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Volumn 117, Issue 14, 2011, Pages 3881-3892

G-CSF improves murine G6PC3-deficient neutrophil function by modulating

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ADENOSINE TRIPHOSPHATE; CALCIUM; CASPASE 3; CASPASE 9; CYTOCHROME C; GLUCOSE; GLUCOSE 6 PHOSPHATASE; GLUCOSE 6 PHOSPHATASE BETA; GLUCOSE 6 PHOSPHATE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; INITIATION FACTOR 2ALPHA; LACTIC ACID; LIPOCORTIN 5; MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN BAX; PROTEIN KINASE B; PROTEIN MCL 1; REACTIVE OXYGEN METABOLITE; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; UNCLASSIFIED DRUG;

EID: 79953818388     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-08-302059     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 0345306587 scopus 로고    scopus 로고
    • A Glucose-6-phosphate Hydrolase, Widely Expressed Outside the Liver, Can Explain Age-dependent Resolution of Hypoglycemia in Glycogen Storage Disease Type Ia
    • DOI 10.1074/jbc.M309472200
    • Shieh J-J, Pan C-J, Mansfield BC, Chou JY.Glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain agedependent resolution of hypoglycemia in glycogen storage disease type Ia. J Biol Chem. 2003; 278(47):47098-47103. (Pubitemid 37452295)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47098-47103
    • Shieh, J.-J.1    Pan, C.-J.2    Mansfield, B.C.3    Chou, J.Y.4
  • 2
    • 1842582072 scopus 로고    scopus 로고
    • Histidine 167 Is the Phosphate Acceptor in Glucose-6-phosphatase-β Forming a Phosphohistidine Enzyme Intermediate during Catalysis
    • DOI 10.1074/jbc.M313271200
    • Ghosh A, Shieh J-J, Pan C-J, Chou JY. Histidine- 167 is the phosphate acceptor in glucose-6- phosphatase-beta forming a phosphohistidineenzyme intermediate during catalysis. J Biol Chem. 2004;279(13):12479-12483. (Pubitemid 38445817)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12479-12483
    • Ghosh, A.1    Shieh, J.-J.2    Pan, C.-J.3    Chou, J.Y.4
  • 3
    • 0033605362 scopus 로고    scopus 로고
    • Inactivation of the glucose 6-phosphate transporter causes glycogen storage disease type 1b
    • DOI 10.1074/jbc.274.9.5532
    • Hiraiwa H, Pan C-J, Lin B, Moses SW, Chou JY. Inactivation of the glucose-6-phosphate transporter causes glycogen storage disease type 1b. J Biol Chem. 1999;274(9):5532-5536. (Pubitemid 29109201)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.9 , pp. 5532-5536
    • Hiraiwa, H.1    Pan, C.-J.2    Lin, B.3    Moses, S.W.4    Chou, J.Y.5
  • 4
    • 0036086034 scopus 로고    scopus 로고
    • Type I glycogen storage diseases: Disorders of the glucose-6-phosphatase complex
    • Chou JY, Matern D, Mansfield BC, Chen Y-T. Type I glycogen storage diseases: disorders of the glucose-6-phosphatase complex. Curr Mol Med. 2002;2(2):121-143. (Pubitemid 34649836)
    • (2002) Current Molecular Medicine , vol.2 , Issue.2 , pp. 121-143
    • Chou, J.Y.1    Matern, D.2    Mansfield, B.C.3    Chen, Y.-T.4
  • 5
    • 32444436610 scopus 로고    scopus 로고
    • Glucose-6-phosphate transporter: The key to glycogen storage disease type Ib
    • Broer S,Wagner CA, eds New York, NY:Springer
    • Chou JY, Mansfield BC. Glucose-6-phosphate transporter: the key to glycogen storage disease type Ib. In: Broer S, Wagner CA, eds. Membrane Transporter Diseases. New York, NY: Springer; 2003:191-205.
    • (2003) Membrane Transporter Diseases , pp. 191-205
    • Chou, J.Y.1    Mansfield, B.C.2
  • 6
    • 0038383286 scopus 로고    scopus 로고
    • Apoptotic neutrophils in the circulation of patients with glycogen storage disease type 1b (GSD1b)
    • Kuijpers TW, Maianski NA, Tool AT, et al. Apoptotic neutrophils in the circulation of patients with glycogen storage disease type 1b (GSD1b). Blood. 2003;101(12):5021-5024. (Pubitemid 36857768)
    • (2003) Blood , vol.101 , Issue.12 , pp. 5021-5024
    • Kuijpers, T.W.1    Maianski, N.A.2    Tool, A.T.J.3    Smit, G.P.A.4    Rake, J.P.5    Roos, D.6    Visser, G.7
  • 7
    • 33847420515 scopus 로고    scopus 로고
    • Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase- beta
    • Cheung YY, Kim SY, Yiu WH, et al. Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase- beta. J Clin Invest. 2007;117(3):784-793.
    • (2007) J Clin Invest , vol.117 , Issue.3 , pp. 784-793
    • Cheung, Y.Y.1    Kim, S.Y.2    Yiu, W.H.3
  • 8
    • 58249089770 scopus 로고    scopus 로고
    • A syndrome with congenital neutropenia and mutations in G6PC3
    • Boztug K, Appaswamy G, Ashikov A, et al. A syndrome with congenital neutropenia and mutations in G6PC3. N Engl J Med. 2009;360(1):32-43.
    • (2009) N Engl J Med , vol.360 , Issue.1 , pp. 32-43
    • Boztug, K.1    Appaswamy, G.2    Ashikov, A.3
  • 9
    • 47049108414 scopus 로고    scopus 로고
    • Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type Ib
    • Kim SY, Jun HS, Mead PA, Mansfield BC, Chou JY. Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type Ib. Blood. 2008;111(12):5704-5711.
    • (2008) Blood , vol.111 , Issue.12 , pp. 5704-5711
    • Kim, S.Y.1    Jun, H.S.2    Mead, P.A.3    Mansfield, B.C.4    Chou, J.Y.5
  • 10
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem. 2005;74:739-789. (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 11
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • DOI 10.1038/sj.cdd.4401378
    • Rao RV, Ellerby HM, Bredesen DE. Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ. 2004;11(2):372-380. (Pubitemid 38489415)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.4 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 12
    • 63849157597 scopus 로고    scopus 로고
    • Regulation of neutrophil apoptosis by modulation of PKB/Akt activation
    • Rane MJ, Klein JB. Regulation of neutrophil apoptosis by modulation of PKB/Akt activation. Front Biosci. 2009;14:2400-2412.
    • (2009) Front Biosci , vol.14 , pp. 2400-2412
    • Rane, M.J.1    Klein, J.B.2
  • 13
    • 71549172179 scopus 로고    scopus 로고
    • PI-3-K and AKT: Onto the mitochondria
    • Stiles BL. PI-3-K and AKT: onto the mitochondria. Adv Drug Deliv Rev. 2009;61(14):1276-1282.
    • (2009) Adv Drug Deliv Rev , vol.61 , Issue.14 , pp. 1276-1282
    • Stiles, B.L.1
  • 15
    • 0036390010 scopus 로고    scopus 로고
    • Granulocyte colonystimulating factor in glycogen storage disease type 1b: Results of the European Study on Glycogen Storage Disease Type 1
    • Visser G, Rake JP, Labrune P, Leonard JV, Ullrich,K, Smit GP. Granulocyte colonystimulating factor in glycogen storage disease type 1b: results of the European Study on Glycogen Storage Disease Type 1. Eur J Pediatr. 2002; 161(suppl 1):S83-S87.
    • (2002) Eur J Pediatr , vol.161 , Issue.SUPPL. 1
    • Visser, G.1    Rake, J.P.2    Labrune, P.3    Leonard, J.V.4    Ullrich, K.5    Smit, G.P.6
  • 16
    • 0035863817 scopus 로고    scopus 로고
    • Recombinant human granulocyte colony-stimulating factor therapy for patients with neutropenia and/or neutrophil dysfunction secondary to glycogen storage disease type 1b
    • DOI 10.1182/blood.V97.2.376
    • Calderwood S, Kilpatrick L, Douglas SD, et al. Recombinant human granulocyte colonystimulating factor therapy for patients with neutropenia and/or neutrophil dysfunction secondary to glycogen storage disease type 1b. Blood. 2001; 97(2):376-382. (Pubitemid 32060320)
    • (2001) Blood , vol.97 , Issue.2 , pp. 376-382
    • Calderwood, S.1    Kilpatrick, L.2    Douglas, S.D.3    Freedman, M.4    Smith-Whitley, K.5    Rolland, M.6    Kurtzberg, J.7
  • 17
    • 77957943766 scopus 로고    scopus 로고
    • Severe congenital neutropenia due to G6PC3 deficiency with increased neutrophil CXCR4 expression and myelokathexis
    • McDermott DH, DeRavin SS, Jun HS, et al. Severe congenital neutropenia due to G6PC3 deficiency with increased neutrophil CXCR4 expression and myelokathexis. Blood. 2010;116(15): 2793-2802.
    • (2010) Blood , vol.116 , Issue.15 , pp. 2793-2802
    • McDermott, D.H.1    DeRavin, S.S.2    Jun, H.S.3
  • 18
    • 17644389497 scopus 로고    scopus 로고
    • Heterogeneous expression pattern of pro- and anti-apoptotic factors in myeloid progenitor cells of patients with severe congenital neutropenia treated with granulocyte colony-stimulating factor
    • DOI 10.1111/j.1365-2141.2005.05428.x
    • Cario G, Skokowa J, Wang Z, et al. Heterogeneous expression pattern of pro- and antiapoptotic factors in myeloid progenitor cells of patients with severe congenital neutropenia treated with granulocyte colony-stimulating factor. Br J Haematol. 2005;129(2):275-278. (Pubitemid 40562449)
    • (2005) British Journal of Haematology , vol.129 , Issue.2 , pp. 275-278
    • Cario, G.1    Skokowa, J.2    Wang, Z.3    Bucan, V.4    Zeidler, C.5    Stanulla, M.6    Schrappe, M.7    Welte, K.8
  • 19
    • 0037079734 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor inhibits the mitochondria-dependent activation of caspase-3 in neutrophils
    • DOI 10.1182/blood.V99.2.672
    • Maianski NA, Mul FP, van Buul JD, Roos D, Kuijpers TW. Granulocyte colony-stimulating factor inhibits the mitochondria-dependent activation of caspase-3 in neutrophils. Blood. 2002;99(2): 672-679. (Pubitemid 34533107)
    • (2002) Blood , vol.99 , Issue.2 , pp. 672-679
    • Maianski, N.A.1    Mul, F.P.J.2    Van Buul, J.D.3    Roos, D.4    Kuijpers, T.W.5
  • 20
    • 2442666527 scopus 로고    scopus 로고
    • Bid truncation, Bid/Bax targeting to the mitochondria, and caspase activation associated with neutrophil apoptosis are inhibited by granulocyte colony-stimulating factor
    • Maianski NA, Roos D, Kuijpers TW. Bid truncation, Bid/Bax targeting to the mitochondria, and caspase activation associated with neutrophil apoptosis are inhibited by granulocyte colonystimulating factor. J Immunol. 2004;172(11):7024-7030. (Pubitemid 38669144)
    • (2004) Journal of Immunology , vol.172 , Issue.11 , pp. 7024-7030
    • Maianski, N.A.1    Roos, D.2    Kuijpers, T.W.3
  • 21
    • 77957959873 scopus 로고    scopus 로고
    • Lack of glucose recycling between endoplasmic reticulum and cytoplasm underlies cellular dysfunction in glucose-6-phosphatase-beta-deficient neutrophils in a congenital neutropenia syndrome
    • Jun HS, Lee YM, McDermott DH, et al. Lack of glucose recycling between endoplasmic reticulum and cytoplasm underlies cellular dysfunction in glucose-6-phosphatase-beta-deficient neutrophils in a congenital neutropenia syndrome. Blood. 2010;116(15):2783-2792.
    • (2010) Blood , vol.116 , Issue.15 , pp. 2783-2792
    • Jun, H.S.1    Lee, Y.M.2    McDermott, D.H.3
  • 23
    • 33746524202 scopus 로고    scopus 로고
    • Method for monitoring of mitochondrial cytochrome c release during cell death: Immunodetection of cytochrome c by flow cytometry after selective permeabilization of the plasma membrane
    • DOI 10.1002/cyto.a.20273
    • Campos CB, Paim BA, Cosso RG, Castilho RF, Rottenberg H, Vercesi AE. Method for monitoringof mitochondrial cytochrome c release during cell death: immunodetection of cytochrome c by flow cytometry after selective permeabilization of the plasma membrane. Cytometry A. 2006;69(6):515-523. (Pubitemid 44651338)
    • (2006) Cytometry Part A , vol.69 , Issue.6 , pp. 515-523
    • Campos, C.B.L.1    Paim, B.A.2    Cosso, R.G.3    Castilho, R.F.4    Rottenberg, H.5    Vercesi, A.E.6
  • 24
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • DOI 10.1038/sj.cdd.4401373
    • Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 2004;11(4):381-389. (Pubitemid 38489416)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.4 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 25
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann MP, Pirola L. Structure and function of phosphoinositide 3-kinases. Biochim Biophys Acta. 1998;1436(1):127-150.
    • (1998) Biochim Biophys Acta , vol.1436 , Issue.1 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 27
    • 34347214070 scopus 로고    scopus 로고
    • The role of SHIP in macrophages
    • Sly LM, Ho V, Antignano F, et al. The role of SHIP in macrophages. Front Biosci. 2007;12:2836-2848.
    • (2007) Front Biosci , vol.12 , pp. 2836-2848
    • Sly, L.M.1    Ho, V.2    Antignano, F.3
  • 28
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • DOI 10.1016/j.molcel.2004.08.025, PII S1097276504005118
    • Haynes CM, Titus EA, Cooper AA. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell. 2004;15(5):767-776. (Pubitemid 39194906)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 30
    • 34347242634 scopus 로고    scopus 로고
    • Therapeutic potential of superoxide dismutase (SOD) for resolution of inflammation
    • DOI 10.1007/s00011-006-5195-y
    • Yasui K, Baba A. Therapeutic potential of superoxide dismutase (SOD) for resolution of inflammation. Inflamm Res. 2006;55(9):359-363. (Pubitemid 44825292)
    • (2006) Inflammation Research , vol.55 , Issue.9 , pp. 359-363
    • Yasui, K.1    Baba, A.2
  • 32
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT,Wolter KG, Youle RJ. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci U S A. 1997;94(8):3668-3672.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.8 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 35
    • 33645299092 scopus 로고    scopus 로고
    • Caspases at the crossroads of immunecell life and death
    • Siegel RM. Caspases at the crossroads of immunecell life and death. Nat Rev Immunol. 2006;6:308-317.
    • (2006) Nat Rev Immunol , vol.6 , pp. 308-317
    • Siegel, R.M.1
  • 36
    • 34249828162 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor and its receptor in normal myeloid cell development, leukemia and related blood cell disorders
    • DOI 10.2741/2103
    • Touw IP, van de Geijn GJ. Granulocyte colonystimulating factor and its receptor in normal myeloid cell development, leukemia and related blood cell disorders. Front Biosci. 2007;12:800-815. (Pubitemid 46846857)
    • (2007) Frontiers in Bioscience , vol.12 , Issue.3 , pp. 800-815
    • Touw, I.P.1    Van De Geijn, G.-J.M.2
  • 37
    • 0031982999 scopus 로고    scopus 로고
    • Acute regulation of glucose transport after activation of human peripheral blood neutrophils by phorbol myristate acetate, fMLP, and granulocyte-macrophage colony-stimulating factor
    • Tan AS, Ahmed N, Berridge MV. Acute regulation of glucose transport after activation of human peripheral blood neutrophils by phorbol myristate acetate, fMLP, and granulocyte-macrophage colony-stimulating factor. Blood. 1998;91(2):649-655. (Pubitemid 28053390)
    • (1998) Blood , vol.91 , Issue.2 , pp. 649-655
    • Tan, A.S.1    Ahmed, N.2    Berridge, M.V.3
  • 39
    • 0015896530 scopus 로고
    • Inhibition of glucose transport in the human erythrocyte by cytochalasin B
    • Bloch R. Inhibition of glucose transport in the human erythrocyte by cytochalasin B. Biochemistry. 1973;12(23):4799-4801.
    • (1973) Biochemistry , vol.12 , Issue.23 , pp. 4799-4801
    • Bloch, R.1
  • 40
    • 32044448517 scopus 로고    scopus 로고
    • 2-Deoxyglucose: An anticancer and antiviral therapeutic, but not any more a low glucose mimetic
    • DOI 10.1016/j.lfs.2005.07.001, PII S0024320505006983
    • Kang HT, Hwang ES. 2-Deoxyglucose: an anticancer and antiviral therapeutic, but not any more a low glucose mimetic. Life Sci. 2006;78(12): 1392-1399. (Pubitemid 43199960)
    • (2006) Life Sciences , vol.78 , Issue.12 , pp. 1392-1399
    • Kang, H.T.1    Hwang, E.S.2
  • 41
    • 33644855216 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1
    • DOI 10.1016/j.molcel.2006.02.009, PII S1097276506001110
    • Maurer U, Charvet C, Wagman AS, Dejardin E, Green DR. Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol Cell. 2006;21(6):749-760. (Pubitemid 43376126)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 749-760
    • Maurer, U.1    Charvet, C.2    Wagman, A.S.3    Dejardin, E.4    Green, D.R.5
  • 43
    • 19444374556 scopus 로고    scopus 로고
    • Mediation of cell death by poly(ADP-ribose) polymerase-1
    • DOI 10.1016/j.phrs.2005.02.011, PII S1043661805000435
    • Koh DW, Dawson TM, Dawson VL. Mediation of cell death by poly(ADP-ribose) polymerase-1. Pharmacol Res. 2005;52(5579):5-14. (Pubitemid 40725595)
    • (2005) Pharmacological Research , vol.52 , Issue.SPEC. ISS. , pp. 5-14
    • Koh, D.W.1    Dawson, T.M.2    Dawson, V.L.3
  • 44
    • 0037837858 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor signals for increased glucose transport via phosphatidylinositol 3-kinase- and hydrogen peroxide-dependent mechanisms
    • DOI 10.1074/jbc.M212541200
    • Dhar-Mascareno M, Chen J, Zhang RH, Cárcamo JM, Golde DW. Granulocyte-macrophage colonystimulating factor signals for increased glucose transport via phosphatidylinositol 3-kinase- and hydrogen peroxide-dependent mechanisms. J Biol Chem. 2003;278(13):11107-11114. (Pubitemid 36792663)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11107-11114
    • Dhar-Mascareno, M.1    Chen, J.2    Zhang, R.H.3    Carcamo, J.M.4    Golde, D.W.5
  • 45
    • 18844388999 scopus 로고    scopus 로고
    • Minireview: Hexose-6-phosphate dehydrogenase and redox control of 11β-hydroxysteroid dehydrogenase type 1 activity
    • DOI 10.1210/en.2005-0117
    • Hewitt KN, Walker EA, Stewart PM. Minireview: hexose-6-phosphate dehydrogenase and redox control of 11beta-hydroxysteroid dehydrogenase type 1 activity. Endocrinology. 2005;146(6):2539-2543. (Pubitemid 40695555)
    • (2005) Endocrinology , vol.146 , Issue.6 , pp. 2539-2543
    • Hewitt, K.N.1    Walker, E.A.2    Stewart, P.M.3


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