15-Deoxy-Δ12,14-prostaglandin J2: An electrophilic trigger of cellular responses

Chemical Research in Toxicology

Volumn 21, Issue 1, 2008, Pages 138-144

  Uchida, Koji ^a   Shibata, Takahiro ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

15 DEOXY DELTA12,14 PROSTAGLANDIN J2; CYCLOPENTENONE; CYSTEINE; CYTOSKELETON PROTEIN; GLUTATHIONE; PROSTAGLANDIN D2; PROSTAGLANDIN SYNTHASE; SELENIUM; THIOL DERIVATIVE;

ANTIOXIDANT ACTIVITY; APOPTOSIS; CELL ACTIVITY; CELL DIFFERENTIATION; CELL FUNCTION; CELL GROWTH; COVALENT BOND; HUMAN; INFLAMMATION; MICHAEL ADDITION; NERVE CELL DIFFERENTIATION; NONHUMAN; OXIDATION REDUCTION REACTION; PATHOPHYSIOLOGY; PROTEIN METABOLISM; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; ANTIOXIDANTS; APOPTOSIS; CELL DIFFERENTIATION; CYTOSKELETON; HUMANS; IMMUNOLOGIC FACTORS; INFLAMMATION; NEURONS; OXIDATION-REDUCTION; PROSTAGLANDIN D2;

EID: 38949126129     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx700177j     Document Type: Review

References (77)

1. Smith, W. L. (1989) The eicosanoids and their biochemical mechanisms of action. Biochem. J. 259, 315-324.
2. Smith, W. L. (1992) Prostanoid biosynthesis and mechanisms of action. Am. J. Physiol. 263, F181-F191.
3. 2. Prostaglandins 35, 277-300.
4. Urade, Y., and Eguchi, N. (2002) Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediators 68-69, 375-382.
5. 2: anti-tumour and anti-viral activities and the mechanisms involved. Eicosanoids 3, 189-199.
6. Herschman, H. R., Reddy, S. T., and Xie, W. (1997) Function and regulation of prostaglandin synthase-2. Adv. Exp. Med. Biol. 407, 61-66.
7. 2 levels as a predictor of periodontal attachment loss. J. Periodontal Res. 21, 101-112.
8. 2. Prostaglandins 35, 277-300.
9. 2 11-ketoreductase, contribution of prostaglandin F synthetase and its cellular localization. J. Biol. Chem. 265, 12029-12035.
10. 2. Identification of products formed in vitro. J. Biol. Chem. 258, 11713-11718.
11. 2 formed in human plasma. Proc. Natl. Acad. U.S.A. 81, 1317-1321.
12. 2 and related compounds: an update. Prostaglandins Leukotrienes Essent. Fatty Acids 47, 1-12.
13. 2 is a ligand for the adipocyte determination factor PPARγ. Cell 83, 803-812.
14. 2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation. Cell 83, 813-819.
15. Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., and Santoro, M. G. (2000) Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403, 103-108.
16. Bui, T., and Straus, D. S. (1998) Effects of cyclopentenone prostaglandins and related compounds on insulin-like growth factor-I and Waf1 gene expression. Biochim. Biophys. Acta 1397, 31-42.
17. 2 metabolite generated during inflammatory processes. J. Biol. Chem. 277, 10459-10466.
18. 2 in human urine. J. Biol. Chem. 263, 16619-16625.
19. Gilroy, D. W., Colville-Nash, P. R., Willis, D., Chivers, J., Paul-Clark, M. J., and Willoughby, D. A. (1999) Inducible cyclooxygenase may have anti-inflammatory properties. Nat. Med. 5, 698-701.
20. 2: the endogenous electrophile that induces neuronal apoptosis. Proc. Natl. Acad. Sci. U.S.A. 99, 7367-7372.
21. 2. Mol. Cell. Biol. 24, 36-45.
22. 2 and Nrf2 pathways in protection against acute lung injury. Am. J. Respir. Crit. Care Med. 171, 1260-1266.
23. Coste, A., Dubourdeau, M., Linas, M. D., Cassaing, S., Lepert, J. C., Balard, P., Chalmeton, S., Bernad, J., Orfila, C., Seguela, J. P., and Pipy, B. (2003) PPARγ promotes mannose receptor gene expression in murine macrophages and contributes to the induction of this receptor by IL-13. Immunity 19, 329-339.
24. 2 and the ligation of PPARγ. J. Clin. Invest. 112, 945-955.
25. 1 methyl esters with thiols. J. Am. Chem. Soc. 119, 2376-2385.
26. 2 addition in mesangial cells: role in the inhibition of pro-inflammatory genes. Mol. Pharmacol. 66, 1349-1358.
27. 2 inhibits transcriptional activity of estrogen receptor-alpha via covalent modification of DNA-binding domain. Cancer Res. 67, 2595-602.
28. Shibata, T., Yamada, T., Ishii, T., Kumazawa, S., Nakamura, H., Masutani, H., Yodoi, J., and Uchida, K. (2003) Thioredoxin as a molecular target of cyclopentenone prostaglandins. J. Biol. Chem. 278, 26046-26054.
29. Shiraki, T., Kamiya, N., Shiki, S., Kodama, T. S., Kakizuka, A., and Jingami, H. (2005) α,β-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor γ. J. Biol. Chem. 280, 14145-14153.
30. 2 to the PPARγ ligand-binding domain by multi-wavelength global fitting. Biochem. J. 393, 749-55.
31. 2 binds to and activates H-Ras. Proc. Natl. Acad. Sci. U.S.A. 100, 4112-4111.
32. Prestera, T., Zhang, Y., Spencer, S. R., Wilczak, C. A., and Talalay, P. (1993) The electrophile counterattack response: protection against neoplasia and toxicity. Adv. Enzyme Regul. 33, 281-296.
33. Rushmore, T. H., King, R. G., Paulson, K. E., and Pickett, C. B. (1990) Regulation of glutathione S-transferase Ya subunit gene expression: identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Proc. Natl. Acad. Sci. U.S.A. 87, 3826-3830.
34. Dinkova-Kostova, A. T., Holtzclaw, W. D., and Kensler, T. W. (2005) The role of Keap1 in cellular protective responses. Chem. Res. Toxicol. 18, 1779-1791.
35. 2-induced expression of glutathione S-transferases. J. Biol. Chem. 275, 11291-11299.
36. Levonen, A. L., Landar, A., Ramachandran, A., Ceaser, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., and Darley-Usmar, V. M. (2004) Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 378, 373-382.
37. Hosoya, T., Maruyama, A., Kang, M.-I., Kawatani, Y., Shibata, T., Uchida, K., Warabi, E., Noguchi, N., Itoh, K., and Yamamoto, M. (2005) Differential responses of the Nrf2-Keap1 system to laminar and oscillatory shear stresses in endothelial cells. J. Biol. Chem. 280, 27244-27250.
38. Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M. I., Kobayashi, A., Yamamoto, M., Kensler, T. W., and Talalay, P. (2004) Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers. Proc. Natl. Acad. Sci.U.S.A. 101, 2040-2045.
39. Gao, L., Wang, J., Sekhar, K. R., Yin, H., Yared, N. F., Schneider, S. N., Sasi, S., Dalton, T. P., Anderson, M. E., Chan, J. Y., Morrow, J. D., and Freeman, M.L. (2007) Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3. J. Biol. Chem. 282, 2529-37.
40. Kobayashi, A., Kang, M. I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., and Yamamoto, M. (2006) Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol. Cell. Biol. 26, 221-9.
41. Zhang, D. D., and Hannink, M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23, 8137-8151.
42. Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., and Mesecar, A. D. (2005) Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2. Proc. Natl. Acad. Sci. U.S.A. 102, 10070-10075.
43. 2 attenuates the development of acute and chronic inflammation. Mol. Pharmacol. 61, 997-1007.
44. 2 inhibits multiple steps in the NF-κB signaling pathway. Proc. Natl. Acad. Sci. U.S.A. 97, 4844-4849.
45. 2 inhibition of NF-κB-DNA binding through covalent modification of the p50 subunit. J. Biol. Chem. 276, 35530-35536.
46. 2 in macrophages. J. Biol.Chem., 282, 17964-17973.
47. Kostadinova, R., Washi, W., and Michalik, L. (2005) PPARs in diseases: control mechanisms of inflammation. Curr. Med. Chem. 12, 2995-3009.
48. Yang, X. Y., Wang, L. H., Chen, T., Hodge, D. R., Resau, J. H., DaSilva, L., and Farrar, W. L. (2000) Activation of human T lymphocytes is inhibited by peroxisome proliferator-activated receptor γ (PPARγ) agonists: PPARγ co-association with transcription factor NFAT. J. Biol. Chem. 275, 4541-4544.
49. Li, M., Pascual, G., and Glass, C. K. (2000) Peroxisome proliferator-activated receptor γ-dependent repression of the inducible nitric oxide synthase gene. Mol. Cell. Biol. 20, 4699-4707.
50. Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J., and Glass, C. K. (1998) The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation. Nature 391, 79-82.
51. Jiang, C., Ting, A. T., and Seed, B. (1998) PPAR-γ agonists inhibit production of monocyte inflammatory cytokines. Nature 391, 82-86.
52. Kondo, M., Oya-Ito, T., Kumagai, T., Osawa, T., and Uchida, K. (2001) Cyclopentenone prostaglandins as potential inducers of intracellular oxidative stress. J. Biol. Chem. 276, 12076-12083.
53. Ishii, T., Sakurai, T., Usami, H., and Uchida, K. (2005) Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry 44, 13893-13901.
54. 2. Chem. Res. Toxicol. 17, 1313-1322.
55. Moos, P. J., Edes, K., Cassidy, P., Massuda, E., and Fitzpatrick, F. A. (2003) Electrophilic prostaglandins and lipid aldehydes repress redox-sensitive transcription factors p53 and hypoxia-inducible factor by impairing the selenoprotein thioredoxin reductase. J. Biol. Chem. 278, 745-750.
56. 2 on proteasome. Biochemistry 42, 13960-13968.
57. Mullally, J. E., Moos, P. J., Edes, K., and Fitzpatrick, F. A. (2001) Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway. J. Biol. Chem. 276, 30366-30373.
58. 2 alters pro-survival and pro-death gene expression patterns and 26 S proteasome assembly in human neuroblastoma cells. J. Biol. Chem. 281, 21377-21386.
59. Ciechanover, A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21.
60. Jentsch, S., and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell 82, 881-884.
61. Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
62. Hortelano, S., Castrillo, A., Alvarez, A. M., and Bosca, L. (2000) Contribution of cyclopentenone prostaglandins to the resolution of inflammation through the potentiation of apoptosis in activated macrophages. J. Immunol. 165, 6525-6531.
63. 2 production in murine macrophages. Synergistic action of cyclic AMP on cyclooxygenase-2 expression and prostaglandin E2 synthesis. J. Biol. Chem. 272, 31065-31072.
64. Kobayashi, M., Ono, H., Mihara, K., Tauchi, H., Komatsu, K., Shibata, T., Shimizu, H., Uchida, K., and Yamamoto, K. (2006) ATM activation by a sulfhydryl-reactive inflammatory cyclopentenone prostaglandin. Genes Cells 11, 779-789.
65. Moos, P. J., Edes, K., and Fitzpatrick, F. A. (2000) Inactivation of wild-type p53 tumor suppressor by electrophilic prostaglandins. Proc. Natl. Acad. Sci. U.S.A. 97, 9215-9220.
66. Mullally, J. E., and Fitzpatrick, F. A. (2002) Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death. Mol. Pharmacol. 62, 351-358.
67. 2-M phase progression in human breast cancer cells via the down-regulation of cyclin B1 and survivin expression. Breast Cancer Res. Treat. 102, 263-273.
68. 2 induces death receptor 5 expression through mRNA stabilization independently of PPARγ and potentiates TRAIL-induced apoptosis. Mol. Cancer Ther. 5, 1827-1835.
69. 2. J. Biol. Chem. 278, 51251-51260.
70. 2 in mesangial cells reveals multiple interactions with the cytoskeleton. J. Am. Soc. Nephrol. 17, 89-98.
71. 2 in mitochondria. Biochem. J. 394, 185-195.
72. Gayarre, J., Sanchez, D., Sanchez-Gomez, F. J., Terron, M. C., Llorca, O., and Perez-Sala, D. (2006) Addition of electrophilic lipids to actin alters filament structure. Biochem. Biophys. Res. Commun. 349, 1387-1393.
73. 2 target in neuroblastoma cells: Mass spectrometric, computational and functional approaches to investigate the effect of cytoskeletal deagangement. Biochemistry 46, 2707-2718.
74. 2 in mesangial cells reveals multiple interactions with the cytoskeleton. J. Am. Soc. Nephrol. 17, 89-98.
75. 2 and its metabolites promote neurite outgrowth induced by nerve growth factor in PC12 cells. Biochem. Biophys. Res. Commun. 258, 50-53.
76. Satoh, T., Furuta, K., Tomokiyo, K., Nakatsuka, D., Tanikawa, M., Nakanishi, M., Miura, M., Tanaka, S., Koike, T., Hatanaka, H., Ikuta, K., Suzuki, M., and Watanabe, Y. (2000) Facilitatory roles of novel compounds designed from cyclopentenone prostaglandins on neurite outgrowth-promoting activities of nerve growth factor. J. Neurochem. 75, 1092-1102.
77. 2 derivatives. Chem. Asian J. 1, 669-677.