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Volumn 117, Issue 3, 2007, Pages 784-793

Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase-β

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE 6 PHOSPHATASE; GLUCOSE 6 PHOSPHATASE BETA; UNCLASSIFIED DRUG;

EID: 33847420515     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI30443     Document Type: Article
Times cited : (100)

References (50)
  • 1
    • 0036086034 scopus 로고    scopus 로고
    • Type I glycogen storage diseases: Disorders of the glucose-6-phosphatase complex
    • Chou, J.Y., Matern, D., Mansfield, B.C., and Chen, Y.T. 2002. Type I glycogen storage diseases: disorders of the glucose-6-phosphatase complex. Curr. Mol. Med. 2:121-143.
    • (2002) Curr. Mol. Med , vol.2 , pp. 121-143
    • Chou, J.Y.1    Matern, D.2    Mansfield, B.C.3    Chen, Y.T.4
  • 2
    • 32444436610 scopus 로고    scopus 로고
    • Glucose-6-phosphate transporter: The key to glycogen storage disease type Ib
    • S. Broer and C.A. Wagner, editors. Springer. New York, New York, USA
    • Chou, J.Y., and Mansfield, B.C. 2003. Glucose-6-phosphate transporter: the key to glycogen storage disease type Ib. In Membrane transporter diseases. S. Broer and C.A. Wagner, editors. Springer. New York, New York, USA. 191-205.
    • (2003) Membrane transporter diseases , pp. 191-205
    • Chou, J.Y.1    Mansfield, B.C.2
  • 3
    • 0019195556 scopus 로고
    • Neutropenia and impaired neutrophil migration in type 1B glycogen storage disease
    • Beaudet, A.L., Anderson, D.C., Michels, V.V., Arion, W.J., and Lange, A.J. 1980. Neutropenia and impaired neutrophil migration in type 1B glycogen storage disease. J. Pediatr. 97:906-910.
    • (1980) J. Pediatr , vol.97 , pp. 906-910
    • Beaudet, A.L.1    Anderson, D.C.2    Michels, V.V.3    Arion, W.J.4    Lange, A.J.5
  • 4
    • 0027212015 scopus 로고
    • Defective neutrophil and monocyte functions in glycogen storage disease type 1b: A literature review
    • Gitzelmann, R., and Bosshard, N.U. 1993. Defective neutrophil and monocyte functions in glycogen storage disease type 1b: a literature review. Eur. J. Pediatr. 152(Suppl.):S33-S38.
    • (1993) Eur. J. Pediatr , vol.152 , Issue.SUPPL.
    • Gitzelmann, R.1    Bosshard, N.U.2
  • 5
    • 0036694924 scopus 로고    scopus 로고
    • Rothbaum, R., et al. 2002. Shwachman-Diamond syndrome: report from an international conference. J. Pediatr. 141:266-270.
    • Rothbaum, R., et al. 2002. Shwachman-Diamond syndrome: report from an international conference. J. Pediatr. 141:266-270.
  • 8
    • 29244442582 scopus 로고    scopus 로고
    • Congenital neutropenias
    • Zeidler, C. 2005. Congenital neutropenias. Hematology. 10 (Suppl. 1):306-311.
    • (2005) Hematology , vol.10 , Issue.SUPPL. 1 , pp. 306-311
    • Zeidler, C.1
  • 10
    • 0033553477 scopus 로고    scopus 로고
    • Transmembrane topology of human glucose-6-phosphate transporter
    • Pan, C.J., Lin, B., and Chou, J.Y. 1999. Transmembrane topology of human glucose-6-phosphate transporter. J. Biol. Chem. 274:13865-13869.
    • (1999) J. Biol. Chem , vol.274 , pp. 13865-13869
    • Pan, C.J.1    Lin, B.2    Chou, J.Y.3
  • 11
    • 0030063963 scopus 로고    scopus 로고
    • Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type 1a mouse
    • Lei, K.J., et al. 1996. Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type 1a mouse. Nat. Genet. 13:203-209.
    • (1996) Nat. Genet , vol.13 , pp. 203-209
    • Lei, K.J.1
  • 12
    • 0033605362 scopus 로고    scopus 로고
    • Inactivation of the glucose-6-phosphate transporter causes glycogen storage disease type 1b
    • Hiraiwa, H., Pan, C.-J., Lin, B., Moses, S.W., and Chou, J.Y. 1999. Inactivation of the glucose-6-phosphate transporter causes glycogen storage disease type 1b. J. Biol. Chem. 274:5532-5536.
    • (1999) J. Biol. Chem , vol.274 , pp. 5532-5536
    • Hiraiwa, H.1    Pan, C.-J.2    Lin, B.3    Moses, S.W.4    Chou, J.Y.5
  • 13
    • 0000102915 scopus 로고
    • Multifunctional glucose-6-phosphatase: A critical review
    • 2nd Edition. A.N. Martonosi, editor. Springer. New York, New York, USA
    • Nordlie, R.C., and Sukalski, K.A. 1985. Multifunctional glucose-6-phosphatase: a critical review. In The enzymes of biological membranes. 2nd Edition. A.N. Martonosi, editor. Springer. New York, New York, USA. 349-398.
    • (1985) The enzymes of biological membranes , pp. 349-398
    • Nordlie, R.C.1    Sukalski, K.A.2
  • 15
    • 0033610792 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs encoding a candidate glycogen storage disease type 1b protein in rodents
    • Lin, B., Annabi, B., Hiraiwa, H., Pan, C.J., and Chou, J.Y. 1998. Cloning and characterization of cDNAs encoding a candidate glycogen storage disease type 1b protein in rodents. J. Biol. Chem. 273:31656-31670.
    • (1998) J. Biol. Chem , vol.273 , pp. 31656-31670
    • Lin, B.1    Annabi, B.2    Hiraiwa, H.3    Pan, C.J.4    Chou, J.Y.5
  • 16
    • 0142102538 scopus 로고    scopus 로고
    • Identification and characterization of a new human glucose-6-phosphatase isoform
    • Guionie, O., Clottes, E., Stafford, K., and Burchell, A. 2003. Identification and characterization of a new human glucose-6-phosphatase isoform. FEBS Lett. 551:159-164.
    • (2003) FEBS Lett , vol.551 , pp. 159-164
    • Guionie, O.1    Clottes, E.2    Stafford, K.3    Burchell, A.4
  • 17
    • 0345306587 scopus 로고    scopus 로고
    • Glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain age-dependent resolution of hypoglycemia in glycogen storage disease type Ia
    • Shieh, J.J., Pan, C.J., Mansfield, B.C., and Chou, J.Y. 2003. Glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain age-dependent resolution of hypoglycemia in glycogen storage disease type Ia. J. Biol. Chem. 278:47098-47103.
    • (2003) J. Biol. Chem , vol.278 , pp. 47098-47103
    • Shieh, J.J.1    Pan, C.J.2    Mansfield, B.C.3    Chou, J.Y.4
  • 18
    • 1842582072 scopus 로고    scopus 로고
    • Histidine-167 is the phosphate acceptor in glucose-6-phosphatase-β forming a phosphohistidine-enzyme intermediate during catalysis
    • Ghosh, A., Shieh, J.J., Pan, C.J., and Chou, J.Y. 2004. Histidine-167 is the phosphate acceptor in glucose-6-phosphatase-β forming a phosphohistidine-enzyme intermediate during catalysis. J. Biol. Chem. 279:12479-12483.
    • (2004) J. Biol. Chem , vol.279 , pp. 12479-12483
    • Ghosh, A.1    Shieh, J.J.2    Pan, C.J.3    Chou, J.Y.4
  • 19
    • 0037031827 scopus 로고    scopus 로고
    • The catalytic center of glucose-6-phosphatase: His176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis
    • Ghosh, A., et al. 2002. The catalytic center of glucose-6-phosphatase: His176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis. J. Biol. Chem. 277:32837-32842.
    • (2002) J. Biol. Chem , vol.277 , pp. 32837-32842
    • Ghosh, A.1
  • 20
    • 0000437518 scopus 로고    scopus 로고
    • Folding of secretory and membrane proteins
    • Kuznetsov, G., and Nigam, S.K. 1998. Folding of secretory and membrane proteins. N. Engl. J. Med. 339:1688-1695.
    • (1998) N. Engl. J. Med , vol.339 , pp. 1688-1695
    • Kuznetsov, G.1    Nigam, S.K.2
  • 21
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A.S. 2001. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26:504-510.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 22
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B., and Braakman, I. 2004. Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16:343-349.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 23
    • 33644858343 scopus 로고    scopus 로고
    • The unfolded protein response: A stress signaling pathway critical for health and disease
    • Zhang, K., and Kaufman, R.J. 2006. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology. 66(Suppl. 1):S102-S109.
    • (2006) Neurology , vol.66 , Issue.SUPPL. 1
    • Zhang, K.1    Kaufman, R.J.2
  • 24
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz, V.L.J., Crawford, C.E., Jackson, P.K., Bronson, R.T., and Mulligan, R.C. 1991. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell. 65:1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.J.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 25
    • 0005050988 scopus 로고    scopus 로고
    • The anatomy and physiology of hematopoiesis
    • 5th edition. D.G. Nathon and S.H. Orkin, editors. W.B. Saunders. Philadelphia, Pennsylvania, USA
    • Sieff, C.A., Nathan, D.G., and Clark, S.C. 1998. The anatomy and physiology of hematopoiesis. In Hematology of infancy and childhood. Volume 1. 5th edition. D.G. Nathon and S.H. Orkin, editors. W.B. Saunders. Philadelphia, Pennsylvania, USA. 161-236.
    • (1998) Hematology of infancy and childhood , vol.1 , pp. 161-236
    • Sieff, C.A.1    Nathan, D.G.2    Clark, S.C.3
  • 26
    • 10744222849 scopus 로고    scopus 로고
    • Impaired glucose homeostasis, neutrophil trafficking and function in mice lacking the glucose-6-phosphate transporter
    • Chen, L.Y., et al. 2003. Impaired glucose homeostasis, neutrophil trafficking and function in mice lacking the glucose-6-phosphate transporter. Hum. Mol. Genet. 12:2547-2558.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 2547-2558
    • Chen, L.Y.1
  • 27
    • 0028921518 scopus 로고
    • Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation
    • Borregaard, N., Sehested, M., Nielsen, B.S., Sengelov, H., and Kjeldsen, L. 1995. Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation. Blood. 85:812-817.
    • (1995) Blood , vol.85 , pp. 812-817
    • Borregaard, N.1    Sehested, M.2    Nielsen, B.S.3    Sengelov, H.4    Kjeldsen, L.5
  • 28
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretary vesicles in inflammation
    • Faurschou, M., and Borregaard, N. 2003. Neutrophil granules and secretary vesicles in inflammation. Microbes Infect. 5:1317-1327.
    • (2003) Microbes Infect , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 29
    • 0026072892 scopus 로고
    • Characterization and regulation of RB6-8C5 antigen expression on murine bone marrow cells
    • Hestdal, K.K., et al. 1991. Characterization and regulation of RB6-8C5 antigen expression on murine bone marrow cells. J. Immunol. 147:22-28.
    • (1991) J. Immunol , vol.147 , pp. 22-28
    • Hestdal, K.K.1
  • 30
    • 0027272534 scopus 로고
    • Selective expression of Ly-6G on myeloid lineage cells in mouse bone marrow. RB6-8C5 mAb to granulocyte-differentiation antigen (Gr-1) detects members of the Ly-6 family
    • Fleming, T.J., Fleming, M.L., and Malek, T.R. 1993. Selective expression of Ly-6G on myeloid lineage cells in mouse bone marrow. RB6-8C5 mAb to granulocyte-differentiation antigen (Gr-1) detects members of the Ly-6 family. J. Immunol. 151:2399-2408.
    • (1993) J. Immunol , vol.151 , pp. 2399-2408
    • Fleming, T.J.1    Fleming, M.L.2    Malek, T.R.3
  • 32
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • doi:10.1172/JCI26373
    • Xu, C., Bailly-Maitre, B., and Reed, J.C. 2005. Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Invest. 115:2656-2664. doi:10.1172/JCI26373.
    • (2005) J. Clin. Invest , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 33
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M., and Kaufman, R.J. 2005. The mammalian unfolded protein response. Annu. Rev. Biochem. 74:739-789.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 34
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • Vance, J.E., and Steenbergen, R. 2005. Metabolism and functions of phosphatidylserine. Prog. Lipid Res. 44:207-234.
    • (2005) Prog. Lipid Res , vol.44 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 35
    • 26444560960 scopus 로고    scopus 로고
    • Caspases: Pharmacological manipulation of cell death
    • doi:10.1172/JCI26252
    • Lavrik, I.N., Golks, A., and Krammer, P.H. 2005. Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115:2665-2672. doi:10.1172/JCI26252.
    • (2005) J. Clin. Invest , vol.115 , pp. 2665-2672
    • Lavrik, I.N.1    Golks, A.2    Krammer, P.H.3
  • 36
    • 33645299092 scopus 로고    scopus 로고
    • Caspases at the crossroads of immune-cell life and death
    • Siegel, R.M. 2006. Caspases at the crossroads of immune-cell life and death. Nat. Rev. Immunol. 6:308-317.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 308-317
    • Siegel, R.M.1
  • 37
    • 0142218366 scopus 로고    scopus 로고
    • Regulation of transbilayer plasma membrane phospholipid asymmetry
    • Daleke, D.L. 2003. Regulation of transbilayer plasma membrane phospholipid asymmetry. J. Lipid Res. 44:233-242.
    • (2003) J. Lipid Res , vol.44 , pp. 233-242
    • Daleke, D.L.1
  • 38
    • 2342436237 scopus 로고    scopus 로고
    • Recent advances in the imaging of programmed cell death
    • Blankenberg, F.G. 2004. Recent advances in the imaging of programmed cell death. Curr. Pharm. Des. 10:1457-1467.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 1457-1467
    • Blankenberg, F.G.1
  • 39
    • 33749382320 scopus 로고    scopus 로고
    • Bone-marrow derived cells require a functional glucose-6-phosphate transporter for normal myeloid functions
    • Kim, S.Y., et al. 2006. Bone-marrow derived cells require a functional glucose-6-phosphate transporter for normal myeloid functions. J. Biol. Chem. 281:28794-28801.
    • (2006) J. Biol. Chem , vol.281 , pp. 28794-28801
    • Kim, S.Y.1
  • 40
    • 0030777698 scopus 로고    scopus 로고
    • Silva, A.J., et al. 1997. Mutant mice and neuroscience: recommendations concerning genetic background. Banbury Conference on Genetic Background in Mice. Neuron. 19:755-759.
    • Silva, A.J., et al. 1997. Mutant mice and neuroscience: recommendations concerning genetic background. Banbury Conference on Genetic Background in Mice. Neuron. 19:755-759.
  • 41
    • 0036642255 scopus 로고    scopus 로고
    • Knockout mice: Simple solutions to the problems of genetic background and flanking genes
    • Wolfer, D.P., Crusio, W.E., and Lipp, H.P. 2002. Knockout mice: simple solutions to the problems of genetic background and flanking genes. Trends Neurosci. 25:336-340.
    • (2002) Trends Neurosci , vol.25 , pp. 336-340
    • Wolfer, D.P.1    Crusio, W.E.2    Lipp, H.P.3
  • 42
    • 0036150976 scopus 로고    scopus 로고
    • Model of differential susceptibility to mucosal Burkholderia pseudomallei infection
    • Liu, B., Koo, G.C., Yap, E.H., Chua, K.L., and Gan, Y.H. 2001. Model of differential susceptibility to mucosal Burkholderia pseudomallei infection. Infect. Immun. 70:504-511.
    • (2001) Infect. Immun , vol.70 , pp. 504-511
    • Liu, B.1    Koo, G.C.2    Yap, E.H.3    Chua, K.L.4    Gan, Y.H.5
  • 43
    • 18144379929 scopus 로고    scopus 로고
    • Mouse genetic background influences severity of immune responses following trauma-hemorrhage
    • Matsutani, T., Anantha-Samy, T.S., Kang, S.C., Bland, K.I., and Chaudry, I.H. 2005. Mouse genetic background influences severity of immune responses following trauma-hemorrhage. Cytokine. 30:168-176.
    • (2005) Cytokine , vol.30 , pp. 168-176
    • Matsutani, T.1    Anantha-Samy, T.S.2    Kang, S.C.3    Bland, K.I.4    Chaudry, I.H.5
  • 44
    • 0038383286 scopus 로고    scopus 로고
    • Apoptotic neutrophils in the circulation of patients with glycogen storage disease type 1b (GSD1b)
    • Kuijpers, T.W., et al. 2003. Apoptotic neutrophils in the circulation of patients with glycogen storage disease type 1b (GSD1b). Blood. 101:5021-5024.
    • (2003) Blood , vol.101 , pp. 5021-5024
    • Kuijpers, T.W.1
  • 45
    • 18844388999 scopus 로고    scopus 로고
    • Minireview: Hexose-6-phosphate dehydrogenase and redox control of 11beta-hydroxysteroid dehydrogenase type 1 activity
    • Hewitt, K.N., Walker, E.A., and Stewart, P.M. 2005. Minireview: hexose-6-phosphate dehydrogenase and redox control of 11beta-hydroxysteroid dehydrogenase type 1 activity. Endocrinology. 146:2539-2543.
    • (2005) Endocrinology , vol.146 , pp. 2539-2543
    • Hewitt, K.N.1    Walker, E.A.2    Stewart, P.M.3
  • 46
    • 33646007919 scopus 로고    scopus 로고
    • Hexose-6-phosphate dehydrogenase knock-out mice lack 11 beta-hydroxysteroid dehydrogenase type 1-mediated glucocorticoid generation
    • Lavery, G.G., et al. 2006. Hexose-6-phosphate dehydrogenase knock-out mice lack 11 beta-hydroxysteroid dehydrogenase type 1-mediated glucocorticoid generation. J. Biol. Chem. 281:6546-6551.
    • (2006) J. Biol. Chem , vol.281 , pp. 6546-6551
    • Lavery, G.G.1
  • 47
    • 4043077286 scopus 로고    scopus 로고
    • 11beta-hydroxysteroid dehydrogenase type 1: A tissue-specific regulator of glucocorticoid response
    • Tomlinson, J.W., et al. 2004. 11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response. Endocr. Rev. 25:831-866.
    • (2004) Endocr. Rev , vol.25 , pp. 831-866
    • Tomlinson, J.W.1
  • 48
    • 2942731517 scopus 로고    scopus 로고
    • A potential new role for muscle in blood glucose homeostasis
    • Shieh, J.J., Pan, C.J., Mansfield, B.C., and Chou, J.Y. 2004. A potential new role for muscle in blood glucose homeostasis. J. Biol. Chem. 279:26215-26219.
    • (2004) J. Biol. Chem , vol.279 , pp. 26215-26219
    • Shieh, J.J.1    Pan, C.J.2    Mansfield, B.C.3    Chou, J.Y.4
  • 49
    • 0027136174 scopus 로고
    • The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
    • Lin, H.Y., et al. 1993. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol. Biol. Cell. 4:1109-1119.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1109-1119
    • Lin, H.Y.1
  • 50
    • 0033557172 scopus 로고    scopus 로고
    • Impaired antibacterial host defense in mice lacking the N-formylpeptide receptor
    • Gao, J.L., Lee, E.J., and Murphy, P.M. 1999. Impaired antibacterial host defense in mice lacking the N-formylpeptide receptor. J. Exp. Med. 189:657-662.
    • (1999) J. Exp. Med , vol.189 , pp. 657-662
    • Gao, J.L.1    Lee, E.J.2    Murphy, P.M.3


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