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Volumn 87, Issue 3, 2008, Pages 268-278

Exacerbated corneal inflammation and neovascularization in the HO-2 null mice is ameliorated by biliverdin

Author keywords

biliverdin; hemangiogenesis; heme oxygenase; inflammation; lymphangiogenesis

Indexed keywords

BILIVERDIN;

EID: 50849094843     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2008.06.007     Document Type: Article
Times cited : (26)

References (60)
  • 2
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • Abraham N.G., and Kappas A. Pharmacological and clinical aspects of heme oxygenase. Pharmacol. Rev. 60 (2008) 79-127
    • (2008) Pharmacol. Rev. , vol.60 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 3
    • 0023232407 scopus 로고
    • Presence of heme oxygensae and NADPH cytochrome P450 (c) reductase in human corneal epithelium
    • Abraham N.G., Lin J., Dunn M.W., and Schwartzman M.L. Presence of heme oxygensae and NADPH cytochrome P450 (c) reductase in human corneal epithelium. Invest. Ophthalmol. Vis. Sci. 28 (1987) 1464-1472
    • (1987) Invest. Ophthalmol. Vis. Sci. , vol.28 , pp. 1464-1472
    • Abraham, N.G.1    Lin, J.2    Dunn, M.W.3    Schwartzman, M.L.4
  • 4
    • 6944229471 scopus 로고    scopus 로고
    • Heme oxygenase-1 induced in Muller cells plays a protective role in retinal ischemia-reperfusion injury in rats
    • Arai-Gaun S., Katai N., Kikuchi T., Kurokawa T., Ohta K., and Yoshimura N. Heme oxygenase-1 induced in Muller cells plays a protective role in retinal ischemia-reperfusion injury in rats. Invest. Ophthalmol. Vis. Sci. 45 (2004) 4226-4232
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 4226-4232
    • Arai-Gaun, S.1    Katai, N.2    Kikuchi, T.3    Kurokawa, T.4    Ohta, K.5    Yoshimura, N.6
  • 5
  • 7
    • 0034723274 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase-2 by hypoxia and PPAR ligands in the rabbit corneal epithelium
    • Bonazzi A., Mastyugin V., Mieyal P.A., Dunn M.W., and Laniado Schwartzman M. Regulation of cyclooxygenase-2 by hypoxia and PPAR ligands in the rabbit corneal epithelium. J. Biol. Chem. 275 (2000) 2837-2844
    • (2000) J. Biol. Chem. , vol.275 , pp. 2837-2844
    • Bonazzi, A.1    Mastyugin, V.2    Mieyal, P.A.3    Dunn, M.W.4    Laniado Schwartzman, M.5
  • 8
    • 0038206550 scopus 로고    scopus 로고
    • Heme oxygenase-2 protects against lipid peroxidation-mediated cell loss and impaired motor recovery after traumatic brain injury
    • Chang E.F., Wong R.J., Vreman H.J., Igarashi T., Galo E., Sharp F.R., Stevenson D.K., and Noble-Haeusslein L.J. Heme oxygenase-2 protects against lipid peroxidation-mediated cell loss and impaired motor recovery after traumatic brain injury. J. Neurosci. 23 (2003) 3689-3696
    • (2003) J. Neurosci. , vol.23 , pp. 3689-3696
    • Chang, E.F.1    Wong, R.J.2    Vreman, H.J.3    Igarashi, T.4    Galo, E.5    Sharp, F.R.6    Stevenson, D.K.7    Noble-Haeusslein, L.J.8
  • 9
    • 0037099359 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene transfer inhibits inducible nitric oxide synthase expression and protects genetically fat Zucker rat livers from ischemia-reperfusion injury
    • Coito A.J., Buelow R., Shen X.D., Amersi F., Moore C., Volk H.D., Busuttil R.W., and Kupiec-Weglinski J.W. Heme oxygenase-1 gene transfer inhibits inducible nitric oxide synthase expression and protects genetically fat Zucker rat livers from ischemia-reperfusion injury. Transplantation 74 (2002) 96-102
    • (2002) Transplantation , vol.74 , pp. 96-102
    • Coito, A.J.1    Buelow, R.2    Shen, X.D.3    Amersi, F.4    Moore, C.5    Volk, H.D.6    Busuttil, R.W.7    Kupiec-Weglinski, J.W.8
  • 10
    • 0028917018 scopus 로고
    • A closed eye-contact lens model of corneal inflammation. II. Inhibition of cytochrome P450 arachidonic acid metabolism alleviates inflammatory sequelae
    • Conners M.S., Stoltz R.A., Dunn M.W., Levere R.D., Abraham N.G., and Schwartzman M.L. A closed eye-contact lens model of corneal inflammation. II. Inhibition of cytochrome P450 arachidonic acid metabolism alleviates inflammatory sequelae. Invest. Ophthalmol. Vis. Sci. 36 (1995) 841-850
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 841-850
    • Conners, M.S.1    Stoltz, R.A.2    Dunn, M.W.3    Levere, R.D.4    Abraham, N.G.5    Schwartzman, M.L.6
  • 12
    • 33745026496 scopus 로고    scopus 로고
    • Time course of angiogenesis and lymphangiogenesis after brief corneal inflammation
    • Cursiefen C., Maruyama K., Jackson D.G., Streilein J.W., and Kruse F.E. Time course of angiogenesis and lymphangiogenesis after brief corneal inflammation. Cornea 25 (2006) 443-447
    • (2006) Cornea , vol.25 , pp. 443-447
    • Cursiefen, C.1    Maruyama, K.2    Jackson, D.G.3    Streilein, J.W.4    Kruse, F.E.5
  • 14
    • 33751071823 scopus 로고    scopus 로고
    • Down-regulation of heme oxygenase-2 is associated with the increased expression of heme oxygenase-1 in human cell lines
    • Ding Y., Zhang Y.Z., Furuyama K., Ogawa K., Igarashi K., and Shibahara S. Down-regulation of heme oxygenase-2 is associated with the increased expression of heme oxygenase-1 in human cell lines. FEBS J. 273 (2006) 5333-5346
    • (2006) FEBS J. , vol.273 , pp. 5333-5346
    • Ding, Y.1    Zhang, Y.Z.2    Furuyama, K.3    Ogawa, K.4    Igarashi, K.5    Shibahara, S.6
  • 18
    • 13244285610 scopus 로고    scopus 로고
    • Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults
    • Foresti R., Green C.J., and Motterlini R. Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults. Biochem. Soc. Symp. (2004) 177-192
    • (2004) Biochem. Soc. Symp. , pp. 177-192
    • Foresti, R.1    Green, C.J.2    Motterlini, R.3
  • 19
    • 35648987863 scopus 로고    scopus 로고
    • Biliverdin inhibits activation of NF-kappaB: reversal of inhibition by human biliverdin reductase
    • Gibbs P.E., and Maines M.D. Biliverdin inhibits activation of NF-kappaB: reversal of inhibition by human biliverdin reductase. Int. J. Cancer 121 (2007) 2567-2574
    • (2007) Int. J. Cancer , vol.121 , pp. 2567-2574
    • Gibbs, P.E.1    Maines, M.D.2
  • 21
    • 0034720318 scopus 로고    scopus 로고
    • Functional human heme oxygenase has a neuroprotective effect on adult rat ganglion cells after pressure-induced ischemia
    • Hegazy K.A., Dunn M.W., and Sharma S.C. Functional human heme oxygenase has a neuroprotective effect on adult rat ganglion cells after pressure-induced ischemia. Neuroreport 11 (2000) 1185-1189
    • (2000) Neuroreport , vol.11 , pp. 1185-1189
    • Hegazy, K.A.1    Dunn, M.W.2    Sharma, S.C.3
  • 23
    • 22544454485 scopus 로고    scopus 로고
    • Catalytically inactive heme oxygenase-2 mutant is cytoprotective
    • Kim Y.S., and Dore S. Catalytically inactive heme oxygenase-2 mutant is cytoprotective. Free Radic. Biol. Med. 39 (2005) 558-564
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 558-564
    • Kim, Y.S.1    Dore, S.2
  • 24
    • 10344219952 scopus 로고    scopus 로고
    • Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity
    • Kim Y.S., Zhuang H., Koehler R.C., and Dore S. Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity. Free Radic. Biol. Med. 38 (2005) 85-92
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 85-92
    • Kim, Y.S.1    Zhuang, H.2    Koehler, R.C.3    Dore, S.4
  • 27
    • 0037340031 scopus 로고    scopus 로고
    • Heme oxygenase attenuates angiotensin II-mediated increase in cyclooxygenase-2 activity in human femoral endothelial cells
    • Li Volti G., Seta F., Schwartzman M.L., Nasjletti A., and Abraham N.G. Heme oxygenase attenuates angiotensin II-mediated increase in cyclooxygenase-2 activity in human femoral endothelial cells. Hypertension 41 (2003) 715-719
    • (2003) Hypertension , vol.41 , pp. 715-719
    • Li Volti, G.1    Seta, F.2    Schwartzman, M.L.3    Nasjletti, A.4    Abraham, N.G.5
  • 28
    • 0023731036 scopus 로고    scopus 로고
    • Heme oxygenase: function, multiplicity, regulatory mechanisms and clinical applications
    • Maines M.D. Heme oxygenase: function, multiplicity, regulatory mechanisms and clinical applications. FASEB J. 2 (1998) 2557-2568
    • (1998) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 30
    • 1842330947 scopus 로고    scopus 로고
    • Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis
    • McCoubrey Jr. 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
    • (1997) J. Biol. Chem. , vol.272 , pp. 12568-12574
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 35
    • 0242509964 scopus 로고    scopus 로고
    • Protective role of heme oxygenase-1 against endotoxin-induced uveitis in rats
    • Ohta K., Kikuchi T., Arai S., Yoshida N., Sato A., and Yoshimura N. Protective role of heme oxygenase-1 against endotoxin-induced uveitis in rats. Exp. Eye Res. 77 (2003) 665-673
    • (2003) Exp. Eye Res. , vol.77 , pp. 665-673
    • Ohta, K.1    Kikuchi, T.2    Arai, S.3    Yoshida, N.4    Sato, A.5    Yoshimura, N.6
  • 37
    • 0036096305 scopus 로고    scopus 로고
    • Carbon monoxide: innovative anti-inflammatory properties of an age-old gas molecule
    • Otterbein L.E. Carbon monoxide: innovative anti-inflammatory properties of an age-old gas molecule. Antioxid. Redox. Signal 4 (2002) 309-319
    • (2002) Antioxid. Redox. Signal , vol.4 , pp. 309-319
    • Otterbein, L.E.1
  • 40
    • 33646436473 scopus 로고    scopus 로고
    • Glutamate induces oxidative stress and apoptosis in cerebral vascular endothelial cells: contributions of HO-1 and HO-2 to cytoprotection
    • Parfenova H., Basuroy S., Bhattacharya S., Tcheranova D., Qu Y., Regan R.F., and Leffler C.W. Glutamate induces oxidative stress and apoptosis in cerebral vascular endothelial cells: contributions of HO-1 and HO-2 to cytoprotection. Am. J. Physiol. Cell Physiol. 290 (2006) C1399-C1410
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Parfenova, H.1    Basuroy, S.2    Bhattacharya, S.3    Tcheranova, D.4    Qu, Y.5    Regan, R.F.6    Leffler, C.W.7
  • 41
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) 2002-2007
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2002-2007
    • Pfaffl, M.W.1
  • 42
    • 0028880959 scopus 로고
    • Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
    • Poss K.D., Thomas M.J., Ebralidze A.K., O'Dell T.J., and Tonegawa S. Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice. Neuron 15 (1995) 867-873
    • (1995) Neuron , vol.15 , pp. 867-873
    • Poss, K.D.1    Thomas, M.J.2    Ebralidze, A.K.3    O'Dell, T.J.4    Tonegawa, S.5
  • 43
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss K.D., and Tonegawa S. Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 10919-10924
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 44
    • 0141749478 scopus 로고    scopus 로고
    • Heme oxygenase-2 knockout neurons are less vulnerable to hemoglobin toxicity
    • Rogers B., Yakopson V., Teng Z.P., Guo Y., and Regan R.F. Heme oxygenase-2 knockout neurons are less vulnerable to hemoglobin toxicity. Free Radic. Biol. Med. 35 (2003) 872-881
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 872-881
    • Rogers, B.1    Yakopson, V.2    Teng, Z.P.3    Guo, Y.4    Regan, R.F.5
  • 45
    • 2542461143 scopus 로고    scopus 로고
    • Carbon monoxide: to boldly go where NO has gone before
    • Ryter S.W., Morse D., and Choi A.M. Carbon monoxide: to boldly go where NO has gone before. Sci. STKE 2004 (2004) RE6
    • (2004) Sci. STKE , vol.2004
    • Ryter, S.W.1    Morse, D.2    Choi, A.M.3
  • 46
    • 1542314436 scopus 로고    scopus 로고
    • Carbon monoxide in biology and medicine
    • Ryter S.W., and Otterbein L.E. Carbon monoxide in biology and medicine. Bioessays 26 (2004) 270-280
    • (2004) Bioessays , vol.26 , pp. 270-280
    • Ryter, S.W.1    Otterbein, L.E.2
  • 50
    • 0242525192 scopus 로고    scopus 로고
    • The heme oxygenase dilemma in cellular homeostasis: new insights for the feedback regulation of heme catabolism
    • 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
    • (2003) Tohoku J. Exp. Med. , vol.200 , pp. 167-186
    • Shibahara, S.1
  • 52
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker R., Yamamoto Y., McDonagh A.F., Glazer A.N., and Ames B.N. Bilirubin is an antioxidant of possible physiological importance. Science 235 (1987) 1043-1046
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 53
    • 0032881831 scopus 로고    scopus 로고
    • Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression
    • Wagener F.A., da Silva J.L., Farley T., de Witte T., Kappas A., and Abraham N.G. Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression. J. Pharmacol. Exp. Ther. 291 (1999) 416-423
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 416-423
    • Wagener, F.A.1    da Silva, J.L.2    Farley, T.3    de Witte, T.4    Kappas, A.5    Abraham, N.G.6
  • 55
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: a novel target for the modulation of the inflammatory response
    • Willis D., Moore A.R., Frederick R., and Willoughby D.A. Heme oxygenase: a novel target for the modulation of the inflammatory response. Nat. Med. 2 (1996) 87-90
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.