메뉴 건너뛰기




Volumn 39, Issue 1, 2003, Pages 43-56

The regulation of glucose metabolism by HIF-1 mediates a neuroprotective response to amyloid beta peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CLOZAPINE; FLUPHENAZINE; GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; HEXOKINASE; HEXOSE PHOSPHATE; HYPOXIA INDUCIBLE FACTOR 1; NEUROLEPTIC AGENT; PYRUVATE KINASE;

EID: 0038644221     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00367-2     Document Type: Article
Times cited : (209)

References (62)
  • 1
    • 0035960878 scopus 로고    scopus 로고
    • Inhibition of glucose transport in PC12 cells by the atypical antipsychotic drugs risperidone and clozapine, and structural analogs of clozapine
    • Ardizzone T.D., Bradley R.J., Freeman A.M. III, Dwyer D.S. Inhibition of glucose transport in PC12 cells by the atypical antipsychotic drugs risperidone and clozapine, and structural analogs of clozapine. Brain Res. 923:2001;82-90.
    • (2001) Brain Res. , vol.923 , pp. 82-90
    • Ardizzone, T.D.1    Bradley, R.J.2    Freeman A.M. III3    Dwyer, D.S.4
  • 3
    • 0027217527 scopus 로고
    • Heat shock partially protects rat pheochromocytoma PC12 cells from amyloid β peptide toxicity
    • Behl C., Schubert D. Heat shock partially protects rat pheochromocytoma PC12 cells from amyloid β peptide toxicity. Neurosci. Lett. 154:1993;1-4.
    • (1993) Neurosci. Lett. , vol.154 , pp. 1-4
    • Behl, C.1    Schubert, D.2
  • 4
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 5
    • 0037131170 scopus 로고    scopus 로고
    • Brain genomic response following hypoxia and re-oxygenation in the neonatal rat
    • Bernaudin M., Tang Y., Reilly M., Petit E., Sharp F.R. Brain genomic response following hypoxia and re-oxygenation in the neonatal rat. J. Biol. Chem. 277:2002;39728-39738.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39728-39738
    • Bernaudin, M.1    Tang, Y.2    Reilly, M.3    Petit, E.4    Sharp, F.R.5
  • 6
    • 0035577767 scopus 로고    scopus 로고
    • Brain metabolism and brain disease: Is metabolic deficiency the proximate cause of Alzheimer dementia?
    • Blass J.P. Brain metabolism and brain disease. is metabolic deficiency the proximate cause of Alzheimer dementia? J. Neurosci. Res. 66:2001;851-856.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 851-856
    • Blass, J.P.1
  • 8
    • 0030719486 scopus 로고    scopus 로고
    • Aerobic glycolysis by proliferating cells
    • Brand K. Aerobic glycolysis by proliferating cells. J. Bioenerg. Biomembr. 29:1997;355-364.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 355-364
    • Brand, K.1
  • 11
    • 0036316323 scopus 로고    scopus 로고
    • Specificity of resistance to oxidative stress
    • Dargusch R., Schubert D. Specificity of resistance to oxidative stress. J. Neurochem. 81:2002;1394-1400.
    • (2002) J. Neurochem. , vol.81 , pp. 1394-1400
    • Dargusch, R.1    Schubert, D.2
  • 12
    • 0033787295 scopus 로고    scopus 로고
    • Two splice variants of the hypoxia-inducible factor HIF-1α as potential dimerization partners of ARNT2 in neurons
    • Drutel G., Kathmann M., Heron A., Gros C., Mace S., Schwartz H.C., Arrang J.M. Two splice variants of the hypoxia-inducible factor HIF-1α as potential dimerization partners of ARNT2 in neurons. Eur. J. Neurosci. 12:2000;3701-3708.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 3701-3708
    • Drutel, G.1    Kathmann, M.2    Heron, A.3    Gros, C.4    Mace, S.5    Schwartz, H.C.6    Arrang, J.M.7
  • 14
    • 0035930627 scopus 로고    scopus 로고
    • Induction of vascular endothelial growth factor expression and hypoxia-inducible factor 1alpha protein by the oxidative stressor arsenite
    • Duyndam M.C., Hulscher T.M., Fontijn D., Pinedo H.M., Boven E. Induction of vascular endothelial growth factor expression and hypoxia-inducible factor 1alpha protein by the oxidative stressor arsenite. J. Biol. Chem. 276:2001;48066-48076.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48066-48076
    • Duyndam, M.C.1    Hulscher, T.M.2    Fontijn, D.3    Pinedo, H.M.4    Boven, E.5
  • 17
    • 0036591850 scopus 로고    scopus 로고
    • Interactions of oxidative stress with cellular calcium dynamics and glucose metabolism in Alzheimer's disease
    • Gibson G.E. Interactions of oxidative stress with cellular calcium dynamics and glucose metabolism in Alzheimer's disease. Free Radic. Biol. Med. 32:2002;1061-1070.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1061-1070
    • Gibson, G.E.1
  • 18
    • 0001205689 scopus 로고
    • Hyperglycemia and glycosuria following chlorpromazine therapy
    • Hiles B.W. Hyperglycemia and glycosuria following chlorpromazine therapy. JAMA. 162:1956;1651.
    • (1956) JAMA , vol.162 , pp. 1651
    • Hiles, B.W.1
  • 19
    • 0036312611 scopus 로고    scopus 로고
    • Alteration of amino acid metabolism in neuronal aggregate cultures exposed to hypoglycaemic conditions
    • Honegger P., Braissant O., Henry H., Boulat O., Bachmann C., Zurich M.-G., Pardo B. Alteration of amino acid metabolism in neuronal aggregate cultures exposed to hypoglycaemic conditions. J. Neurochem. 81:2002;1141-1151.
    • (2002) J. Neurochem. , vol.81 , pp. 1141-1151
    • Honegger, P.1    Braissant, O.2    Henry, H.3    Boulat, O.4    Bachmann, C.5    Zurich, M.-G.6    Pardo, B.7
  • 20
    • 0027933949 scopus 로고
    • Immunolabelling of hippocampal microvessel glucose transporter protein is reduced in Alzheimer's disease
    • Horwood N., Davies D.C. Immunolabelling of hippocampal microvessel glucose transporter protein is reduced in Alzheimer's disease. Virchows Arch. 425:1994;69-72.
    • (1994) Virchows Arch. , vol.425 , pp. 69-72
    • Horwood, N.1    Davies, D.C.2
  • 22
    • 0037088576 scopus 로고    scopus 로고
    • Heat induction of the unphosphorylated form of hypoxia-inducible factor-1α is dependent on heat shock protein-90 activity
    • Katschinski D.M., Le L., Heinrich D., Wagner K.F., Hofer T., Schindler S.G., Wenger R.H. Heat induction of the unphosphorylated form of hypoxia-inducible factor-1α is dependent on heat shock protein-90 activity. J. Biol. Chem. 277:2002;9262-9267.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9262-9267
    • Katschinski, D.M.1    Le, L.2    Heinrich, D.3    Wagner, K.F.4    Hofer, T.5    Schindler, S.G.6    Wenger, R.H.7
  • 23
  • 24
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein W.L., Krafft G.A., Finch C.E. Targeting small Abeta oligomers. the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24:2001;219-224.
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 25
    • 0030867994 scopus 로고    scopus 로고
    • A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion
    • Li Y., Maher P., Schubert D. A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion. Neuron. 19:1997;453-463.
    • (1997) Neuron , vol.19 , pp. 453-463
    • Li, Y.1    Maher, P.2    Schubert, D.3
  • 26
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim G.P., Chu T., Yang F., Beech W., Frautschy S.A., Cole G.M. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J. Neurosci. 21:2001;8370-8377.
    • (2001) J. Neurosci. , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 28
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction
    • Liu Y., Peterson D.A., Kimura H., Schubert D. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69:1997;581-593.
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 30
    • 0027364185 scopus 로고
    • Glucose enhancement of memory in patients with probable senile dementia of the Alzheimer's type
    • Manning C.A., Ragozzino M.E., Gold P.E. Glucose enhancement of memory in patients with probable senile dementia of the Alzheimer's type. Neurobiol. Aging. 14:1993;523-528.
    • (1993) Neurobiol. Aging , vol.14 , pp. 523-528
    • Manning, C.A.1    Ragozzino, M.E.2    Gold, P.E.3
  • 32
    • 0026050541 scopus 로고
    • Would decreased aluminum ingestion reduce the incidence of Alzheimer's disease?
    • McLachlan D.R.C., Kruck T.P., Lukiw W.J., Krishnan S.S. Would decreased aluminum ingestion reduce the incidence of Alzheimer's disease? Can. Med. Assoc. J. 145:1991;793-804.
    • (1991) Can. Med. Assoc. J. , vol.145 , pp. 793-804
    • McLachlan, D.R.C.1    Kruck, T.P.2    Lukiw, W.J.3    Krishnan, S.S.4
  • 33
    • 0036830469 scopus 로고    scopus 로고
    • Regulation of gene expression by oxygen: NF-κB and HIF-1, two extremes
    • Michiels C., Minet E., Mottet D., Raes M. Regulation of gene expression by oxygen. NF-κB and HIF-1, two extremes Free Radic. Biol. Med. 33:2002;1231-1242.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1231-1242
    • Michiels, C.1    Minet, E.2    Mottet, D.3    Raes, M.4
  • 34
    • 0026512651 scopus 로고
    • Differences of regional cerebral glucose metabolism between presenile and senile dementia of Alzheimer type
    • Mielke R., Herholz K., Grond M., Kessler J., Heiss W.D. Differences of regional cerebral glucose metabolism between presenile and senile dementia of Alzheimer type. Neurobiol. Aging. 13:1991;93-98.
    • (1991) Neurobiol. Aging , vol.13 , pp. 93-98
    • Mielke, R.1    Herholz, K.2    Grond, M.3    Kessler, J.4    Heiss, W.D.5
  • 36
    • 0032917662 scopus 로고    scopus 로고
    • The activity of the pentose phosphate pathway is increased in response to oxidative stress in Alzheimer's disease
    • Palmer A.M. The activity of the pentose phosphate pathway is increased in response to oxidative stress in Alzheimer's disease. J. Neural Transm. 106:1999;317-328.
    • (1999) J. Neural Transm. , vol.106 , pp. 317-328
    • Palmer, A.M.1
  • 37
    • 0030894036 scopus 로고    scopus 로고
    • The inhibitory effects of β-amyloid on glutamate and glucose uptakes by cultured astrocytes
    • Parpura-Gill A., Beitz D., Uemura E. The inhibitory effects of β-amyloid on glutamate and glucose uptakes by cultured astrocytes. Brain Res. 754:1997;65-71.
    • (1997) Brain Res. , vol.754 , pp. 65-71
    • Parpura-Gill, A.1    Beitz, D.2    Uemura, E.3
  • 39
    • 0033569839 scopus 로고    scopus 로고
    • Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease
    • Russell R.L., Siedlak S.L., Raina A.K., Bautista J.M., Smith M.A., Perry G. Increased neuronal glucose-6-phosphate dehydrogenase and sulfhydryl levels indicate reductive compensation to oxidative stress in Alzheimer disease. Arch. Biochem. Biophys. 370:1999;236-239.
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 236-239
    • Russell, R.L.1    Siedlak, S.L.2    Raina, A.K.3    Bautista, J.M.4    Smith, M.A.5    Perry, G.6
  • 40
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzyme activity in amyloid beta protein-resistant cells
    • Sagara Y., Dargusch R., Klier F.G., Schubert D., Behl C. Increased antioxidant enzyme activity in amyloid beta protein-resistant cells. J. Neurosci. 16:1996;497-505.
    • (1996) J. Neurosci. , vol.16 , pp. 497-505
    • Sagara, Y.1    Dargusch, R.2    Klier, F.G.3    Schubert, D.4    Behl, C.5
  • 41
    • 0033613855 scopus 로고    scopus 로고
    • Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression
    • Salvemini F., Franze A., Iervolino A., Filosa S., Salzano S., Ursini M.V. Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression. J. Biol. Chem. 274:1999;2750-2757.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2750-2757
    • Salvemini, F.1    Franze, A.2    Iervolino, A.3    Filosa, S.4    Salzano, S.5    Ursini, M.V.6
  • 43
    • 0033664539 scopus 로고    scopus 로고
    • Insulin receptors and insulin action in the brain: Review and clinical implications
    • Schulingkamp R.J., Pagano T.C., Hung D., Raffa R.B. Insulin receptors and insulin action in the brain. review and clinical implications Neurosci. Biobehav. Rev. 24:2000;855-872.
    • (2000) Neurosci. Biobehav. Rev. , vol.24 , pp. 855-872
    • Schulingkamp, R.J.1    Pagano, T.C.2    Hung, D.3    Raffa, R.B.4
  • 45
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • Semenza G.L. Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1. Annu. Rev. Cell Dev. Biol. 15:1999;551-578.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 48
    • 0023627915 scopus 로고
    • Mitochondrial function in brain tissue in primary degenerative dementia
    • Sims N.R., Finegan J.M., Blass J.P., Bowen D.M., Neary D. Mitochondrial function in brain tissue in primary degenerative dementia. Brain Res. 436:1987;30-38.
    • (1987) Brain Res. , vol.436 , pp. 30-38
    • Sims, N.R.1    Finegan, J.M.2    Blass, J.P.3    Bowen, D.M.4    Neary, D.5
  • 50
    • 0033526781 scopus 로고    scopus 로고
    • Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-a) proteins
    • Srinivas V., Zhang L., Shu X., Caro J. Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-a) proteins. Biochem. Biophys. Res. Commun. 260:1999;557-561.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 557-561
    • Srinivas, V.1    Zhang, L.2    Shu, X.3    Caro, J.4
  • 51
    • 0037177589 scopus 로고    scopus 로고
    • Maneuvering in the complex path from genotype to phenotype
    • Strohman R. Maneuvering in the complex path from genotype to phenotype. Science. 296:2002;701-703.
    • (2002) Science , vol.296 , pp. 701-703
    • Strohman, R.1
  • 52
    • 0035809930 scopus 로고    scopus 로고
    • Regulation of antioxidant metabolism by translation initiation factor-2 alpha
    • Tan S., Somia N., Maher P., Schubert D. Regulation of antioxidant metabolism by translation initiation factor-2 alpha. J. Cell Biol. 152:2001;997-1006.
    • (2001) J. Cell Biol. , vol.152 , pp. 997-1006
    • Tan, S.1    Somia, N.2    Maher, P.3    Schubert, D.4
  • 53
    • 0034535535 scopus 로고    scopus 로고
    • Cell death or synaptic loss in Alzheimer disease
    • Terry R.D. Cell death or synaptic loss in Alzheimer disease. J. Neuropathol. Exp. Neurol. 59:2000;1118-1119.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 1118-1119
    • Terry, R.D.1
  • 54
    • 0000354585 scopus 로고
    • Structural basis of the cognitive alterations in Alzheimer disease
    • R.D. Terry, R. Katzman, & K.L. Bick. New York: Raven Press. 179-196.pp
    • Terry R.D., Masliah E., Hansen L.A. Structural basis of the cognitive alterations in Alzheimer disease. Terry R.D., Katzman R., Bick K.L. Alzheimer Disease. 1994;Raven Press, New York. 179-196.pp.
    • (1994) Alzheimer Disease
    • Terry, R.D.1    Masliah, E.2    Hansen, L.A.3
  • 55
    • 0014244137 scopus 로고
    • Phenothiazines and diabetes in hospitalized women
    • Thonnard-Neumann E. Phenothiazines and diabetes in hospitalized women. Am. J. Psychiatry. 124:1968;978-982.
    • (1968) Am. J. Psychiatry , vol.124 , pp. 978-982
    • Thonnard-Neumann, E.1
  • 56
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang G.L., Jiang B.H., Rue E.A., Semenza G.L. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. USA. 92:1995;5510-5514.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 57
    • 0025215947 scopus 로고
    • Coordinate reciprocal trends in glycolytic and mitochondrial transcript accumulations during the in vitro differentiation of human myoblasts
    • Webster K.A., Gunning P., Hardeman E., Wallace D.C., Kedes L. Coordinate reciprocal trends in glycolytic and mitochondrial transcript accumulations during the in vitro differentiation of human myoblasts. J. Cell. Physiol. 142:1990;566-573.
    • (1990) J. Cell. Physiol. , vol.142 , pp. 566-573
    • Webster, K.A.1    Gunning, P.2    Hardeman, E.3    Wallace, D.C.4    Kedes, L.5
  • 59
    • 0027530567 scopus 로고
    • Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells
    • Wong W.L., Brostrom M.A., Kuznetsov G., Gmitter-Yellen D., Brostrom C.O. Inhibition of protein synthesis and early protein processing by thapsigargin in cultured cells. Biochem. J. 289:1993;71-79.
    • (1993) Biochem. J. , vol.289 , pp. 71-79
    • Wong, W.L.1    Brostrom, M.A.2    Kuznetsov, G.3    Gmitter-Yellen, D.4    Brostrom, C.O.5
  • 60
    • 0003751067 scopus 로고
    • Freehold, NJ: Worthington Biochemical Corporation
    • Worthington C. Worthington Enzyme Manual. 1947;Worthington Biochemical Corporation, Freehold, NJ.
    • (1947) Worthington Enzyme Manual
    • Worthington, C.1
  • 61
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein. reversal by tachykinin neuropeptides Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 62
    • 0034307672 scopus 로고    scopus 로고
    • A method for determination of pyridine nucleotides using a single extract
    • Zhang Z., Yu J., Stanton R.C. A method for determination of pyridine nucleotides using a single extract. Anal. Biochem. 285:2000;163-167.
    • (2000) Anal. Biochem. , vol.285 , pp. 163-167
    • Zhang, Z.1    Yu, J.2    Stanton, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.