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Volumn 325, Issue 1, 2004, Pages 101-108

Intracellular glutathione status regulates mouse bone marrow monocyte-derived macrophage differentiation and phagocytic activity

Author keywords

Cell differentiation; GSH GSSG ratio; Macrophages; Phagocytosis; Redox state

Indexed keywords

COLONY STIMULATING FACTOR 1; COLONY STIMULATING FACTOR RECEPTOR; GLUTATHIONE; MESSENGER RNA;

EID: 7444268515     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.220     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 29 2000 222 230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 2
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • E.R. Stadtman, and B.S. Berlett Reactive oxygen-mediated protein oxidation in aging and disease Drug Metab. Rev. 30 1998 225 243
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 3
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • D.R. Green, and J.C. Reed Mitochondria and apoptosis Science 281 1998 1309 1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 4
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • G. Kroemer, B. Dallaporta, and M. Resche-Rigon The mitochondrial death/life regulator in apoptosis and necrosis Annu. Rev. Physiol. 60 1998 619 642
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 5
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • T. Finkel, and N.J. Holbrook Oxidants, oxidative stress and the biology of ageing Nature 408 2000 239 247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 6
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • E.R. Stadtman Protein oxidation and aging Science 257 1992 1220 1224
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 7
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • O. Epp, R. Ladenstein, and A. Wendel The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution Eur. J. Biochem. 133 1983 51 69
    • (1983) Eur. J. Biochem. , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 8
    • 0033543748 scopus 로고    scopus 로고
    • Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury
    • J. Bai, A.M. Rodriguez, J.A. Melendez, and A.I. Cederbaum Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury J. Biol. Chem. 274 1999 26217 26224
    • (1999) J. Biol. Chem. , vol.274 , pp. 26217-26224
    • Bai, J.1    Rodriguez, A.M.2    Melendez, J.A.3    Cederbaum, A.I.4
  • 9
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical (O2-.), superoxide dismutases, and related matters
    • I. Fridovich Superoxide anion radical (O2-.), superoxide dismutases, and related matters J. Biol. Chem. 272 1997 18515 18517
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 10
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • W.A. Prinz, F. Aslund, A. Holmgren, and J. Beckwith The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm J. Biol. Chem. 272 1997 15661 15667
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 11
    • 0030296409 scopus 로고    scopus 로고
    • S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione
    • C.H. Jung, and J.A. Thomas S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione Arch. Biochem. Biophys. 335 1996 61 72
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 61-72
    • Jung, C.H.1    Thomas, J.A.2
  • 13
    • 0035894203 scopus 로고    scopus 로고
    • Altered differentiation in rat and rabbit limb bud micromass cultures by glutathione modulating agents
    • J.M. Hansen, E.W. Carney, and C. Harris Altered differentiation in rat and rabbit limb bud micromass cultures by glutathione modulating agents Free Radic. Biol. Med. 31 2001 1582 1592
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1582-1592
    • Hansen, J.M.1    Carney, E.W.2    Harris, C.3
  • 14
    • 0031783956 scopus 로고    scopus 로고
    • Endogenous glutathione conjugates: Occurrence and biological functions
    • W. Wang, and N. Ballatori Endogenous glutathione conjugates: occurrence and biological functions Pharmacol. Rev. 50 1998 335 356
    • (1998) Pharmacol. Rev. , vol.50 , pp. 335-356
    • Wang, W.1    Ballatori, N.2
  • 15
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • S.C. Lu Regulation of hepatic glutathione synthesis: current concepts and controversies FASEB J. 13 1999 1169 1183
    • (1999) FASEB J. , vol.13 , pp. 1169-1183
    • Lu, S.C.1
  • 17
    • 0034142146 scopus 로고    scopus 로고
    • Developmental patterns of zygotes from transgenic female mice with elevated tissue glutathione
    • S.J. Rzucidlo, and B.G. Brackett Developmental patterns of zygotes from transgenic female mice with elevated tissue glutathione J. Exp. Zool. 286 2000 173 180
    • (2000) J. Exp. Zool. , vol.286 , pp. 173-180
    • Rzucidlo, S.J.1    Brackett, B.G.2
  • 18
    • 0031149804 scopus 로고    scopus 로고
    • Redox state changes in density-dependent regulation of proliferation
    • D.E. Hutter, B.G. Till, and J.J. Greene Redox state changes in density-dependent regulation of proliferation Exp. Cell Res. 232 1997 435 438
    • (1997) Exp. Cell Res. , vol.232 , pp. 435-438
    • Hutter, D.E.1    Till, B.G.2    Greene, J.J.3
  • 19
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry-glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • I.A. Cotgreave, and R.G. Gerdes Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem. Biophys. Res. Commun. 242 1998 1 9
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 20
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic. Biol. Med. 30 2001 1191 1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 21
    • 1842822873 scopus 로고    scopus 로고
    • 12-O-tetradecanoylphorbol-13-acetate may both potentiate and decrease the generation of apoptosis by the antileukemic agent arsenic trioxide in human promonocytic cells. Regulation by extracellular signal-regulated protein kinases and glutathione
    • C. Fernandez, A.M. Ramos, P. Sancho, D. Amran, E. de Blas, and P. Aller 12-O-tetradecanoylphorbol-13-acetate may both potentiate and decrease the generation of apoptosis by the antileukemic agent arsenic trioxide in human promonocytic cells. Regulation by extracellular signal-regulated protein kinases and glutathione J. Biol. Chem. 279 2004 3877 3884
    • (2004) J. Biol. Chem. , vol.279 , pp. 3877-3884
    • Fernandez, C.1    Ramos, A.M.2    Sancho, P.3    Amran, D.4    De Blas, E.5    Aller, P.6
  • 22
    • 0037147267 scopus 로고    scopus 로고
    • NADPH oxidase-dependent oxidation and externalization of phosphatidylserine during apoptosis in Me2SO-differentiated HL-60 cells. Role in phagocytic clearance
    • A. Arroyo, M. Modriansky, F.B. Serinkan, R.I. Bello, T. Matsura, J. Jiang, V.A. Tyurin, Y.Y. Tyurina, B. Fadeel, and V.E. Kagan NADPH oxidase-dependent oxidation and externalization of phosphatidylserine during apoptosis in Me2SO-differentiated HL-60 cells. Role in phagocytic clearance J. Biol. Chem. 277 2002 49965 49975
    • (2002) J. Biol. Chem. , vol.277 , pp. 49965-49975
    • Arroyo, A.1    Modriansky, M.2    Serinkan, F.B.3    Bello, R.I.4    Matsura, T.5    Jiang, J.6    Tyurin, V.A.7    Tyurina, Y.Y.8    Fadeel, B.9    Kagan, V.E.10
  • 23
    • 0031868832 scopus 로고    scopus 로고
    • Differential regulation of glutathione by oxidants and dexamethasone in alveolar epithelial cells
    • I. Rahman, A. Bel, B. Mulier, K. Donaldson, and W. MacNee Differential regulation of glutathione by oxidants and dexamethasone in alveolar epithelial cells Am. J. Physiol. 275 1998 L80 86
    • (1998) Am. J. Physiol. , vol.275
    • Rahman, I.1    Bel, A.2    Mulier, B.3    Donaldson, K.4    MacNee, W.5
  • 24
    • 0022389598 scopus 로고
    • Effects of the free radical generator paraquat on differentiation, superoxide dismutase, glutathione and inorganic peroxides in microplasmodia of Physarum polycephalum
    • R.G. Allen, R.K. Newton, K.J. Farmer, and C. Nations Effects of the free radical generator paraquat on differentiation, superoxide dismutase, glutathione and inorganic peroxides in microplasmodia of Physarum polycephalum Cell Tissue Kinet. 18 1985 623 630
    • (1985) Cell Tissue Kinet. , vol.18 , pp. 623-630
    • Allen, R.G.1    Newton, R.K.2    Farmer, K.J.3    Nations, C.4
  • 25
    • 0029098713 scopus 로고
    • Role of glutathione redox cycle in TNF-alpha-mediated endothelial cell dysfunction
    • M. Toborek, S.W. Barger, M.P. Mattson, C.J. McClain, and B. Hennig Role of glutathione redox cycle in TNF-alpha-mediated endothelial cell dysfunction Atherosclerosis 117 1995 179 188
    • (1995) Atherosclerosis , vol.117 , pp. 179-188
    • Toborek, M.1    Barger, S.W.2    Mattson, M.P.3    McClain, C.J.4    Hennig, B.5
  • 26
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • H.J. Forman, and M. Torres Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling Am. J. Respir. Crit. Care Med. 166 2002 S4 8
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166
    • Forman, H.J.1    Torres, M.2
  • 28
    • 0036681842 scopus 로고    scopus 로고
    • Stimulation by toll-like receptors inhibits osteoclast differentiation
    • M. Takami, N. Kim, J. Rho, and Y. Choi Stimulation by toll-like receptors inhibits osteoclast differentiation J. Immunol. 169 2002 1516 1523
    • (2002) J. Immunol. , vol.169 , pp. 1516-1523
    • Takami, M.1    Kim, N.2    Rho, J.3    Choi, Y.4
  • 29
    • 0036433010 scopus 로고    scopus 로고
    • Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals
    • M.W. Boehme, P. Galle, and W. Stremmel Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals Immunology 107 2002 340 349
    • (2002) Immunology , vol.107 , pp. 340-349
    • Boehme, M.W.1    Galle, P.2    Stremmel, W.3
  • 30
    • 0033213963 scopus 로고    scopus 로고
    • Fibroblast-secreted macrophage colony-stimulating factor is responsible for generation of biphenotypic B/macrophage cells from a subset of mouse B lymphocytes
    • M.A. Borrello, and R.P. Phipps Fibroblast-secreted macrophage colony-stimulating factor is responsible for generation of biphenotypic B/macrophage cells from a subset of mouse B lymphocytes J. Immunol. 163 1999 3605 3611
    • (1999) J. Immunol. , vol.163 , pp. 3605-3611
    • Borrello, M.A.1    Phipps, R.P.2
  • 32
    • 0037165648 scopus 로고    scopus 로고
    • Selenoprotein W is a glutathione-dependent antioxidant in vivo
    • D. Jeong, T.S. Kim, Y.W. Chung, B.J. Lee, and I.Y. Kim Selenoprotein W is a glutathione-dependent antioxidant in vivo FEBS Lett. 517 2002 225 228
    • (2002) FEBS Lett. , vol.517 , pp. 225-228
    • Jeong, D.1    Kim, T.S.2    Chung, Y.W.3    Lee, B.J.4    Kim, I.Y.5
  • 34
    • 0344944226 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition by selenium compounds mediated by oxidation of the protein thiol groups and generation of the superoxide
    • T.S. Kim, B.Y. Yun, and I.Y. Kim Induction of the mitochondrial permeability transition by selenium compounds mediated by oxidation of the protein thiol groups and generation of the superoxide Biochem. Pharmacol. 66 2003 2301 2311
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 2301-2311
    • Kim, T.S.1    Yun, B.Y.2    Kim, I.Y.3
  • 36
    • 0842282565 scopus 로고    scopus 로고
    • Imbalanced gp130-dependent signaling in macrophages alters macrophage colony-stimulating factor responsiveness via regulation of c-fms expression
    • B.J. Jenkins, D. Grail, M. Inglese, C. Quilici, S. Bozinovski, P. Wong, and M. Ernst Imbalanced gp130-dependent signaling in macrophages alters macrophage colony-stimulating factor responsiveness via regulation of c-fms expression Mol. Cell. Biol. 24 2004 1453 1463
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1453-1463
    • Jenkins, B.J.1    Grail, D.2    Inglese, M.3    Quilici, C.4    Bozinovski, S.5    Wong, P.6    Ernst, M.7
  • 37
    • 0020065765 scopus 로고
    • Gamma-glutamyl transpeptidase and glutathione in aging IMR-90 fibroblasts and in differentiating 3T3 L1 preadipocytes
    • S. Takahashi, and M. Zeydel Gamma-glutamyl transpeptidase and glutathione in aging IMR-90 fibroblasts and in differentiating 3T3 L1 preadipocytes Arch. Biochem. Biophys. 214 1982 260 267
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 260-267
    • Takahashi, S.1    Zeydel, M.2
  • 38
    • 0024382255 scopus 로고
    • Oxidative influence on development and differentiation: An overview of a free radical theory of development
    • R.G. Allen, and A.K. Balin Oxidative influence on development and differentiation: an overview of a free radical theory of development Free Radic. Biol. Med. 6 1989 631 661
    • (1989) Free Radic. Biol. Med. , vol.6 , pp. 631-661
    • Allen, R.G.1    Balin, A.K.2
  • 39
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinskey, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 40
    • 0032783530 scopus 로고    scopus 로고
    • Mitochondrial glutathione modulates TNF-alpha-induced endothelial cell dysfunction
    • K.H. Chen, L.M. Reece, and J.F. Leary Mitochondrial glutathione modulates TNF-alpha-induced endothelial cell dysfunction Free Radic. Biol. Med. 27 1999 100 109
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 100-109
    • Chen, K.H.1    Reece, L.M.2    Leary, J.F.3
  • 42
    • 0030765053 scopus 로고    scopus 로고
    • Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling
    • R.P. Bourette, G.M. Myles, J.L. Choi, and L.R. Rohrschneider Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling EMBO J. 16 1997 5880 5893
    • (1997) EMBO J. , vol.16 , pp. 5880-5893
    • Bourette, R.P.1    Myles, G.M.2    Choi, J.L.3    Rohrschneider, L.R.4
  • 43
    • 0032479989 scopus 로고    scopus 로고
    • PU.1 regulates both cytokine-dependent proliferation and differentiation of granulocyte/macrophage progenitors
    • R.P. DeKoter, J.C. Walsh, and H. Singh PU.1 regulates both cytokine-dependent proliferation and differentiation of granulocyte/macrophage progenitors EMBO J. 17 1998 4456 4468
    • (1998) EMBO J. , vol.17 , pp. 4456-4468
    • Dekoter, R.P.1    Walsh, J.C.2    Singh, H.3
  • 44
    • 0029119989 scopus 로고
    • Growth hormone and colony-stimulating factor 1 share multiple response elements in the c-fos promoter
    • C. Chen, R.W. Clarkson, Y. Xie, D.A. Hume, and M.J. Waters Growth hormone and colony-stimulating factor 1 share multiple response elements in the c-fos promoter Endocrinology 136 1995 4505 4516
    • (1995) Endocrinology , vol.136 , pp. 4505-4516
    • Chen, C.1    Clarkson, R.W.2    Xie, Y.3    Hume, D.A.4    Waters, M.J.5
  • 47
    • 0029948821 scopus 로고    scopus 로고
    • IL-3, GM-CSF and CSF-1 modulate c-fms mRNA more rapidly in human early monocytic progenitors than in mature or transformed monocytic cells
    • B. Panterne, A. Hatzfeld, P. Sansilvestri, A. Cardoso, M.N. Monier, P. Batard, and J. Hatzfeld IL-3, GM-CSF and CSF-1 modulate c-fms mRNA more rapidly in human early monocytic progenitors than in mature or transformed monocytic cells J. Cell Sci. 109 Pt. 7 1996 1795 1801
    • (1996) J. Cell Sci. , vol.109 , Issue.7 , pp. 1795-1801
    • Panterne, B.1    Hatzfeld, A.2    Sansilvestri, P.3    Cardoso, A.4    Monier, M.N.5    Batard, P.6    Hatzfeld, J.7


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