메뉴 건너뛰기




Volumn 38, Issue 3, 2014, Pages 188-195

Proteasome inhibition induces both antioxidant and hb f responses in sickle cell disease via the nrf2 pathway

Author keywords

Antioxidant response; Hb F; Nuclear factor (erythroid derived 2) like 2 (NFE2L2 of Nrf2); Proteasome inhibitors; Reactive oxygen species (ROS); Sickle cell disease

Indexed keywords

ANTIOXIDANT; BORTEZOMIB; GLUTATHIONE; HEMOGLOBIN F; IMMUNOGLOBULIN; IXAZOMIB CITRATE; PROTEASOME; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR NRF2; ANTINEOPLASTIC AGENT; ATP DEPENDENT 26S PROTEASE; BORONIC ACID DERIVATIVE; NFE2L2 PROTEIN, HUMAN; PROTEASOME INHIBITOR; PYRAZINE DERIVATIVE;

EID: 84900468337     PISSN: 03630269     EISSN: 1532432X     Source Type: Journal    
DOI: 10.3109/03630269.2014.898651     Document Type: Article
Times cited : (13)

References (32)
  • 1
    • 79956089142 scopus 로고    scopus 로고
    • Oxidative stress in sickle cell disease: Pathophysiology and potential implications for disease management
    • Nur E, Biemond BJ, Otten H-MB, et al. Oxidative stress in sickle cell disease: Pathophysiology and potential implications for disease management. Am J Hematol. 2011;86(6):484-489.
    • (2011) Am J Hematol , vol.86 , Issue.6 , pp. 484-489
    • Nur, E.1    Biemond, B.J.2    H-Mb, O.3
  • 2
    • 69549107429 scopus 로고    scopus 로고
    • Vasculopathy in sickle cell disease: Biology, pathophysiology, genetics, translational medicine and new research directions
    • Kato GJ, Hebbel RP, Steinberg MH, Gladwin MT. Vasculopathy in sickle cell disease: Biology, pathophysiology, genetics, translational medicine and new research directions. Am J Hematol. 2009; 84(9):618-625.
    • (2009) Am J Hematol , vol.84 , Issue.9 , pp. 618-625
    • Kato, G.J.1    Hebbel, R.P.2    Steinberg, M.H.3    Gladwin, M.T.4
  • 4
    • 20444468127 scopus 로고    scopus 로고
    • Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice
    • Wood KC, Hebbel RP, Granger DN. Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice. FASEB J. 2005;19(8):989-991.
    • (2005) Faseb J , vol.19 , Issue.8 , pp. 989-991
    • Wood, K.C.1    Hebbel, R.P.2    Granger, D.N.3
  • 5
    • 3042621306 scopus 로고    scopus 로고
    • Anti-inflammatory therapy ameliorates leukocyte adhesion and microvascular flow abnormalities in transgenic sickle mice
    • Kaul DK, Liu XD, Choong S, et al. Anti-inflammatory therapy ameliorates leukocyte adhesion and microvascular flow abnormalities in transgenic sickle mice. Am J Physiol Heart Circ Physiol. 2004;287(1):H293-H301.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287 , Issue.1
    • Kaul, D.K.1    Liu, X.D.2    Choong, S.3
  • 6
    • 79851512889 scopus 로고    scopus 로고
    • Small molecule modulators of antioxidant response pathway
    • Hur W, Gray NS. Small molecule modulators of antioxidant response pathway. Curr Opin Chem Biol. 2011;15(1):162-173.
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.1 , pp. 162-173
    • Hur, W.1    Gray, N.S.2
  • 7
    • 79954416526 scopus 로고    scopus 로고
    • The cytoprotective role of the Keap1-Nrf2 pathway
    • Baird L, Dinkova-Kostova AT. The cytoprotective role of the Keap1-Nrf2 pathway. Arch Toxicol. 2011;85(4):241-272.
    • (2011) Arch Toxicol , vol.85 , Issue.4 , pp. 241-272
    • Baird, L.1    Dinkova-Kostova, A.T.2
  • 8
    • 77958115724 scopus 로고    scopus 로고
    • Regulation of the Nrf2-Keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases
    • Villeneuve NF, Lau A, Zhang DD. Regulation of the Nrf2-Keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases. Antioxid Redox Signal. 2010;13(11):1699-1712.
    • (2010) Antioxid Redox Signal , vol.13 , Issue.11 , pp. 1699-1712
    • Villeneuve, N.F.1    Lau, A.2    Zhang, D.D.3
  • 9
    • 79958007234 scopus 로고    scopus 로고
    • Induction of human fetal hemoglobin via the NRF2 antioxidant response signaling pathway
    • Macari ER, Lowrey CH. Induction of human fetal hemoglobin via the NRF2 antioxidant response signaling pathway. Blood. 2011; 117(22):5987-5997.
    • (2011) Blood , vol.117 , Issue.22 , pp. 5987-5997
    • Macari, E.R.1    Lowrey, C.H.2
  • 10
    • 79960147525 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia
    • Akinsheye I, Alsultan A, Solovieff N, et al. Fetal hemoglobin in sickle cell anemia. Blood. 2011;118(1):19-27.
    • (2011) Blood , vol.118 , Issue.1 , pp. 19-27
    • Akinsheye, I.1    Alsultan, A.2    Solovieff, N.3
  • 11
    • 0028291736 scopus 로고
    • Mortality in sickle cell disease. Life expectancy and risk factors for early death
    • Platt OS, Brambilla DJ, Rosse WF, et al. Mortality in sickle cell disease. Life expectancy and risk factors for early death. N Engl J Med. 1994;330(23):1639-1644.
    • (1994) N Engl J Med , vol.330 , Issue.23 , pp. 1639-1644
    • Platt, O.S.1    Brambilla, D.J.2    Rosse, W.F.3
  • 12
    • 0025770390 scopus 로고
    • Pain in sickle cell disease. Rates and risk factors
    • Platt OS, Thorington BD, Brambilla DJ, et al. Pain in sickle cell disease. Rates and risk factors. N Engl J Med. 1991;325(1):11-16.
    • (1991) N Engl J Med , vol.325 , Issue.1 , pp. 11-16
    • Platt, O.S.1    Thorington, B.D.2    Brambilla, D.J.3
  • 13
    • 84857642529 scopus 로고    scopus 로고
    • Expression of fetal hemoglobin in adult humans exposed to high altitude hypoxia
    • Risso A, Fabbro D, Damante G, Antonutto G. Expression of fetal hemoglobin in adult humans exposed to high altitude hypoxia. Blood Cells Molec Dis. 2012;48(3):147-153.
    • (2012) Blood Cells Molec Dis , vol.48 , Issue.3 , pp. 147-153
    • Risso, A.1    Fabbro, D.2    Damante, G.3    Antonutto, G.4
  • 14
    • 0031463908 scopus 로고    scopus 로고
    • BFU-E colony growth in response to hydroxyurea: Correlation between in vitro and in vivo fetal hemoglobin induction
    • Yang YM, Pace B, Kitchens D, et al. BFU-E colony growth in response to hydroxyurea: Correlation between in vitro and in vivo fetal hemoglobin induction. Am J Hematol. 1997;56(4):252-258.
    • (1997) Am J Hematol , vol.56 , Issue.4 , pp. 252-258
    • Yang, Y.M.1    Pace, B.2    Kitchens, D.3
  • 15
    • 0038045578 scopus 로고    scopus 로고
    • In vitro induction of fetal hemoglobin in human erythroid progenitor cells
    • Ho JA, Pickens CV, Gamscik MP, et al. In vitro induction of fetal hemoglobin in human erythroid progenitor cells. Exp Hematol. 2003;31(7):586-591.
    • (2003) Exp Hematol , vol.31 , Issue.7 , pp. 586-591
    • Ho, J.A.1    Pickens, C.V.2    Gamscik, M.P.3
  • 16
    • 78651096626 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic study of two doses of bortezomib in patients with relapsed multiple myeloma
    • Reece DE, Sullivan D, Lonial S, et al. Pharmacokinetic and pharmacodynamic study of two doses of bortezomib in patients with relapsed multiple myeloma. Cancer Chemother Pharmacol. 2011;67(1):57-67.
    • (2011) Cancer Chemother Pharmacol , vol.67 , Issue.1 , pp. 57-67
    • Reece, D.E.1    Sullivan, D.2    Lonial, S.3
  • 17
    • 0034595064 scopus 로고    scopus 로고
    • Inhibition of the 26S proteasome induces expression of GLCLC, the catalytic subunit for gamma-glutamylcysteine synthetase
    • Sekhar KR, Soltanninassab SR, Borrelli MJ, et al. Inhibition of the 26S proteasome induces expression of GLCLC, the catalytic subunit for gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 2000;270(1):311-317.
    • (2000) Biochem Biophys Res Commun , vol.270 , Issue.1 , pp. 311-317
    • Sekhar, K.R.1    Soltanninassab, S.R.2    Borrelli, M.J.3
  • 18
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D, Killeen E, Naquin R, et al. Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J Biol Chem. 2003; 278(4):2396-2402.
    • (2003) J Biol Chem , vol.278 , Issue.4 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3
  • 19
    • 0032032313 scopus 로고    scopus 로고
    • A proteasome inhibitor, an antioxidant or a salicylate, but not a glucocorticoid blocks constitutive and cytokine-inducible expression of P-selectin in human endothelial cells
    • Xia L, Pan J, Yao L, McEver RP. A proteasome inhibitor, an antioxidant or a salicylate, but not a glucocorticoid blocks constitutive and cytokine-inducible expression of P-selectin in human endothelial cells. Blood. 1998;91(5):1625-1632.
    • (1998) Blood , vol.91 , Issue.5 , pp. 1625-1632
    • Xia, L.1    Pan, J.2    Yao, L.3    McEver, R.P.4
  • 20
    • 84867744658 scopus 로고    scopus 로고
    • Proteasome inhibition decreases inflammation in human endothelial cells exposed to liposaccharide
    • Lalu MM, Xu H, Sankaralingam S, Davidge ST. Proteasome inhibition decreases inflammation in human endothelial cells exposed to liposaccharide. J Cardiovasc Pharmacol. 2012; 60(4):381-389.
    • (2012) J Cardiovasc Pharmacol , vol.60 , Issue.4 , pp. 381-389
    • Lalu, M.M.1    Xu, H.2    Sankaralingam, S.3    Davidge, S.T.4
  • 21
    • 84867818765 scopus 로고    scopus 로고
    • Reawakening fetal hemoglobin: Prospects for new therapies for the b-globin disorders
    • Bauer DE, Kamran SC, Orkin SH. Reawakening fetal hemoglobin: Prospects for new therapies for the b-globin disorders. Blood. 2012; 120(15):2945-2953.
    • (2012) Blood , vol.120 , Issue.15 , pp. 2945-2953
    • Bauer, D.E.1    Kamran, S.C.2    Orkin, S.H.3
  • 22
    • 78649719826 scopus 로고    scopus 로고
    • Reversing the hemoglobin switch
    • Sankaran VG, Nathan DG. Reversing the hemoglobin switch. N Engl J Med. 2010;363(23):2258-2260.
    • (2010) N Engl J Med , vol.363 , Issue.23 , pp. 2258-2260
    • Sankaran, V.G.1    Nathan, D.G.2
  • 23
    • 80052500364 scopus 로고    scopus 로고
    • Progress in understanding the hemoglobin switch
    • Forget BG. Progress in understanding the hemoglobin switch. N Engl J Med. 2011;365(9):852-854.
    • (2011) N Engl J Med , vol.365 , Issue.9 , pp. 852-854
    • Forget, B.G.1
  • 24
    • 80855133522 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics, and pharmacogenetics of hydroxyurea treatment for children with sickle cell anemia
    • Ware RE, Despotovic JM, Mortier NA, et al. Pharmacokinetics, pharmacodynamics, and pharmacogenetics of hydroxyurea treatment for children with sickle cell anemia. Blood. 2011; 118(18):4985-4991.
    • (2011) Blood , vol.118 , Issue.18 , pp. 4985-4991
    • Ware, R.E.1    Despotovic, J.M.2    Mortier, N.A.3
  • 25
    • 77956840802 scopus 로고    scopus 로고
    • Hydroxyurea therapy requires HbF induction for clinical benefit in a sickle cell mouse model
    • Lebensburger JD, Pestina TI, Ware RE, et al. Hydroxyurea therapy requires HbF induction for clinical benefit in a sickle cell mouse model. Haematologica. 2010;95(9):1599-1603.
    • (2010) Haematologica , vol.95 , Issue.9 , pp. 1599-1603
    • Lebensburger, J.D.1    Pestina, T.I.2    Ware, R.E.3
  • 26
    • 0030893396 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia: Determinants of response to hydroxyurea
    • Steinberg MH, Lu Z-H, Barton FB, et al. Fetal hemoglobin in sickle cell anemia: Determinants of response to hydroxyurea. Blood. 1997;89(3):1078-1088.
    • (1997) Blood , vol.89 , Issue.3 , pp. 1078-1088
    • Steinberg, M.H.1    Lu, Z.-H.2    Barton, F.B.3
  • 27
    • 64549108112 scopus 로고    scopus 로고
    • Oxidative stress by targeted agents promotes cytotoxicity in hematologic malignancies
    • Chandra J. Oxidative stress by targeted agents promotes cytotoxicity in hematologic malignancies. Antioxid Redox Signal. 2009; 11(5):1123-1137.
    • (2009) Antioxid Redox Signal , vol.11 , Issue.5 , pp. 1123-1137
    • Chandra, J.1
  • 28
    • 84858321881 scopus 로고    scopus 로고
    • Next-generation proteasome blockers promise safer cancer therapy
    • doi:10.1038/nm0112-7a
    • Mullard A. Next-generation proteasome blockers promise safer cancer therapy. Nat Med. 2012;18(1):7. doi:10.1038/nm0112-7a.
    • (2012) Nat Med , vol.18 , Issue.1 , pp. 7
    • Mullard, A.1
  • 29
    • 77649237033 scopus 로고    scopus 로고
    • Building on bortezomib: Second generation proteasome inhibitors as anti-cancer therapy
    • Dick LR, Fleming PE. Building on bortezomib: Second generation proteasome inhibitors as anti-cancer therapy. Drug Discov Today. 2010;15(5-6):243-249.
    • (2010) Drug Discov Today , vol.15 , Issue.5-6 , pp. 243-249
    • Dick, L.R.1    Fleming, P.E.2
  • 30
    • 84865552564 scopus 로고    scopus 로고
    • An open-label, singlearm, phase 2 study of single-agent carfilzomib in patients with relapsed and/or refractory multiple myeloma who have been previously treated with bortezomib
    • Vij R, Siegel DS, Jagannath S, et al. An open-label, singlearm, phase 2 study of single-agent carfilzomib in patients with relapsed and/or refractory multiple myeloma who have been previously treated with bortezomib. Br J Haematol. 2012; 158(6):739-748.
    • (2012) Br J Haematol , vol.158 , Issue.6 , pp. 739-748
    • Vij, R.1    Siegel, D.S.2    Jagannath, S.3
  • 31
    • 77950238258 scopus 로고    scopus 로고
    • Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer
    • Kupperman E, Lee EC, Cao Y, et al. Evaluation of the proteasome inhibitor MLN9708 in preclinical models of human cancer. Cancer Res. 2010;70(5):1970- 1980.
    • (2010) Cancer Res , vol.70 , Issue.5 , pp. 1970-1980
    • Kupperman, E.1    Lee, E.C.2    Cao, Y.3
  • 32
    • 80051691845 scopus 로고    scopus 로고
    • In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells
    • Chauhan D, Tian Z, Zhou B, et al. In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells. Clin Cancer Res. 2011;17(16):5311-5532.
    • (2011) Clin Cancer Res , vol.17 , Issue.16 , pp. 5311-5532
    • Chauhan, D.1    Tian, Z.2    Zhou, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.