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Volumn 13, Issue 1, 2016, Pages

Heme oxygenase-1 promotes neuron survival through down-regulation of neuronal NLRP1 expression after spinal cord injury

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; HEME OXYGENASE 1; INFLAMMASOME; NOD LIKE RECEPTOR PROTEIN 1; UNCLASSIFIED DRUG; ACTIVATING TRANSCRIPTION FACTOR 4; ATF4 PROTEIN, RAT; HYDROGEN PEROXIDE; NALP1 PROTEIN, RAT; NERVE PROTEIN;

EID: 84963753938     PISSN: None     EISSN: 17422094     Source Type: Journal    
DOI: 10.1186/s12974-016-0521-y     Document Type: Article
Times cited : (63)

References (80)
  • 3
    • 84889030920 scopus 로고    scopus 로고
    • Managing inflammation after spinal cord injury through manipulation of macrophage function
    • Ren Y, Young W. Managing inflammation after spinal cord injury through manipulation of macrophage function. Neural Plast. 2013;2013:945034.
    • (2013) Neural Plast , vol.2013 , pp. 945034
    • Ren, Y.1    Young, W.2
  • 7
    • 84927659436 scopus 로고    scopus 로고
    • Disrupted autophagy after spinal cord injury is associated with ER stress and neuronal cell death
    • Liu S, Sarkar C, Dinizo M, Faden AI, Koh EY, Lipinski MM, et al. Disrupted autophagy after spinal cord injury is associated with ER stress and neuronal cell death. Cell Death Dis. 2015;6, e1582.
    • (2015) Cell Death Dis , vol.6
    • Liu, S.1    Sarkar, C.2    Dinizo, M.3    Faden, A.I.4    Koh, E.Y.5    Lipinski, M.M.6    Wu, J.7
  • 8
    • 3042816808 scopus 로고    scopus 로고
    • The role of excitotoxicity in secondary mechanisms of spinal cord injury: a review with an emphasis on the implications for white matter degeneration
    • Park E, Velumian AA, Fehlings MG. The role of excitotoxicity in secondary mechanisms of spinal cord injury: a review with an emphasis on the implications for white matter degeneration. J Neurotrauma. 2004;21:754-74.
    • (2004) J Neurotrauma , vol.21 , pp. 754-774
    • Park, E.1    Velumian, A.A.2    Fehlings, M.G.3
  • 9
    • 84941189756 scopus 로고    scopus 로고
    • Neuronal NLRP1 inflammasome activation of Caspase-1 coordinately regulates inflammatory interleukin-1-beta production and axonal degeneration-associated Caspase-6 activation
    • Kaushal V, Dye R, Pakavathkumar P, Foveau B, Flores J, Hyman B, et al. Neuronal NLRP1 inflammasome activation of Caspase-1 coordinately regulates inflammatory interleukin-1-beta production and axonal degeneration-associated Caspase-6 activation. Cell Death Differ. 2015;22:1676-86.
    • (2015) Cell Death Differ , vol.22 , pp. 1676-1686
    • Kaushal, V.1    Dye, R.2    Pakavathkumar, P.3    Foveau, B.4    Flores, J.5    Hyman, B.6    Ghetti, B.7    Koller, B.H.8    LeBlanc, A.C.9
  • 12
    • 84934989890 scopus 로고    scopus 로고
    • NLRP1 inflammasome is activated in patients with medial temporal lobe epilepsy and contributes to neuronal pyroptosis in amygdala kindling-induced rat model
    • Tan CC, Zhang JG, Tan MS, Chen H, Meng DW, Jiang T, et al. NLRP1 inflammasome is activated in patients with medial temporal lobe epilepsy and contributes to neuronal pyroptosis in amygdala kindling-induced rat model. J Neuroinflammation. 2015;12:18.
    • (2015) J Neuroinflammation , vol.12 , pp. 18
    • Tan, C.C.1    Zhang, J.G.2    Tan, M.S.3    Chen, H.4    Meng, D.W.5    Jiang, T.6    Meng, X.F.7    Li, Y.8    Sun, Z.9    Li, M.M.10
  • 13
    • 84927745897 scopus 로고    scopus 로고
    • Pyroptotic cell death defends against intracellular pathogens
    • Jorgensen I, Miao EA. Pyroptotic cell death defends against intracellular pathogens. Immunol Rev. 2015;265:130-42.
    • (2015) Immunol Rev , vol.265 , pp. 130-142
    • Jorgensen, I.1    Miao, E.A.2
  • 14
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 2002;10:417-26.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 16
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes. Nat Rev Immunol. 2013;13:397-411.
    • (2013) Nat Rev Immunol , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 17
    • 0030606250 scopus 로고    scopus 로고
    • Evidence for the neuronal origin of immunoreactive interleukin-1 beta released by rat hypothalamic explants
    • Tringali G, Mancuso C, Mirtella A, Pozzoli G, Parente L, Preziosi P, et al. Evidence for the neuronal origin of immunoreactive interleukin-1 beta released by rat hypothalamic explants. Neurosci Lett. 1996;219:143-6.
    • (1996) Neurosci Lett , vol.219 , pp. 143-146
    • Tringali, G.1    Mancuso, C.2    Mirtella, A.3    Pozzoli, G.4    Parente, L.5    Preziosi, P.6    Navarra, P.7
  • 18
    • 0031259599 scopus 로고    scopus 로고
    • The release of immunoreactive interleukin-1 beta from rat hypothalamic explants is modulated by neurotransmitters and corticotropin-releasing hormone
    • Tringali G, Mirtella A, Mancuso C, Guerriero G, Preziosi P, Navarra P. The release of immunoreactive interleukin-1 beta from rat hypothalamic explants is modulated by neurotransmitters and corticotropin-releasing hormone. Pharmacol Res. 1997;36:269-73.
    • (1997) Pharmacol Res , vol.36 , pp. 269-273
    • Tringali, G.1    Mirtella, A.2    Mancuso, C.3    Guerriero, G.4    Preziosi, P.5    Navarra, P.6
  • 20
    • 67649360450 scopus 로고    scopus 로고
    • Therapeutic neutralization of the NLRP1 inflammasome reduces the innate immune response and improves histopathology after traumatic brain injury
    • de Rivero Vaccari JP, Lotocki G, Alonso OF, Bramlett HM, Dietrich WD, Keane RW. Therapeutic neutralization of the NLRP1 inflammasome reduces the innate immune response and improves histopathology after traumatic brain injury. J Cereb Blood Flow Metab. 2009;29:1251-61.
    • (2009) J Cereb Blood Flow Metab , vol.29 , pp. 1251-1261
    • Rivero Vaccari, J.P.1    Lotocki, G.2    Alonso, O.F.3    Bramlett, H.M.4    Dietrich, W.D.5    Keane, R.W.6
  • 22
    • 78049442406 scopus 로고    scopus 로고
    • Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential
    • Paine A, Eiz-Vesper B, Blasczyk R, Immenschuh S. Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential. Biochem Pharmacol. 2010;80:1895-903.
    • (2010) Biochem Pharmacol , vol.80 , pp. 1895-1903
    • Paine, A.1    Eiz-Vesper, B.2    Blasczyk, R.3    Immenschuh, S.4
  • 23
    • 70450137050 scopus 로고    scopus 로고
    • The heme oxygenase/biliverdin reductase pathway in drug research and development
    • Mancuso C, Barone E. The heme oxygenase/biliverdin reductase pathway in drug research and development. Curr Drug Metab. 2009;10:579-94.
    • (2009) Curr Drug Metab , vol.10 , pp. 579-594
    • Mancuso, C.1    Barone, E.2
  • 24
    • 0031579657 scopus 로고    scopus 로고
    • Regulation of heme oxygenase-2 by glucocorticoids in neonatal rat brain: characterization of a functional glucocorticoid response element
    • Raju VS, McCoubrey Jr WK, Maines MD. Regulation of heme oxygenase-2 by glucocorticoids in neonatal rat brain: characterization of a functional glucocorticoid response element. Biochim Biophys Acta. 1997;1351:89-104.
    • (1997) Biochim Biophys Acta , vol.1351 , pp. 89-104
    • Raju, V.S.1    McCoubrey, W.K.2    Maines, M.D.3
  • 25
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: a regulator of second messenger gases
    • Maines MD. The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol. 1997;37:517-54.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 27
    • 0025953506 scopus 로고
    • Interleukin-1 and tumour necrosis factor induce hepatic haem oxygenase. Feedback regulation by glucocorticoids
    • Cantoni L, Rossi C, Rizzardini M, Gadina M, Ghezzi P. Interleukin-1 and tumour necrosis factor induce hepatic haem oxygenase. Feedback regulation by glucocorticoids. Biochem J. 1991;279(Pt 3):891-4.
    • (1991) Biochem J , vol.279 , pp. 891-894
    • Cantoni, L.1    Rossi, C.2    Rizzardini, M.3    Gadina, M.4    Ghezzi, P.5
  • 30
    • 0032748074 scopus 로고    scopus 로고
    • Inhibition of heme oxygenase in the central nervous system potentiates endotoxin-induced vasopressin release in the rat
    • Mancuso C, Ragazzoni E, Tringali G, Liberale I, Preziosi P, Grossman A, et al. Inhibition of heme oxygenase in the central nervous system potentiates endotoxin-induced vasopressin release in the rat. J Neuroimmunol. 1999;99:189-94.
    • (1999) J Neuroimmunol , vol.99 , pp. 189-194
    • Mancuso, C.1    Ragazzoni, E.2    Tringali, G.3    Liberale, I.4    Preziosi, P.5    Grossman, A.6    Navarra, P.7
  • 31
    • 0035142856 scopus 로고    scopus 로고
    • Site of injury-directed induction of heme oxygenase-1 and -2 in experimental spinal cord injury: differential functions in neuronal defense mechanisms?
    • Panahian N, Maines MD. Site of injury-directed induction of heme oxygenase-1 and -2 in experimental spinal cord injury: differential functions in neuronal defense mechanisms? J Neurochem. 2001;76:539-54.
    • (2001) J Neurochem , vol.76 , pp. 539-554
    • Panahian, N.1    Maines, M.D.2
  • 33
    • 34247495046 scopus 로고    scopus 로고
    • Heme oxygenase-1 stabilizes the blood-spinal cord barrier and limits oxidative stress and white matter damage in the acutely injured murine spinal cord
    • Lin Y, Vreman HJ, Wong RJ, Tjoa T, Yamauchi T, Noble-Haeusslein LJ. Heme oxygenase-1 stabilizes the blood-spinal cord barrier and limits oxidative stress and white matter damage in the acutely injured murine spinal cord. J Cereb Blood Flow Metab. 2007;27:1010-21.
    • (2007) J Cereb Blood Flow Metab , vol.27 , pp. 1010-1021
    • Lin, Y.1    Vreman, H.J.2    Wong, R.J.3    Tjoa, T.4    Yamauchi, T.5    Noble-Haeusslein, L.J.6
  • 34
    • 84860517355 scopus 로고    scopus 로고
    • Docosahexaenoic acid, but not eicosapentaenoic acid, reduces the early inflammatory response following compression spinal cord injury in the rat
    • Hall JC, Priestley JV, Perry VH, Michael-Titus AT. Docosahexaenoic acid, but not eicosapentaenoic acid, reduces the early inflammatory response following compression spinal cord injury in the rat. J Neurochem. 2012;121:738-50.
    • (2012) J Neurochem , vol.121 , pp. 738-750
    • Hall, J.C.1    Priestley, J.V.2    Perry, V.H.3    Michael-Titus, A.T.4
  • 35
    • 0030971385 scopus 로고    scopus 로고
    • Neurogenesis in postnatal rat spinal cord: a study in primary culture
    • Kehl LJ, Fairbanks CA, Laughlin TM, Wilcox GL. Neurogenesis in postnatal rat spinal cord: a study in primary culture. Science. 1997;276:586-9.
    • (1997) Science , vol.276 , pp. 586-589
    • Kehl, L.J.1    Fairbanks, C.A.2    Laughlin, T.M.3    Wilcox, G.L.4
  • 37
    • 0028919411 scopus 로고
    • A sensitive and reliable locomotor rating scale for open field testing in rats
    • Basso DM, Beattie MS, Bresnahan JC. A sensitive and reliable locomotor rating scale for open field testing in rats. J Neurotrauma. 1995;12:1-21.
    • (1995) J Neurotrauma , vol.12 , pp. 1-21
    • Basso, D.M.1    Beattie, M.S.2    Bresnahan, J.C.3
  • 40
    • 84891745975 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response in the rat contusive spinal cord injury model-susceptibility in specific cell types
    • Matsuyama D, Watanabe M, Suyama K, Kuroiwa M, Mochida J. Endoplasmic reticulum stress response in the rat contusive spinal cord injury model-susceptibility in specific cell types. Spinal Cord. 2014;52:9-16.
    • (2014) Spinal Cord , vol.52 , pp. 9-16
    • Matsuyama, D.1    Watanabe, M.2    Suyama, K.3    Kuroiwa, M.4    Mochida, J.5
  • 41
    • 35648982325 scopus 로고    scopus 로고
    • Cell cycle activation contributes to post-mitotic cell death and secondary damage after spinal cord injury
    • Byrnes KR, Stoica BA, Fricke S, Di Giovanni S, Faden AI. Cell cycle activation contributes to post-mitotic cell death and secondary damage after spinal cord injury. Brain. 2007;130:2977-92.
    • (2007) Brain , vol.130 , pp. 2977-2992
    • Byrnes, K.R.1    Stoica, B.A.2    Fricke, S.3    Giovanni, S.4    Faden, A.I.5
  • 46
    • 84929428860 scopus 로고    scopus 로고
    • Activation and regulation of NLRP3 inflammasome by intrathecal application of SDF-1a in a spinal cord injury model
    • Epub ahead of print
    • Zendedel A, Johann S, Mehrabi S, Joghataei MT, Hassanzadeh G, Kipp M, Beyer C. Activation and regulation of NLRP3 inflammasome by intrathecal application of SDF-1a in a spinal cord injury model. Mol Neurobiol. 2015. Epub ahead of print.
    • (2015) Mol Neurobiol
    • Zendedel, A.1    Johann, S.2    Mehrabi, S.3    Joghataei, M.T.4    Hassanzadeh, G.5    Kipp, M.6    Beyer, C.7
  • 47
    • 77956262043 scopus 로고    scopus 로고
    • Sensing cytoplasmic danger signals by the inflammasome
    • Alnemri ES. Sensing cytoplasmic danger signals by the inflammasome. J Clin Immunol. 2010;30:512-9.
    • (2010) J Clin Immunol , vol.30 , pp. 512-519
    • Alnemri, E.S.1
  • 48
  • 49
    • 84862649049 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) and inflammasome actions in the central nervous system
    • Hanamsagar R, Hanke ML, Kielian T. Toll-like receptor (TLR) and inflammasome actions in the central nervous system. Trends Immunol. 2012;33:333-42.
    • (2012) Trends Immunol , vol.33 , pp. 333-342
    • Hanamsagar, R.1    Hanke, M.L.2    Kielian, T.3
  • 50
    • 84945438257 scopus 로고    scopus 로고
    • Beta-amyloid, microglia, and the inflammasome in Alzheimer's disease
    • Gold M, El Khoury J. Beta-amyloid, microglia, and the inflammasome in Alzheimer's disease. Semin Immunopathol. 2015;37:607-11.
    • (2015) Semin Immunopathol , vol.37 , pp. 607-611
    • Gold, M.1    Khoury, J.2
  • 51
    • 84880491311 scopus 로고    scopus 로고
    • Assessing beta-amyloid-induced NLRP3 inflammasome activation in primary microglia
    • Schnaars M, Beckert H, Halle A. Assessing beta-amyloid-induced NLRP3 inflammasome activation in primary microglia. Methods Mol Biol. 2013;1040:1-8.
    • (2013) Methods Mol Biol , vol.1040 , pp. 1-8
    • Schnaars, M.1    Beckert, H.2    Halle, A.3
  • 54
    • 33750601026 scopus 로고    scopus 로고
    • The innate immune facet of brain: human neurons express TLR-3 and sense viral dsRNA
    • Lafon M, Megret F, Lafage M, Prehaud C. The innate immune facet of brain: human neurons express TLR-3 and sense viral dsRNA. J Mol Neurosci. 2006;29:185-94.
    • (2006) J Mol Neurosci , vol.29 , pp. 185-194
    • Lafon, M.1    Megret, F.2    Lafage, M.3    Prehaud, C.4
  • 56
    • 77953627102 scopus 로고    scopus 로고
    • Human neuronal cells possess functional cytoplasmic and TLR-mediated innate immune pathways influenced by phosphatidylinositol-3 kinase signaling
    • Peltier DC, Simms A, Farmer JR, Miller DJ. Human neuronal cells possess functional cytoplasmic and TLR-mediated innate immune pathways influenced by phosphatidylinositol-3 kinase signaling. J Immunol. 2010;184:7010-21.
    • (2010) J Immunol , vol.184 , pp. 7010-7021
    • Peltier, D.C.1    Simms, A.2    Farmer, J.R.3    Miller, D.J.4
  • 58
    • 4143064639 scopus 로고    scopus 로고
    • Hemin induces heme oxygenase-1 in spinal cord vasculature and attenuates barrier disruption and neutrophil infiltration in the injured murine spinal cord
    • Yamauchi T, Lin Y, Sharp FR, Noble-Haeusslein LJ. Hemin induces heme oxygenase-1 in spinal cord vasculature and attenuates barrier disruption and neutrophil infiltration in the injured murine spinal cord. J Neurotrauma. 2004;21:1017-30.
    • (2004) J Neurotrauma , vol.21 , pp. 1017-1030
    • Yamauchi, T.1    Lin, Y.2    Sharp, F.R.3    Noble-Haeusslein, L.J.4
  • 59
    • 79955671381 scopus 로고    scopus 로고
    • Uptake, metabolism and toxicity of hemin in cultured neurons
    • Dang TN, Robinson SR, Dringen R, Bishop GM. Uptake, metabolism and toxicity of hemin in cultured neurons. Neurochem Int. 2011;58:804-11.
    • (2011) Neurochem Int , vol.58 , pp. 804-811
    • Dang, T.N.1    Robinson, S.R.2    Dringen, R.3    Bishop, G.M.4
  • 60
    • 0030188587 scopus 로고    scopus 로고
    • Heme oxygenase-1: function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury
    • Choi AM, Alam J. Heme oxygenase-1: function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am J Respir Cell Mol Biol. 1996;15:9-19.
    • (1996) Am J Respir Cell Mol Biol , vol.15 , pp. 9-19
    • Choi, A.M.1    Alam, J.2
  • 61
    • 33745839704 scopus 로고    scopus 로고
    • beta-Carotene and cigarette smoke condensate regulate heme oxygenase-1 and its repressor factor Bach1: relationship with cell growth
    • Palozza P, Serini S, Curro D, Calviello G, Igarashi K, Mancuso C. beta-Carotene and cigarette smoke condensate regulate heme oxygenase-1 and its repressor factor Bach1: relationship with cell growth. Antioxid Redox Signal. 2006;8:1069-80.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1069-1080
    • Palozza, P.1    Serini, S.2    Curro, D.3    Calviello, G.4    Igarashi, K.5    Mancuso, C.6
  • 63
    • 59849125389 scopus 로고    scopus 로고
    • Genetic ablation of transcription repressor Bach1 reduces neural tissue damage and improves locomotor function after spinal cord injury in mice
    • Kanno H, Ozawa H, Dohi Y, Sekiguchi A, Igarashi K, Itoi E. Genetic ablation of transcription repressor Bach1 reduces neural tissue damage and improves locomotor function after spinal cord injury in mice. J Neurotrauma. 2009;26:31-9.
    • (2009) J Neurotrauma , vol.26 , pp. 31-39
    • Kanno, H.1    Ozawa, H.2    Dohi, Y.3    Sekiguchi, A.4    Igarashi, K.5    Itoi, E.6
  • 64
    • 84876992081 scopus 로고    scopus 로고
    • Induction of hemeoxygenase-1 expression after inhibition of hemeoxygenase activity promotes inflammation and worsens ischemic brain damage in mice
    • Perez-de-Puig I, Martin A, Gorina R, de la Rosa X, Martinez E, Planas AM. Induction of hemeoxygenase-1 expression after inhibition of hemeoxygenase activity promotes inflammation and worsens ischemic brain damage in mice. Neuroscience. 2013;243:22-32.
    • (2013) Neuroscience , vol.243 , pp. 22-32
    • Perez-de-Puig, I.1    Martin, A.2    Gorina, R.3    Rosa, X.4    Martinez, E.5    Planas, A.M.6
  • 65
    • 30344477376 scopus 로고    scopus 로고
    • The experimental study of hypoxia-inducible factor-1alpha and its target genes in spinal cord injury
    • Xiaowei H, Ninghui Z, Wei X, Yiping T, Linfeng X. The experimental study of hypoxia-inducible factor-1alpha and its target genes in spinal cord injury. Spinal Cord. 2006;44:35-43.
    • (2006) Spinal Cord , vol.44 , pp. 35-43
    • Xiaowei, H.1    Ninghui, Z.2    Wei, X.3    Yiping, T.4    Linfeng, X.5
  • 69
    • 84907456216 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 attenuates lipopolysaccharide-induced inflammasome activation in human gingival epithelial cells
    • Li H, Zhou X, Zhang J. Induction of heme oxygenase-1 attenuates lipopolysaccharide-induced inflammasome activation in human gingival epithelial cells. Int J Mol Med. 2014;34:1039-44.
    • (2014) Int J Mol Med , vol.34 , pp. 1039-1044
    • Li, H.1    Zhou, X.2    Zhang, J.3
  • 71
    • 84861601576 scopus 로고    scopus 로고
    • Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment
    • Barone E, Di Domenico F, Sultana R, Coccia R, Mancuso C, Perluigi M, et al. Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment. Free Radic Biol Med. 2012;52:2292-301.
    • (2012) Free Radic Biol Med , vol.52 , pp. 2292-2301
    • Barone, E.1    Domenico, F.2    Sultana, R.3    Coccia, R.4    Mancuso, C.5    Perluigi, M.6    Butterfield, D.A.7
  • 73
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • He CH, Gong P, Hu B, Stewart D, Choi ME, Choi AM, et al. Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation. J Biol Chem. 2001;276:20858-65.
    • (2001) J Biol Chem , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 75
    • 84907907866 scopus 로고    scopus 로고
    • Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses
    • Biswas C, Shah N, Muthu M, La P, Fernando AP, Sengupta S, et al. Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses. J Biol Chem. 2014;289:26882-94.
    • (2014) J Biol Chem , vol.289 , pp. 26882-26894
    • Biswas, C.1    Shah, N.2    Muthu, M.3    La, P.4    Fernando, A.P.5    Sengupta, S.6    Yang, G.7    Dennery, P.A.8
  • 79
    • 84889094297 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of molecular hydrogen in LPS-stimulated RAW 264.7 macrophages
    • Chen HG, Xie KL, Han HZ, Wang WN, Liu DQ, Wang GL, et al. Heme oxygenase-1 mediates the anti-inflammatory effect of molecular hydrogen in LPS-stimulated RAW 264.7 macrophages. Int J Surg. 2013;11:1060-6.
    • (2013) Int J Surg , vol.11 , pp. 1060-1066
    • Chen, H.G.1    Xie, K.L.2    Han, H.Z.3    Wang, W.N.4    Liu, D.Q.5    Wang, G.L.6    Yu, Y.H.7
  • 80
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
    • Lee TS, Chau LY. Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice. Nat Med. 2002;8:240-6.
    • (2002) Nat Med , vol.8 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2


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