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Volumn 2011, Issue , 2011, Pages

Heme oxygenase-1: A critical link between iron metabolism, erythropoiesis, and development

Author keywords

[No Author keywords available]

Indexed keywords

HEME OXYGENASE 1;

EID: 84855599543     PISSN: 16879104     EISSN: 16879112     Source Type: Journal    
DOI: 10.1155/2011/473709     Document Type: Review
Times cited : (62)

References (43)
  • 2
    • 33846476692 scopus 로고    scopus 로고
    • Methemoglobin - It's not just blue: A concise review
    • DOI 10.1002/ajh.20738
    • Umbreit J., MethemoglobinIt's not just blue: a concise review American Journal of Hematology 2007 82 2 134 144 (Pubitemid 46155276)
    • (2007) American Journal of Hematology , vol.82 , Issue.2 , pp. 134-144
    • Umbreit, J.1
  • 3
    • 77954611973 scopus 로고    scopus 로고
    • Iron loading and overloading due to ineffective erythropoiesis
    • Tanno T., Miller J. L., Iron loading and overloading due to ineffective erythropoiesis Advances in Hematology 2010 2010 8
    • (2010) Advances in Hematology , vol.2010 , pp. 8
    • Tanno, T.1    Miller, J.L.2
  • 4
    • 52549119182 scopus 로고    scopus 로고
    • A central role for free heme in the pathogenesis of severe malaria: The missing link?
    • Ferreira A., Balla J., Jeney V., Balla G., Soares M. P., A central role for free heme in the pathogenesis of severe malaria: the missing link? Journal of Molecular Medicine 2008 86 10 1097 1111
    • (2008) Journal of Molecular Medicine , vol.86 , Issue.10 , pp. 1097-1111
    • Ferreira, A.1    Balla, J.2    Jeney, V.3    Balla, G.4    Soares, M.P.5
  • 7
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
    • Ryter S. W., Alam J., Choi A. M. K., Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications Physiological Reviews 2006 86 2 583 650
    • (2006) Physiological Reviews , vol.86 , Issue.2 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.K.3
  • 8
    • 33750969074 scopus 로고    scopus 로고
    • Heme oxygenase-1: A novel drug target for atherosclerotic diseases?
    • DOI 10.1161/CIRCULATIONAHA.105.598698, PII 0000301720061114000016
    • Stocker R., Perrella M. A., Heme oxygenase-1: a novel drug target for atherosclerotic diseases? Circulation 2006 114 20 2178 2189 (Pubitemid 44747899)
    • (2006) Circulation , vol.114 , Issue.20 , pp. 2178-2189
    • Stocker, R.1    Perrella, M.A.2
  • 9
    • 0036672234 scopus 로고    scopus 로고
    • Heme oxygenase: Evolution, structure, and mechanism
    • Wilks A., Heme oxygenase: evolution, structure, and mechanism Antioxidants and Redox Signaling 2002 4 4 603 614 (Pubitemid 35001444)
    • (2002) Antioxidants and Redox Signaling , vol.4 , Issue.4 , pp. 603-614
    • Wilks, A.1
  • 10
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible
    • Maines M. D., Trakshel G. M., Kutty R. K., Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible Journal of Biological Chemistry 1986 261 1 411 419 (Pubitemid 16103962)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.1 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 11
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse I., Maines M. D., Evidence suggesting that the two forms of heme oxygenase are products of different genes Journal of Biological Chemistry 1988 263 7 3348 3353 (Pubitemid 18072793)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.7 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 13
    • 3042737456 scopus 로고    scopus 로고
    • Caveolae compartmentalization of hemeoxygenase-1 in endothelial cells
    • DOI 10.1096/fj.03-1391com
    • Kim H. P., Wang X., Galbiati F., Ryter S. W., Choi A. M. K., Caveolae compartmentalization of hemeoxygenase-1 in endothelial cells FASEB Journal 2004 18 10 1080 1089 (Pubitemid 38859216)
    • (2004) FASEB Journal , vol.18 , Issue.10 , pp. 1080-1089
    • Kim, H.P.1    Wang, X.2    Galbiati, F.3    Ryter, S.W.4    Choi, A.M.K.5
  • 16
    • 0033405452 scopus 로고    scopus 로고
    • Development of erythroid and myeloid progenitors in the yolk sac and embryo proper of the mouse
    • Palis J., Robertson S., Kennedy M., Wall C., Keller G., Development of erythroid and myeloid progenitors in the yolk sac and embryo proper of the mouse Development 1999 126 22 5073 5084 (Pubitemid 30000420)
    • (1999) Development , vol.126 , Issue.22 , pp. 5073-5084
    • Palis, J.1    Robertson, S.2    Kennedy, M.3    Wall, C.4    Keller, G.5
  • 19
    • 79955945782 scopus 로고    scopus 로고
    • A transient definitive erythroid lineage with unique regulation of the -globin locus in the mammalian embryo
    • McGrath K. E., Frame J. M., Fromm G. J., Koniski A. D., Kingsley P. D., Little J., Bulger M., Palis J., A transient definitive erythroid lineage with unique regulation of the -globin locus in the mammalian embryo Blood 2011 117 17 4600 4608
    • (2011) Blood , vol.117 , Issue.17 , pp. 4600-4608
    • McGrath, K.E.1    Frame, J.M.2    Fromm, G.J.3    Koniski, A.D.4    Kingsley, P.D.5    Little, J.6    Bulger, M.7    Palis, J.8
  • 20
    • 34247129126 scopus 로고    scopus 로고
    • Molecular insights into stress erythropoiesis
    • DOI 10.1097/MOH.0b013e3280de2bf1, PII 0006275220070500000007
    • Socolovsky M., Molecular insights into stress erythropoiesis Current Opinion in Hematology 2007 14 3 215 224 (Pubitemid 46597606)
    • (2007) Current Opinion in Hematology , vol.14 , Issue.3 , pp. 215-224
    • Socolovsky, M.1
  • 21
    • 0002574844 scopus 로고
    • Erythroblastic island, functional unity of bone marrow
    • Bessis M., Erythroblastic island, functional unity of bone marrow Review of Hematology 1958 13 1 8 11
    • (1958) Review of Hematology , vol.13 , Issue.1 , pp. 8-11
    • Bessis, M.1
  • 22
    • 50949089311 scopus 로고    scopus 로고
    • Erythroblastic islands: Niches for erythropoiesis
    • Chasis J. A., Mohandas N., Erythroblastic islands: niches for erythropoiesis Blood 2008 112 3 470 478
    • (2008) Blood , vol.112 , Issue.3 , pp. 470-478
    • Chasis, J.A.1    Mohandas, N.2
  • 23
    • 33845980163 scopus 로고    scopus 로고
    • Maturation and enucleation of primitive erythroblasts during mouse embryogenesis is accompanied by changes in cell-surface antigen expression
    • DOI 10.1182/blood-2006-03-006569
    • Fraser S. T., Isern J., Baron M. H., Maturation and enucleation of primitive erythroblasts during mouse embryogenesis is accompanied by changes in cell-surface antigen expression Blood 2007 109 1 343 352 (Pubitemid 46053076)
    • (2007) Blood , vol.109 , Issue.1 , pp. 343-352
    • Fraser, S.T.1    Isern, J.2    Baron, M.H.3
  • 24
    • 0035760889 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in Stat5a -/- 5b -/- mice due to decreased survival of early erythroblasts
    • Socolovsky M., Nam H. S., Fleming M. D., Haase V. H., Brugnara C., Lodish H. F., Ineffective erythropoiesis in Stat5a -/- 5b -/- mice due to decreased survival of early erythroblasts Blood 2001 98 12 3261 3273
    • (2001) Blood , vol.98 , Issue.12 , pp. 3261-3273
    • Socolovsky, M.1    Nam, H.S.2    Fleming, M.D.3    Haase, V.H.4    Brugnara, C.5    Lodish, H.F.6
  • 26
    • 0035947178 scopus 로고    scopus 로고
    • Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver
    • DOI 10.1126/science.292.5521.1546
    • Kawane K., Fukuyama H., Kondoh G., Takeda J., Ohsawa Y., Uchiyama Y., Nagata S., Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver Science 2001 292 5521 1546 1549 (Pubitemid 32493423)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1546-1549
    • Kawane, K.1    Fukuyama, H.2    Kondoh, G.3    Takeda, J.4    Ohsawa, Y.5    Uchiyama, Y.6    Nagata, S.7
  • 27
    • 0021828779 scopus 로고
    • In vivo recognition and clearance of red blood cells containing phosphatidylserine in their plasma membranes
    • Schroit A. J., Madsen J. W., Tanaka Y., In vivo recognition and clearance of red blood cells containing phosphatidylserine in their plasma membranes Journal of Biological Chemistry 1985 260 8 5131 5138 (Pubitemid 15031516)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.8 , pp. 5131-5138
    • Schroit, A.J.1    Madsen, J.W.2    Tanaka, Y.3
  • 28
    • 34548120227 scopus 로고    scopus 로고
    • Reduced expression of CD47 during murine red blood cell (RBC) senescence and its role in RBC clearance from the circulation
    • DOI 10.1111/j.1537-2995.2007.01348.x
    • Khandelwal S., Van Rooijen N., Saxena R. K., Reduced expression of CD47 during murine red blood cell (RBC) senescence and its role in RBC clearance from the circulation Transfusion 2007 47 9 1725 1732 (Pubitemid 47300620)
    • (2007) Transfusion , vol.47 , Issue.9 , pp. 1725-1732
    • Khandelwal, S.1    Van Rooijen, N.2    Saxena, R.K.3
  • 30
    • 70149083005 scopus 로고    scopus 로고
    • Effect of heme oxygenase-1 deficiency on placental development
    • Zhao H., Wong R. J., Kalish F. S., Nayak N. R., Stevenson D. K., Effect of heme oxygenase-1 deficiency on placental development Placenta 2009 30 10 861 868
    • (2009) Placenta , vol.30 , Issue.10 , pp. 861-868
    • Zhao, H.1    Wong, R.J.2    Kalish, F.S.3    Nayak, N.R.4    Stevenson, D.K.5
  • 32
    • 78650676293 scopus 로고    scopus 로고
    • Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: Effects on macrophage viability and tissue iron distribution
    • Kovtunovych G., Eckhaus M. A., Ghosh M. C., Ollivierre-Wilson H., Rouault T. A., Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: effects on macrophage viability and tissue iron distribution Blood 2010 116 26 6054 6062
    • (2010) Blood , vol.116 , Issue.26 , pp. 6054-6062
    • Kovtunovych, G.1    Eckhaus, M.A.2    Ghosh, M.C.3    Ollivierre-Wilson, H.4    Rouault, T.A.5
  • 35
    • 34147164095 scopus 로고    scopus 로고
    • Human heme oxygenase-1 deficiency: A lesson on serendipity in the discovery of the novel disease
    • DOI 10.1111/j.1442-200X.2007.02353.x
    • Koizumi S., Human heme oxygenase-1 deficiency: a lesson on serendipity in the discovery of the novel disease Pediatrics International 2007 49 2 125 132 (Pubitemid 46558301)
    • (2007) Pediatrics International , vol.49 , Issue.2 , pp. 125-132
    • Koizumi, S.1
  • 37
    • 1942539932 scopus 로고    scopus 로고
    • Marked developmental changes in heme oxygenase-1 (HO-1) expression in the mouse placenta: Correlation between HO-1 expression and placental development
    • DOI 10.1016/j.placenta.2003.10.012
    • Watanabe S., Akagi R., Mori M., Tsuchiya T., Sassa S., Marked developmental changes in heme oxygenase-1 (HO-1) expression in the mouse placenta: correlation between HO-1 expression and placental development Placenta 2004 25 5 387 395 (Pubitemid 38519112)
    • (2004) Placenta , vol.25 , Issue.5 , pp. 387-395
    • Watanabe, S.1    Akagi, R.2    Mori, M.3    Tsuchiya, T.4    Sassa, S.5
  • 38
    • 67349114109 scopus 로고    scopus 로고
    • Inhibitors of heme oxygenase reduce invasion of human primary cytotrophoblast cells in vitro
    • McCaig D., Lyall F., Inhibitors of heme oxygenase reduce invasion of human primary cytotrophoblast cells in vitro Placenta 2009 30 6 536 538
    • (2009) Placenta , vol.30 , Issue.6 , pp. 536-538
    • McCaig, D.1    Lyall, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.