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Volumn 47, Issue 9, 2013, Pages 699-709

Effective NET formation in neutrophils from individuals with G6PD Taiwan-Hakka is associated with enhanced NADP+ biosynthesis

Author keywords

Glucose 6 phosphate dehydrogenase deficiency; NET; NETosis; Neutrophil; Reactive oxygen species

Indexed keywords

3 METHYLADENINE; DIPHENYLIODONIUM SALT; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUCOSE OXIDASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE KINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NICOTINAMIDE NUCLEOTIDE; PHORBOL 13 ACETATE 12 MYRISTATE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; XANTHINE OXIDASE; 3-METHYLADENINE; ADENINE; CATION;

EID: 84882430829     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2013.816420     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan C. Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006; 6: 173-182.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 4
    • 70350029796 scopus 로고    scopus 로고
    • NETs: A new strategy for using old weapons
    • Papayannopoulos V, Zychlinsky A. NETs: a new strategy for using old weapons. Trends Immunol 2009; 30: 513-521.
    • (2009) Trends Immunol , vol.30 , pp. 513-521
    • Papayannopoulos, V.1    Zychlinsky, A.2
  • 7
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • Urban CF, Reichard U, Brinkmann V, Zychlinsky A. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell Microbiol 2006; 8: 668-676.
    • (2006) Cell Microbiol , vol.8 , pp. 668-676
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3    Zychlinsky, A.4
  • 8
    • 34447525439 scopus 로고    scopus 로고
    • Benefi cial suicide: Why neutrophils die to make NETs
    • Brinkmann V, Zychlinsky A. Benefi cial suicide: Why neutrophils die to make NETs. Nat Rev Microbiol 2007; 5: 577-582.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 577-582
    • Brinkmann, V.1    Zychlinsky, A.2
  • 10
    • 32944465559 scopus 로고    scopus 로고
    • DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps
    • Buchanan JT, Simpson AJ, Aziz RK, Liu GY, Kristian SA, Kotb M, et al. DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps. Curr Biol 2006; 16: 396-400.
    • (2006) Curr Biol , vol.16 , pp. 396-400
    • Buchanan, J.T.1    Simpson, A.J.2    Aziz, R.K.3    Liu, G.Y.4    Kristian, S.A.5    Kotb, M.6
  • 11
    • 33645234855 scopus 로고    scopus 로고
    • Induction of neutrophil extracellular DNA lattices by placental microparticles and IL-8 and their presence in preeclampsia
    • Gupta AK, Hasler P, Holzgreve W, Gebhardt S, Hahn S. Induction of neutrophil extracellular DNA lattices by placental microparticles and IL-8 and their presence in preeclampsia. Hum Immunol 2005; 66: 1146-1154.
    • (2005) Hum Immunol , vol.66 , pp. 1146-1154
    • Gupta, A.K.1    Hasler, P.2    Holzgreve, W.3    Gebhardt, S.4    Hahn, S.5
  • 13
    • 51349135381 scopus 로고    scopus 로고
    • Catapult-like release of mitochondrial DNA by eosinophils contributes to antibacterial defense
    • Yousefi S, Gold JA, Andina N, Lee JJ, Kelly AM, Kozlowski E, et al. Catapult-like release of mitochondrial DNA by eosinophils contributes to antibacterial defense. Nat Med 2008; 14: 949-953.
    • (2008) Nat Med , vol.14 , pp. 949-953
    • Yousefi, S.1    Gold, J.A.2    Andina, N.3    Lee, J.J.4    Kelly, A.M.5    Kozlowski, E.6
  • 15
    • 77956426154 scopus 로고    scopus 로고
    • CXCR2 mediates NADPH oxidase-independent neutrophil extracellular trap formation in cystic fi brosis airway infl ammation
    • Marcos V, Zhou Z, Yildirim AO, Bohla A, Hector A, Vitkov L, et al. CXCR2 mediates NADPH oxidase-independent neutrophil extracellular trap formation in cystic fi brosis airway infl ammation. Nat Med 2010; 16: 1018-1023.
    • (2010) Nat Med , vol.16 , pp. 1018-1023
    • Marcos, V.1    Zhou, Z.2    Yildirim, A.O.3    Bohla, A.4    Hector, A.5    Vitkov, L.6
  • 20
    • 67650638848 scopus 로고    scopus 로고
    • Impaired neutrophil extracellular trap (NET) formation: A novel innate immune defi ciency of human neonates
    • Yost CC, Cody MJ, Harris ES, Thornton NL, McInturff AM, Martinez ML, et al. Impaired neutrophil extracellular trap (NET) formation: A novel innate immune defi ciency of human neonates. Blood 2009; 113: 6419-6427.
    • (2009) Blood , vol.113 , pp. 6419-6427
    • Yost, C.C.1    Cody, M.J.2    Harris, E.S.3    Thornton, N.L.4    McInturff, A.M.5    Martinez, M.L.6
  • 22
    • 1242293627 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-defi cient cells show an increased propensity for oxidant-induced senescence
    • Cheng ML, Ho HY, Wu YH, Chiu DT. Glucose-6-phosphate dehydrogenase-defi cient cells show an increased propensity for oxidant-induced senescence. Free Radic Biol Med 2004; 36: 580-591.
    • (2004) Free Radic Biol Med , vol.36 , pp. 580-591
    • Cheng, M.L.1    Ho, H.Y.2    Wu, Y.H.3    Chiu, D.T.4
  • 23
    • 34547105052 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-from oxidative stress to cellular functions and degenerative diseases
    • Ho HY, Cheng ML, Chiu DT. Glucose-6-phosphate dehydrogenase-from oxidative stress to cellular functions and degenerative diseases. Redox Report 2007; 12: 109-118.
    • (2007) Redox Report , vol.12 , pp. 109-118
    • Ho, H.Y.1    Cheng, M.L.2    Chiu, D.T.3
  • 24
    • 67650726503 scopus 로고    scopus 로고
    • Ineff ective GSH regeneration enhances G6PD-knockdown Hep G2 cell sensitivity to diamide-induced oxidative damage
    • Gao LP, Cheng ML, Chou HJ, Yang YH, Ho HY, Chiu DT. Ineff ective GSH regeneration enhances G6PD-knockdown Hep G2 cell sensitivity to diamide-induced oxidative damage. Free Radic Biol Med 2009; 47: 529-535.
    • (2009) Free Radic Biol Med , vol.47 , pp. 529-535
    • Gao, L.P.1    Cheng, M.L.2    Chou, H.J.3    Yang, Y.H.4    Ho, H.Y.5    Chiu, D.T.6
  • 25
    • 0034705709 scopus 로고    scopus 로고
    • Cellular glucose-6-phosphate dehydrogenase (G6PD) status modulates the eff ects of nitric oxide (NO) on human foreskin fi broblasts
    • Cheng ML, Ho HY, Liang CM, Chou YH, Stern A, Lu FJ, Chiu DT. Cellular glucose-6-phosphate dehydrogenase (G6PD) status modulates the eff ects of nitric oxide (NO) on human foreskin fi broblasts. FEBS Lett 2000; 475: 257-262.
    • (2000) FEBS Lett , vol.475 , pp. 257-262
    • Cheng, M.L.1    Ho, H.Y.2    Liang, C.M.3    Chou, Y.H.4    Stern, A.5    Lu, F.J.6    Chiu, D.T.7
  • 26
    • 77954142727 scopus 로고    scopus 로고
    • Impaired dephosphorylation renders G6PD-knockdown HepG2 cells more susceptible to H(2)O(2)-induced apoptosis
    • Lin CJ, Ho HY, Cheng ML, You TH, Yu JS, Chiu DT. Impaired dephosphorylation renders G6PD-knockdown HepG2 cells more susceptible to H(2)O(2)-induced apoptosis. Free Radic Biol Med 2010; 49: 361-373.
    • (2010) Free Radic Biol Med , vol.49 , pp. 361-373
    • Lin, C.J.1    Ho, H.Y.2    Cheng, M.L.3    You, T.H.4    Yu, J.S.5    Chiu, D.T.6
  • 27
    • 0015322180 scopus 로고
    • Complete defi ciency of leukocyte glucose- 6-phosphate dehydrogenase with defective bactericidal activity
    • Cooper MR, DeChatelet LR, McCall CE, LaVia MF, Spurr CL, Baehner RL. Complete defi ciency of leukocyte glucose- 6-phosphate dehydrogenase with defective bactericidal activity. J Clin Invest 1972; 51: 769-778.
    • (1972) J Clin Invest , vol.51 , pp. 769-778
    • Cooper, M.R.1    Dechatelet, L.R.2    McCall, C.E.3    Lavia, M.F.4    Spurr, C.L.5    Baehner, R.L.6
  • 28
    • 0016178453 scopus 로고
    • Single-step separation of red blood cells. Granulocytes and mononuclear leukocytes on discontinuous density gradients of Ficoll-Hypaque
    • English D, Andersen BR. Single-step separation of red blood cells. Granulocytes and mononuclear leukocytes on discontinuous density gradients of Ficoll-Hypaque. J Immunol Methods 1974; 5: 249-252.
    • (1974) J Immunol Methods , vol.5 , pp. 249-252
    • English, D.1    Andersen, B.R.2
  • 29
    • 0037100438 scopus 로고    scopus 로고
    • Inhibition of the spontaneous apoptosis of neutrophil granulocytes by the intracellular parasite Leishmania major
    • Aga E, Katschinski DM, van Zandbergen G, Laufs H, Hansen B, Muller K, et al. Inhibition of the spontaneous apoptosis of neutrophil granulocytes by the intracellular parasite Leishmania major. J Immunol 2002; 169: 898-905.
    • (2002) J Immunol , vol.169 , pp. 898-905
    • Aga, E.1    Katschinski, D.M.2    Van Zandbergen, G.3    Laufs, H.4    Hansen, B.5    Muller, K.6
  • 30
    • 0030031242 scopus 로고    scopus 로고
    • Neonatal jaundice and molecular mutations in glucose-6- phosphate dehydrogenase defi cient newborn infants
    • Huang CS, Hung KL, Huang MJ, Li YC, Liu TH, Tang TK. Neonatal jaundice and molecular mutations in glucose-6- phosphate dehydrogenase defi cient newborn infants. Am J Hematol 1996; 51: 19-25.
    • (1996) Am J Hematol , vol.51 , pp. 19-25
    • Huang, C.S.1    Hung, K.L.2    Huang, M.J.3    Li, Y.C.4    Liu, T.H.5    Tang, T.K.6
  • 31
    • 84870708754 scopus 로고    scopus 로고
    • Characterization of global metabolic responses of glucose-6-phosphate dehydrogenase- defi cient hepatoma cells to diamide-induced oxidative stress
    • Ho HY, Cheng ML, Shiao MS, Chiu DT. Characterization of global metabolic responses of glucose-6-phosphate dehydrogenase- defi cient hepatoma cells to diamide-induced oxidative stress. Free Radic Biol Med 2013; 54: 71-84.
    • (2013) Free Radic Biol Med , vol.54 , pp. 71-84
    • Ho, H.Y.1    Cheng, M.L.2    Shiao, M.S.3    Chiu, D.T.4
  • 32
    • 36348971843 scopus 로고    scopus 로고
    • NAD kinase levels control the NADPH concentration in human cells
    • Pollak N, Niere M, Ziegler M. NAD kinase levels control the NADPH concentration in human cells. J Biol Chem 2007; 282: 33562-33571.
    • (2007) J Biol Chem , vol.282 , pp. 33562-33571
    • Pollak, N.1    Niere, M.2    Ziegler, M.3
  • 33
    • 52649112129 scopus 로고    scopus 로고
    • Isolation and functional analysis of neutrophils
    • Chapter 7:Unit 7.23
    • Clark RA, Nauseef WM. Isolation and functional analysis of neutrophils. Curr Protoc Immunol 2001; Chapter 7:Unit 7.23.
    • (2001) Curr Protoc Immunol
    • Clark, R.A.1    Nauseef, W.M.2
  • 34
    • 60749108379 scopus 로고    scopus 로고
    • Regulation of autophagy by reactive oxygen species (ROS): Implications for cancer progression and treatment
    • Azad MB, Chen Y, Gibson SB. Regulation of autophagy by reactive oxygen species (ROS): implications for cancer progression and treatment. Antioxid Redox Signal 2009; 11: 777-790.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 777-790
    • Azad, M.B.1    Chen, Y.2    Gibson, S.B.3
  • 35
    • 78650890352 scopus 로고    scopus 로고
    • Regulation of autophagy by ROS: Physiology and pathology
    • Scherz-Shouval R, Elazar Z. Regulation of autophagy by ROS: physiology and pathology. Trends Biochem Sci 2011; 36: 30-38.
    • (2011) Trends Biochem Sci , vol.36 , pp. 30-38
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 36
    • 63849206740 scopus 로고    scopus 로고
    • NADPH oxidase activity in the crossroad of neutrophil life and death
    • Arruda MA, Barja-Fidalgo C. NADPH oxidase activity: In the crossroad of neutrophil life and death. Front Biosci 2009; 14: 4546-4556.
    • (2009) Front Biosci , vol.14 , pp. 4546-4556
    • Arruda, M.A.1    Barja-Fidalgo, C.2
  • 38
    • 79961127300 scopus 로고    scopus 로고
    • Reactive oxygen species as signaling molecules in neutrophil chemotaxis
    • Hattori H, Subramanian KK, Sakai J, Luo HR. Reactive oxygen species as signaling molecules in neutrophil chemotaxis. Commun Integr Biol 2010; 3: 278-281.
    • (2010) Commun Integr Biol , vol.3 , pp. 278-281
    • Hattori, H.1    Subramanian, K.K.2    Sakai, J.3    Luo, H.R.4
  • 39
    • 84861452914 scopus 로고    scopus 로고
    • A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress
    • de la Vega L, Grishina I, Moreno R, Kruger M, Braun T, Schmitz ML. A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress. Mol Cell 2012; 46: 472-483.
    • (2012) Mol Cell , vol.46 , pp. 472-483
    • De La Vega, L.1    Grishina, I.2    Moreno, R.3    Kruger, M.4    Braun, T.5    Schmitz, M.L.6
  • 40
    • 79956158509 scopus 로고    scopus 로고
    • Disruption of pyridine nucleotide redox status during oxidative challenge at normal and low-glucose states: Implications for cellular adenosine triphosphate, mitochondrial respiratory activity, and reducing capacity in colon epithelial cells
    • Circu ML, Maloney RE, Aw TY. Disruption of pyridine nucleotide redox status during oxidative challenge at normal and low-glucose states: implications for cellular adenosine triphosphate, mitochondrial respiratory activity, and reducing capacity in colon epithelial cells. Antioxid Redox Signal 2011; 14: 2151-2162.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2151-2162
    • Circu, M.L.1    Maloney, R.E.2    Aw, T.Y.3
  • 41
    • 0027468461 scopus 로고
    • Molecular characterization of glucose-6-phosphate dehydrogenase (G6PD) defi ciency in patients of Chinese descent and identifi cation of new base substitutions in the human G6PD gene
    • Chiu DT, Zuo L, Chao L, Chen E, Louie E, Lubin B, et al. Molecular characterization of glucose-6-phosphate dehydrogenase (G6PD) defi ciency in patients of Chinese descent and identifi cation of new base substitutions in the human G6PD gene. Blood 1993; 81: 2150-2154.
    • (1993) Blood , vol.81 , pp. 2150-2154
    • Chiu, D.T.1    Zuo, L.2    Chao, L.3    Chen, E.4    Louie, E.5    Lubin, B.6
  • 42
    • 0030708939 scopus 로고    scopus 로고
    • Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
    • Carr AC, Winterbourn CC. Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem J 1997; 327: 275-281.
    • (1997) Biochem J , vol.327 , pp. 275-281
    • Carr, A.C.1    Winterbourn, C.C.2
  • 43
    • 0033230360 scopus 로고    scopus 로고
    • Molecular basis and enzymatic properties of glucose 6-phosphate dehydrogenase volendam, leading to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections
    • Roos D, van Zwieten R, Wijnen JT, Gomez-Gallego F, de Boer M, Stevens D, et al. Molecular basis and enzymatic properties of glucose 6-phosphate dehydrogenase volendam, leading to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections. Blood 1999; 94: 2955-2962.
    • (1999) Blood , vol.94 , pp. 2955-2962
    • Roos, D.1    Van Zwieten, R.2    Wijnen, J.T.3    Gomez-Gallego, F.4    De Boer, M.5    Stevens, D.6
  • 44
    • 0036682976 scopus 로고    scopus 로고
    • Deletion of leucine 61 in glucose-6-phosphate dehydrogenase leads to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections
    • van Bruggen R, Bautista JM, Petropoulou T, de Boer M, van Zwieten R, Gomez-Gallego F, et al. Deletion of leucine 61 in glucose-6-phosphate dehydrogenase leads to chronic nonspherocytic anemia, granulocyte dysfunction, and increased susceptibility to infections. Blood 2002; 100: 1026-1030.
    • (2002) Blood , vol.100 , pp. 1026-1030
    • Van Bruggen, R.1    Bautista, J.M.2    Petropoulou, T.3    De Boer, M.4    Van Zwieten, R.5    Gomez-Gallego, F.6
  • 45
    • 1342281277 scopus 로고    scopus 로고
    • Association of glucose-6-phosphate dehydrogenase defi ciency and X-linked chronic granulomatous disease in a child with anemia and recurrent infections
    • Agudelo-Florez P, Costa-Carvalho BT, Lopez JA, Redher J, Newburger PE, Olalla-Saad ST, Condino-Neto A. Association of glucose-6-phosphate dehydrogenase defi ciency and X-linked chronic granulomatous disease in a child with anemia and recurrent infections. Am J Hematol 2004; 75: 151-156.
    • (2004) Am J Hematol , vol.75 , pp. 151-156
    • Agudelo-Florez, P.1    Costa-Carvalho, B.T.2    Lopez, J.A.3    Redher, J.4    Newburger, P.E.5    Olalla-Saad, S.T.6    Condino-Neto, A.7
  • 46
    • 0030904022 scopus 로고    scopus 로고
    • Eff ect of glucose- 6-phosphate dehydrogenase defi ciency on neutrophil function
    • Ardati KO, Bajakian KM, Tabbara KS. Eff ect of glucose- 6-phosphate dehydrogenase defi ciency on neutrophil function. Acta Haematol 1997; 97: 211-215.
    • (1997) Acta Haematol , vol.97 , pp. 211-215
    • Ardati, K.O.1    Bajakian, K.M.2    Tabbara, K.S.3
  • 47
    • 1942533637 scopus 로고    scopus 로고
    • Diurnal fl uctuation of leukocyte G6PD activity. A possible explanation for the normal neutrophil bactericidal activity and the low incidence of pyogenic infections in patients with severe G6PD defi ciency in Israel
    • Wolach B, Ashkenazi M, Grossmann R, Gavrieli R, Friedman Z, Bashan N, Roos D. Diurnal fl uctuation of leukocyte G6PD activity. A possible explanation for the normal neutrophil bactericidal activity and the low incidence of pyogenic infections in patients with severe G6PD defi ciency in Israel. Pediatr Res 2004; 55: 807-813.
    • (2004) Pediatr Res , vol.55 , pp. 807-813
    • Wolach, B.1    Ashkenazi, M.2    Grossmann, R.3    Gavrieli, R.4    Friedman, Z.5    Bashan, N.6    Roos, D.7
  • 48
    • 0032468361 scopus 로고    scopus 로고
    • Bactericidal activity of polymorphonuclear neutrophils in individuals severely defi cient in glucose-6-phosphate dehydrogenase
    • Asghar AH, Ardati KO, Tabbara KS, Bajakian KM. Bactericidal activity of polymorphonuclear neutrophils in individuals severely defi cient in glucose-6-phosphate dehydrogenase. Ann Saudi Med 1998; 18: 363-365.
    • (1998) Ann Saudi Med , vol.18 , pp. 363-365
    • Asghar, A.H.1    Ardati, K.O.2    Tabbara, K.S.3    Bajakian, K.M.4


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