Prostaglandin D2 induces heme oxygenase-1 mRNA expression through the DP2 receptor

Biochemical and Biophysical Research Communications

Volumn 377, Issue 3, 2008, Pages 878-883

  Satarug, Soisungwan ^a,b,c   Wisedpanichkij, Raewadee ^a,b   Takeda, Kazuhisa ^a   Li, Bin ^a   Na Bangchang, Kesara ^b   Moore, Michael R ^c   Shibahara, Shigeki ^a  

^a TOHOKU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b THAMMASAT UNIVERSITY   (Thailand)

^c UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Cadmium; DP2 receptor; Heme oxygenase; Macular degeneration; Malaria; Prostaglandin D2; Retina; Stress

Indexed keywords

15 METHYLPROSTAGLANDIN D2; 3 BENZYL 5 (6 CARBOXYHEXYL) 1 (2 CYCLOHEXYL 2 HYDROXYETHYLAMINO)HYDANTOIN; 5 (6 CARBOXYHEXYL) 1 (3 CYCLOHEXYL 3 HYDROXYPROPYL)HYDANTOIN; HEME; HEME OXYGENASE 1; HEME OXYGENASE 2; MESSENGER RNA; PROSTAGLANDIN D2; PROSTAGLANDIN D2 DERIVATIVE; PROSTAGLANDIN DP2 RECEPTOR; PROSTAGLANDIN RECEPTOR; UNCLASSIFIED DRUG; CADMIUM; CARBAZOLE DERIVATIVE; CAY 10471; IMMUNOGLOBULIN RECEPTOR; PROSTAGLANDIN D2 RECEPTOR; SULFONAMIDE;

ARTICLE; CONCENTRATION RESPONSE; ENZYME INDUCTION; GENE ACTIVITY; HUMAN; HUMAN CELL; PHOTORECEPTOR; PRIORITY JOURNAL; PROMOTER REGION; RETINA MACULA DEGENERATION; BIOSYNTHESIS; CELL LINE; DRUG ANTAGONISM; DRUG EFFECT; DRUG POTENTIATION; ENZYMOLOGY; HOMEOSTASIS; METABOLISM; PHYSIOLOGY; PIGMENT EPITHELIUM;

CADMIUM; CARBAZOLES; CELL LINE; HEME; HEME OXYGENASE-1; HOMEOSTASIS; HUMANS; PROMOTER REGIONS, GENETIC; PROSTAGLANDIN D2; RECEPTORS, IMMUNOLOGIC; RECEPTORS, PROSTAGLANDIN; RETINAL PIGMENT EPITHELIUM; RNA, MESSENGER; SULFONAMIDES;

EID: 56049119088     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.094     Document Type: Article

References (32)

1. Boie Y., Sawyer N., Slipetz D.M., Metters K.M., and Abramovitz M. Molecular cloning and characterization of the human prostanoid DP receptor. J. Biol. Chem. 270 (1995) 18910-18916
2. 2 selectively induces chemotaxis in T helper type 2 cells, eosinophils, and basophils via seven-transmembrane receptor CRTH2. J. Exp. Med. 193 (2001) 255-261
3. 2 receptors DP1 and CRTH2 as an approach to treat allergic diseases. Nat. Rev. Drug Discov. 6 (2007) 313-325
4. Eguchi N., Minami T., Shirafuji N., Kanaoka Y., Tanaka T., Nagata A., Yoshida N., Urade Y., Ito S., and Hayashi O. Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D synthase-deficient mice. Proc. Natl. Acad. Sci. USA 96 (1999) 726-730
5. Urade Y., and Hayaishi O. Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase. Biochim. Biophys. Acta 1482 (2000) 259-271
6. Shibahara S., Han F., Li B., and Takeda K. Hypoxia and heme oxygenases: oxygen sensing and regulation of expression. Antiox. Redox Signal. 9 (2007) 2209-2225
7. Furuyama K., Kaneko K., and Vargas P.D. Heme as a magnificent molecule with multiple missions: heme determines its own fate and governs cellular homeostasis. Tohoku J. Exp. Med. 213 (2007) 1-16
8. 2 induces heme oxygenase-1 in human retinal pigment epithelial cells. Biochem. Biophys. Res. Commun. 67 (2008) 413-419
9. Leung K.W., Liu M., Xu X., Seiler M.J., Barnstable C.J., and Tombran-Tink J. Expression of ZnT and ZIP zinc transporters in the human RPE and their regulation by neurotrophic factors. Invest. Ophthalmol. Vis. Sci. 49 (2008) 1221-1231
10. Beuckmann C.T., Gordo W.C., Kanaoka Y., Eguchi N., Marcheselli V.L., Gerashchenko D.Y., Urade Y., Hayaishi O., and Bazan N.G. Lipocalin-type prostaglandin D synthase (beta-trace) is located in pigment epithelial cells of rat retina and accumulate within interphotoreceptor matrix. J. Neurosci. 16 (1996) 6119-6124
11. Takeda K., Yokoyama S., Aburatani H., Masuda T., Han F., Yoshizawa M., Yamaki N., Yamamoto H., Eguchi N., Urade Y., and Shibahara S. Lipocalin-type prostaglandin D synthase as a melanocyte marker regulated by MITF. Biochem. Biophys. Res. Commun. 339 (2006) 1098-1106
12. Frank R.N., Amin R.H., and Puklin J.E. Antioxidant enzymes in the macular retinal pigment epithelium of eyes with neovascular age-related macular degeneration. Am. J. Ophthalmol. 127 (1999) 694-709
13. Wills N.K., Ramanujam V.M., Chang J., Kalariya N., Lewis J.R., Weng T.X., and van Kuijk F.J. Cadmium accumulation in the human retina: effects of age, gender, and cellular toxicity. Exp. Eye Res. 86 (2008) 41-51
14. Erie J.C., Good J.A., Butz J.A., Hodge D.O., and Pulido J.S. Urinary cadmium and age-related macular degeneration. Am. J. Ophthalmol. 144 (2007) 414-418
15. Beare N.A., Taylor T.E., Harding S.P., Lewallen S., and Molyneux M.E. Malarial retinopathy: a newly established diagnostic sign in severe malaria. Am. J. Trop. Med. Hyg. 75 (2006) 790-797
16. Turner G. Cerebral malaria. Brain Pathol. 7 (1997) 569-582
17. Schluesener H.J., Kremsner P.G., and Meyermann R. Heme oxygenase-1 in lesions of human cerebral malaria. Acta Neuropathol. (Berl) 101 (2001) 65-68
18. Shibahara S. The heme oxygenase dilemma in cellular homeostasis: new insights for the feedback regulation of heme catabolism. Tohoku J. Exp. Med. 200 (2003) 167-186
19. Takeda M., Kikuchi M., Ubalee R., Na-Bangchang K., Ruangweerayut R., Shibahara S., Imai S., and Hirayama K. Microsatellite polymorphism in the heme oxygenease-1 gene promoter is associated with susceptibility to cerebral malaria in Myanmar. Jpn. J. Infect. Dis. 58 (2005) 268-271
20. Kilunga Kubata B., Eguchi N., Urade Y., Yamashita K., Mitamura T., Tai K., Hayaishi O., and Horii T. Plasmodium falciparum produces prostaglandins that are pyrogenic, somnogenic, and immunosuppressive substances in humans. J. Exp. Med. 188 (1998) 1197-1202
21. Dunn K.C., Aotaki-Keen A.E., Putkey F.R., and Hjelmeland L.M. ARPE-19, a human retinal pigment epithelial cell line with differentiated properties. Exp. Eye Res. 62 (1996) 155-169
22. Davis A.A., Bernstein P.S., Bok D., Turner J., Nachtigal M., and Hunt R.C. A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture. Invest. Ophthalmol. Vis. Sci. 36 (1995) 955-964
23. Zhang Y., Furuyama K., Kaneko K., Ding Y., Ogawa K., Yoshizawa M., Kawamura M., Takeda K., Yoshida T., and Shibahara S. Hypoxia reduces the expression of heme oxygenase-2 in various types of human cell lines: a possible strategy for the maintenance of intracellular heme level. FEBS J. 273 (2006) 3136-3147
24. Udono-Fujimori R., Takahashi K., Takeda K., Furuyama K., Kaneko K., Takahashi S., Tamai M., and Shibahara S. Expression of heme oxygenase-1 is repressed by interferon-γ and induced by hypoxia in human retinal pigment epithelial cells. Eur. J. Biochem. 271 (2004) 3076-3084
25. Takahashi S., Takahashi Y., Ito K., Nagano T., Shibahara S., and Miura T. Positive and negative regulation of the human heme oxygenase-1 gene expression in cultured cells. Biochim. Biophys. Acta 1447 (1999) 231-235
26. Gerashchenko D., Beuckmann C.T., Kanaoka Y., Eguchi N., Gordon W.C., Urade Y., Bazan N.G., and Hayaishi O. Dominant expression of rat prostanoid DP receptor mRNA in leptomeninges, inner segments of photoreceptor cells, iris epithelium, and ciliary processes. J. Neurochem. 71 (1998) 937-945
27. 2 receptor, CRTH2. Br. J. Pharmacol. 137 (2002) 1163-1172
28. Takeda K., Ishizawa S., Sato M., Yoshida T., and Shibahara S. Identification of a cis-acting element that is responsible for cadmium-mediated induction of the human heme oxygenase gene. J. Biol. Chem. 269 (1994) 22858-22867
29. Satarug S., Nishijo M., Lasker J.M., Edwards R.J., and Moore M.R. Kidney dysfunction and hypertension: role for cadmium, p450 and heme oxygenases?. Tohoku J. Exp. Med. 208 (2006) 179-202
30. Erie J.C., Butz J.A., Good J.A., Erie E.A., Burritt M.F., and Cameron J.D. Heavy metal concentrations in human eyes. Am. J. Ophthalmol. 139 (2005) 888-893
31. Miyamura N., Ogawa T., Boylan S., Morse L.S., Handa J.T., and Hjelmeland L.M. Topographic and age-dependent expression of heme oxygenase-1 and catalase in the human retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 45 (2004) 1562-1565
32. McCoubrey W.K., Huang T.J., and Maines M.D. Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. J. Biol. Chem. 272 (1997) 12568-12574