabetic rats,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 68, no. 3, pp. 225–231, 2003. View at Publisher · View at Google Scholar
  53. A. Jawerbaum, E. Capobianco, and C. Pustovrh et al., “Influence of peroxisome proliferator-activated receptor γ activation by its endogenous ligand 15-deoxy Δ12,14 prostaglandin J2 on nitric oxide production in term placental tissues from diabetic women,” Molecular Human Reproduction, vol. 10, no. 9, pp. 671–676, 2004. View at Publisher · View at Google Scholar · View at PubMed
  54. A. Jawerbaum and E. González, “Diabetic pregnancies: the challenge of developing in a pro-inflammatory environment,” Current Medicinal Chemistry, vol. 13, no. 18, pp. 2127–2138, 2006. View at Publisher · View at Google Scholar
  55. M. J. Willi, M. Winkler, D.-C. Fischer, T. Reineke, H. Maul, and W. Rath, “Chorioamnionitis: elevated interleukin-6 and interleukin-8 concentrations in the lower uterine segment,” Journal of Perinatal Medicine, vol. 30, no. 4, pp. 292–296, 2002. View at Publisher · View at Google Scholar · View at PubMed
  56. V. Zaga, G. Estrada-Gutierrez, J. Beltran-Montoya, R. Maida-Claros, R. Lopez-Vancell, and F. Vadillo-Ortega, “Secretions of interleukin-1β and tumor necrosis factor α by whole fetal membranes depend on initial interactions of amnion or choriodecidua with lipopolysaccharides or group B streptococci,” Biology of Reproduction, vol. 71, no. 4, pp. 1296–1302, 2004. View at Publisher · View at Google Scholar · View at PubMed
  57. B. Jacobsson, I. Mattsby-Baltzer, and H. Hagberg, “Interleukin-6 and interleukin-8 in cervical and amniotic fluid: relationship to microbial invasion of the chorioamniotic membranes,” Journal of Obstetrics and Gynaecology, vol. 112, no. 6, pp. 719–724, 2005. View at Publisher · View at Google Scholar · View at PubMed
  58. V. Zaga-Clavellina, G. G. Lopez, and G. Estrada-Gutierrez et al., “Incubation of human chorioamniotic membranes with Candida albicans induces differential synthesis and secretion of interleukin-1β, interleukin-6, prostaglandin E2, and 92 kDa type IV collagenase,” Mycoses, vol. 49, no. 1, pp. 6–13, 2006. View at Publisher · View at Google Scholar · View at PubMed
  59. B. Toth, D. Hornung, C. Scholz, S. Djalali, K. Friese, and U. Jeschke, “Peroxisome proliferator-activated receptors: new players in the field of reproduction,” American Journal of Reproductive Immunology, vol. 58, no. 3, pp. 289–310, 2007. View at Publisher · View at Google Scholar · View at PubMed