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Volumn 1, Issue 1, 2004, Pages 26-35

Hypoxic Preconditioning Protects against Ischemic Brain Injury

Author keywords

EPO; erythropoietin; HIF; Hypoxia; hypoxia inducible factor; ischemia; oxygen; preconditioning; stress proteins; stroke; VEGF

Indexed keywords

COBALT CHLORIDE; DEFEROXAMINE; ERYTHROPOIETIN; GLUCOSE TRANSPORTER; GLYCOLYTIC ENZYME; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; PROTEIN; RNA; TRANSCRIPTION FACTOR EGR 1; VASCULOTROPIN; ARNT PROTEIN, RAT; AROMATIC HYDROCARBON RECEPTOR; DNA BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 18744389551     PISSN: 15455343     EISSN: 15455351     Source Type: Journal    
DOI: 10.1602/neurorx.1.1.26     Document Type: Article
Times cited : (227)

References (172)
  • 1
    • 0031713593 scopus 로고    scopus 로고
    • Ischaemic preconditioning: mechanisms and potential clinical applications
    • Hawaleshka A., and Jacobsohn E. Ischaemic preconditioning: mechanisms and potential clinical applications. Can J Anaesth 45 (1998) 670-682
    • (1998) Can J Anaesth , vol.45 , pp. 670-682
    • Hawaleshka, A.1    Jacobsohn, E.2
  • 3
    • 0035937488 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced ischemic tolerance is associated with increased levels of ceramide in brain and in plasma
    • Zimmermann C., Ginis I., Furuya K., Klimanis D., Ruetzler C., Spatz M., and Hallenbeck J. Lipopolysaccharide-induced ischemic tolerance is associated with increased levels of ceramide in brain and in plasma. Brain Res 895 (2001) 59-65
    • (2001) Brain Res , vol.895 , pp. 59-65
    • Zimmermann, C.1    Ginis, I.2    Furuya, K.3    Klimanis, D.4    Ruetzler, C.5    Spatz, M.6    Hallenbeck, J.7
  • 4
    • 0031657749 scopus 로고    scopus 로고
    • Ischemic preconditioning and brain tolerance: temporal histological and functional outcomes, protein synthesis requirement, and interleukin-1 receptor antagonist and early gene expression
    • Barone F., White R., Spera P., Ellison J., Currie R., Wang X., and Feuerstein G. Ischemic preconditioning and brain tolerance: temporal histological and functional outcomes, protein synthesis requirement, and interleukin-1 receptor antagonist and early gene expression. Stroke 29 (1998) 1937-1950
    • (1998) Stroke , vol.29 , pp. 1937-1950
    • Barone, F.1    White, R.2    Spera, P.3    Ellison, J.4    Currie, R.5    Wang, X.6    Feuerstein, G.7
  • 5
    • 0035399856 scopus 로고    scopus 로고
    • Activation of the nuclear factor-κB is a key event in brain tolerance
    • Blondeau N., Widmann C., Lazdunski M., and Heurteaux C. Activation of the nuclear factor-κB is a key event in brain tolerance. J Neurosci 21 (2001) 4668-4677
    • (2001) J Neurosci , vol.21 , pp. 4668-4677
    • Blondeau, N.1    Widmann, C.2    Lazdunski, M.3    Heurteaux, C.4
  • 6
    • 0032836405 scopus 로고    scopus 로고
    • NMDA receptor antagonism, but not AMPA receptor antagonism attenuates induced ischaemic tolerance in the gerbil hippocampus
    • Bond A., Lodge D., Hicks C., Ward M., and O'Neill M. NMDA receptor antagonism, but not AMPA receptor antagonism attenuates induced ischaemic tolerance in the gerbil hippocampus. Eur J Pharmacol 380 (1999) 91-99
    • (1999) Eur J Pharmacol , vol.380 , pp. 91-99
    • Bond, A.1    Lodge, D.2    Hicks, C.3    Ward, M.4    O'Neill, M.5
  • 7
    • 0029990512 scopus 로고    scopus 로고
    • Stress proteins and tolerance to focal cerebral ischemia
    • Chen J., Graham S., Zhu R., and Simon R. Stress proteins and tolerance to focal cerebral ischemia. J Cereb Blood Flow Metab 16 (1996) 566-577
    • (1996) J Cereb Blood Flow Metab , vol.16 , pp. 566-577
    • Chen, J.1    Graham, S.2    Zhu, R.3    Simon, R.4
  • 8
    • 0031037347 scopus 로고    scopus 로고
    • Ischemic tolerance in the brain
    • Chen J., and Simon R. Ischemic tolerance in the brain. Neurology 48 (1997) 306-311
    • (1997) Neurology , vol.48 , pp. 306-311
    • Chen, J.1    Simon, R.2
  • 9
    • 0034724792 scopus 로고    scopus 로고
    • Benign focal ischemic preconditioning induces neuronal Hsp70 and prolonged astrogliosis with expression of Hsp27
    • Currie R., Ellison J., White R., Feuerstein G., Wang X., and Barone F. Benign focal ischemic preconditioning induces neuronal Hsp70 and prolonged astrogliosis with expression of Hsp27. Brain Res 863 (2000) 169-181
    • (2000) Brain Res , vol.863 , pp. 169-181
    • Currie, R.1    Ellison, J.2    White, R.3    Feuerstein, G.4    Wang, X.5    Barone, F.6
  • 10
    • 0029941898 scopus 로고    scopus 로고
    • Hypoxia triggers neuroprotective alterations in hippocampal gene expression via a heme-containing sensor
    • Gage A., and Stanton P. Hypoxia triggers neuroprotective alterations in hippocampal gene expression via a heme-containing sensor. Brain Res 719 (1996) 172-178
    • (1996) Brain Res , vol.719 , pp. 172-178
    • Gage, A.1    Stanton, P.2
  • 13
    • 0037227249 scopus 로고    scopus 로고
    • Ischemic preconditioning in the hippocampus of a knockout mouse lacking SUR1-based K(ATP) channels
    • Munoz A., Nakazaki M., Goodman J., Barrios R., Onetti C., Bryan J., and Aguilar-Bryan L. Ischemic preconditioning in the hippocampus of a knockout mouse lacking SUR1-based K(ATP) channels. Stroke 34 (2003) 164-170
    • (2003) Stroke , vol.34 , pp. 164-170
    • Munoz, A.1    Nakazaki, M.2    Goodman, J.3    Barrios, R.4    Onetti, C.5    Bryan, J.6    Aguilar-Bryan, L.7
  • 14
    • 0036124848 scopus 로고    scopus 로고
    • Cardioprotective effects of chronic hypoxia and ischaemic preconditioning are not additive
    • Neckar J., Papousek F., Novakova O., Ost'adal B., and Kolar F. Cardioprotective effects of chronic hypoxia and ischaemic preconditioning are not additive. Basic Res Cardiol 97 (2002) 161-167
    • (2002) Basic Res Cardiol , vol.97 , pp. 161-167
    • Neckar, J.1    Papousek, F.2    Novakova, O.3    Ost'adal, B.4    Kolar, F.5
  • 15
    • 85047677005 scopus 로고
    • Acute ischaemic preconditioning and chronic hypoxia independently increase myocardial tolerance to ischaemia
    • Tajima M., Katayose D., Bessho M., and Isoyama S. Acute ischaemic preconditioning and chronic hypoxia independently increase myocardial tolerance to ischaemia. Cardiovasc Res 28 (1994) 312-319
    • (1994) Cardiovasc Res , vol.28 , pp. 312-319
    • Tajima, M.1    Katayose, D.2    Bessho, M.3    Isoyama, S.4
  • 16
    • 0037133177 scopus 로고    scopus 로고
    • Ischemic preconditioning acts upstream of GluR2 down-regulation to afford neuroprotection in the hippocampal CA1
    • Tanaka H., Calderone A., Jover T., Grooms S., Yokota H., Zukin R., and Bennett M. Ischemic preconditioning acts upstream of GluR2 down-regulation to afford neuroprotection in the hippocampal CA1. Proc Natl Acad Sci USA 99 (2002) 2362-2367
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2362-2367
    • Tanaka, H.1    Calderone, A.2    Jover, T.3    Grooms, S.4    Yokota, H.5    Zukin, R.6    Bennett, M.7
  • 17
    • 0036949526 scopus 로고    scopus 로고
    • Hypoxic preconditioning increases brain glycogen and delays energy depletion from hypoxia-ischemia in the immature rat
    • Brucklacher R., Vannucci R., and Vannucci S. Hypoxic preconditioning increases brain glycogen and delays energy depletion from hypoxia-ischemia in the immature rat. Dev Neurosci 24 (2002) 411-417
    • (2002) Dev Neurosci , vol.24 , pp. 411-417
    • Brucklacher, R.1    Vannucci, R.2    Vannucci, S.3
  • 18
    • 0033485450 scopus 로고    scopus 로고
    • A global hypoxia preconditioning model: neuroprotection against seizure-induced specific gravity changes (edema) and brain damage in rats
    • Emerson M., Nelson S., Samson F., and Pazdernik T. A global hypoxia preconditioning model: neuroprotection against seizure-induced specific gravity changes (edema) and brain damage in rats. Brain Res Brain Res Protoc 4 (1999) 360-366
    • (1999) Brain Res Brain Res Protoc , vol.4 , pp. 360-366
    • Emerson, M.1    Nelson, S.2    Samson, F.3    Pazdernik, T.4
  • 19
    • 0033577458 scopus 로고    scopus 로고
    • Hypoxia preconditioning attenuates brain edema associated with kainic acid-induced status epilepticus in rats
    • Emerson M., Nelson S., Samson F., and Pazdernik T. Hypoxia preconditioning attenuates brain edema associated with kainic acid-induced status epilepticus in rats. Brain Res 825 (1999) 189-193
    • (1999) Brain Res , vol.825 , pp. 189-193
    • Emerson, M.1    Nelson, S.2    Samson, F.3    Pazdernik, T.4
  • 20
    • 0028221633 scopus 로고
    • Neuroprotection from ischemic brain injury by hypoxic preconditioning in the neonatal rat
    • Gidday J., Fitzgibbons J., Shah A., and Park T. Neuroprotection from ischemic brain injury by hypoxic preconditioning in the neonatal rat. Neurosci Lett 168 (1994) 221-224
    • (1994) Neurosci Lett , vol.168 , pp. 221-224
    • Gidday, J.1    Fitzgibbons, J.2    Shah, A.3    Park, T.4
  • 22
    • 0035854092 scopus 로고    scopus 로고
    • Cerebral protection by hypoxic preconditioning in a murine model of focal ischemia-reperfusion
    • Miller B., Perez R., Shah A., Gonzales E., Park T., and Gidday J. Cerebral protection by hypoxic preconditioning in a murine model of focal ischemia-reperfusion. Neuroreport 12 (2001) 1663-1669
    • (2001) Neuroreport , vol.12 , pp. 1663-1669
    • Miller, B.1    Perez, R.2    Shah, A.3    Gonzales, E.4    Park, T.5    Gidday, J.6
  • 23
    • 0028362264 scopus 로고
    • Preconditioning with hypoxia versus global ischemia in the isolated rat heart: effect on function and metabolism
    • Moolman J., Genade S., Winterbach R., and Lochner A. Preconditioning with hypoxia versus global ischemia in the isolated rat heart: effect on function and metabolism. Cardioscience 5 (1994) 73-80
    • (1994) Cardioscience , vol.5 , pp. 73-80
    • Moolman, J.1    Genade, S.2    Winterbach, R.3    Lochner, A.4
  • 24
    • 0030561569 scopus 로고    scopus 로고
    • Anoxic preconditioning in hippocampal slices: role of adenosine
    • Perez-Pinzon M., Mumford P., Rosenthal M., and Sick T. Anoxic preconditioning in hippocampal slices: role of adenosine. Neuroscience 75 (1996) 687-694
    • (1996) Neuroscience , vol.75 , pp. 687-694
    • Perez-Pinzon, M.1    Mumford, P.2    Rosenthal, M.3    Sick, T.4
  • 25
    • 0034674373 scopus 로고    scopus 로고
    • The importance of free hydroxyl radicals to hypoxia preconditioning
    • Rauca C., Zerbe R., Jantze H., and Krug M. The importance of free hydroxyl radicals to hypoxia preconditioning. Brain Res 868 (2000) 147-149
    • (2000) Brain Res , vol.868 , pp. 147-149
    • Rauca, C.1    Zerbe, R.2    Jantze, H.3    Krug, M.4
  • 28
    • 0034966729 scopus 로고    scopus 로고
    • Hypoxia/reoxygenation promotes myocardial angiogenesis via an NF κB-dependent mechanism in a rat model of chronic myocardial infarction
    • Sasaki H., Ray P., Zhu L., Otani H., Asahara T., and Maulik N. Hypoxia/reoxygenation promotes myocardial angiogenesis via an NF κB-dependent mechanism in a rat model of chronic myocardial infarction. J Mol Cell Cardiol 33 (2001) 283-294
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 283-294
    • Sasaki, H.1    Ray, P.2    Zhu, L.3    Otani, H.4    Asahara, T.5    Maulik, N.6
  • 29
    • 0035919886 scopus 로고    scopus 로고
    • Excitotoxic preconditioning elicited by both glutamate and hypoxia and abolished by lactate transport inhibition in rat hippocampal slices
    • Schurr A., Payne R., Tseng M., Gozal E., and Gozal D. Excitotoxic preconditioning elicited by both glutamate and hypoxia and abolished by lactate transport inhibition in rat hippocampal slices. Neurosci Lett 307 (2001) 151-154
    • (2001) Neurosci Lett , vol.307 , pp. 151-154
    • Schurr, A.1    Payne, R.2    Tseng, M.3    Gozal, E.4    Gozal, D.5
  • 30
    • 85047679229 scopus 로고
    • Hypoxic preconditioning attenuates stunning caused by repeated coronary artery occlusions in dog heart
    • Shizukuda Y., Iwamoto T., Mallet R., and Downey H. Hypoxic preconditioning attenuates stunning caused by repeated coronary artery occlusions in dog heart. Cardiovasc Res 27 (1993) 559-564
    • (1993) Cardiovasc Res , vol.27 , pp. 559-564
    • Shizukuda, Y.1    Iwamoto, T.2    Mallet, R.3    Downey, H.4
  • 31
    • 0031868459 scopus 로고    scopus 로고
    • Hypoxic preconditioning and hypoxic-ischemic brain damage in the immature rat: pathologic and metabolic correlates
    • Vannucci R., Towfighi J., and Vannucci S. Hypoxic preconditioning and hypoxic-ischemic brain damage in the immature rat: pathologic and metabolic correlates. J Neurochem 71 (1998) 1215-1220
    • (1998) J Neurochem , vol.71 , pp. 1215-1220
    • Vannucci, R.1    Towfighi, J.2    Vannucci, S.3
  • 32
    • 0036093403 scopus 로고    scopus 로고
    • Chronic hypoxia preconditioning increases survival in rats suffering from heatstroke
    • Wen H., Lee C., Lee W., Huang K., and Lin M. Chronic hypoxia preconditioning increases survival in rats suffering from heatstroke. Clin Exp Pharmacol Physiol 29 (2002) 435-440
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , pp. 435-440
    • Wen, H.1    Lee, C.2    Lee, W.3    Huang, K.4    Lin, M.5
  • 33
    • 0036703627 scopus 로고    scopus 로고
    • Neuroprotection by hypoxic preconditioning requires sequential activation of vascular endothelial growth factor receptor and Akt
    • Wick A., Wick W., Waltenberger J., Weller M., Dichgans J., and Schulz J. Neuroprotection by hypoxic preconditioning requires sequential activation of vascular endothelial growth factor receptor and Akt. J Neurosci 22 (2002) 6401-6407
    • (2002) J Neurosci , vol.22 , pp. 6401-6407
    • Wick, A.1    Wick, W.2    Waltenberger, J.3    Weller, M.4    Dichgans, J.5    Schulz, J.6
  • 34
    • 0035972870 scopus 로고    scopus 로고
    • A forebrain ischemic preconditioning model established in C57Black/Crj6 mice
    • Wu C., Zhan R., Qi S., Fujihara H., Taga K., and Shimoji K. A forebrain ischemic preconditioning model established in C57Black/Crj6 mice. J Neurosci Methods 107 (2001) 101-106
    • (2001) J Neurosci Methods , vol.107 , pp. 101-106
    • Wu, C.1    Zhan, R.2    Qi, S.3    Fujihara, H.4    Taga, K.5    Shimoji, K.6
  • 35
    • 0032858122 scopus 로고    scopus 로고
    • Changes of adenosine and its A(1) receptor in hypoxic preconditioning
    • Zhang W., and Lu G. Changes of adenosine and its A(1) receptor in hypoxic preconditioning. Biol Signals Recept 8 (1999) 275-280
    • (1999) Biol Signals Recept , vol.8 , pp. 275-280
    • Zhang, W.1    Lu, G.2
  • 37
    • 0034433445 scopus 로고    scopus 로고
    • Ischemic tolerance in the rat neocortex following hypothermic preconditioning
    • Nishio S., Yunoki M., Chen Z., Anzivino M., and Lee K. Ischemic tolerance in the rat neocortex following hypothermic preconditioning. J Neurosurg 93 (2000) 845-851
    • (2000) J Neurosurg , vol.93 , pp. 845-851
    • Nishio, S.1    Yunoki, M.2    Chen, Z.3    Anzivino, M.4    Lee, K.5
  • 38
    • 0030805199 scopus 로고    scopus 로고
    • Chemical preconditioning: a cytoprotective strategy
    • Riepe M., and Ludolph A. Chemical preconditioning: a cytoprotective strategy. Mol Cell Biochem 174 (1997) 249-254
    • (1997) Mol Cell Biochem , vol.174 , pp. 249-254
    • Riepe, M.1    Ludolph, A.2
  • 39
    • 0035833541 scopus 로고    scopus 로고
    • Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades
    • Digicaylioglu M., and Lipton S. Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades. Nature 412 (2001) 641-647
    • (2001) Nature , vol.412 , pp. 641-647
    • Digicaylioglu, M.1    Lipton, S.2
  • 40
    • 0036167642 scopus 로고    scopus 로고
    • TNF-α-induced tolerance to ischemic injury involves differential control of NF-κB transactivation: the role of NF-κB association with p300 adaptor
    • Ginis I., Jaiswal R., Klimanis D., Liu J., Greenspon J., and Hallenbeck J. TNF-α-induced tolerance to ischemic injury involves differential control of NF-κB transactivation: the role of NF-κB association with p300 adaptor. J Cereb Blood Flow Metab 22 (2002) 142-152
    • (2002) J Cereb Blood Flow Metab , vol.22 , pp. 142-152
    • Ginis, I.1    Jaiswal, R.2    Klimanis, D.3    Liu, J.4    Greenspon, J.5    Hallenbeck, J.6
  • 41
    • 0035092459 scopus 로고    scopus 로고
    • Cell permeable exogenous ceramide reduces infarct size in spontaneously hypertensive rats supporting in vitro studies that have implicated ceramide in induction of tolerance to ischemia
    • Furuya K., Ginis I., Takeda H., Chen Y., and Hallenbeck J. Cell permeable exogenous ceramide reduces infarct size in spontaneously hypertensive rats supporting in vitro studies that have implicated ceramide in induction of tolerance to ischemia. J Cereb Blood Flow Metab 21 (2001) 226-232
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 226-232
    • Furuya, K.1    Ginis, I.2    Takeda, H.3    Chen, Y.4    Hallenbeck, J.5
  • 42
    • 0033839757 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in hypoxia-induced ischemic tolerance in neonatal rat brain
    • Bergeron M., Gidday J., Yu A., Semenza G., Ferriero D., and Sharp F. Role of hypoxia-inducible factor-1 in hypoxia-induced ischemic tolerance in neonatal rat brain. Ann Neurol 48 (2000) 285-296
    • (2000) Ann Neurol , vol.48 , pp. 285-296
    • Bergeron, M.1    Gidday, J.2    Yu, A.3    Semenza, G.4    Ferriero, D.5    Sharp, F.6
  • 44
    • 0037036917 scopus 로고    scopus 로고
    • Isoflurane-induced prolonged protection against cerebral ischemia in mice: a redox sensitive mechanism?
    • Kapinya K., Prass K., and Dirnagl U. Isoflurane-induced prolonged protection against cerebral ischemia in mice: a redox sensitive mechanism?. Neuroreport 13 (2002) 1431-1435
    • (2002) Neuroreport , vol.13 , pp. 1431-1435
    • Kapinya, K.1    Prass, K.2    Dirnagl, U.3
  • 45
    • 0034053127 scopus 로고    scopus 로고
    • The protease thrombin is an endogenous mediator of hippocampal neuroprotection against ischemia at low concentrations but causes degeneration at high concentrations
    • Striggow F., Riek M., Breder J., Henrich-Noack P., Reymann K., and Reiser G. The protease thrombin is an endogenous mediator of hippocampal neuroprotection against ischemia at low concentrations but causes degeneration at high concentrations. Proc Natl Acad Sci USA 97 (2000) 2264-2269
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2264-2269
    • Striggow, F.1    Riek, M.2    Breder, J.3    Henrich-Noack, P.4    Reymann, K.5    Reiser, G.6
  • 46
    • 0037265689 scopus 로고    scopus 로고
    • The role of thrombin and thrombin receptors in ischemic, hemorrhagic and traumatic brain injury: deleterious or protective?
    • Xi G., Reiser G., and Keep R. The role of thrombin and thrombin receptors in ischemic, hemorrhagic and traumatic brain injury: deleterious or protective?. J Neurochem 84 (2003) 3-9
    • (2003) J Neurochem , vol.84 , pp. 3-9
    • Xi, G.1    Reiser, G.2    Keep, R.3
  • 47
    • 0036211764 scopus 로고    scopus 로고
    • Normobaric hypoxia induces tolerance to focal permanent cerebral ischemia in association with an increased expression of hypoxia-inducible factor-1 and its target genes, erythropoietin and VEGF, in the adult mouse brain
    • Bernaudin M., Nedelec A., Divoux D., MacKenzie E., Petit E., and Schumann-Bard P. Normobaric hypoxia induces tolerance to focal permanent cerebral ischemia in association with an increased expression of hypoxia-inducible factor-1 and its target genes, erythropoietin and VEGF, in the adult mouse brain. J Cereb Blood Flow Metab 22 (2002) 393-403
    • (2002) J Cereb Blood Flow Metab , vol.22 , pp. 393-403
    • Bernaudin, M.1    Nedelec, A.2    Divoux, D.3    MacKenzie, E.4    Petit, E.5    Schumann-Bard, P.6
  • 49
    • 0032924754 scopus 로고    scopus 로고
    • Hypoxia versus ischemia
    • Simon R. Hypoxia versus ischemia. Neurology 52 (1999) 7-8
    • (1999) Neurology , vol.52 , pp. 7-8
    • Simon, R.1
  • 50
    • 0033435198 scopus 로고    scopus 로고
    • Induction of hypoxia-inducible factor-1 (HIF-1) and its target genes following focal ischaemia in rat brain
    • Bergeron M., Yu A., Solway K., Semenza G., and Sharp F. Induction of hypoxia-inducible factor-1 (HIF-1) and its target genes following focal ischaemia in rat brain. Eur J Neurosci 11 (1999) 4159-4170
    • (1999) Eur J Neurosci , vol.11 , pp. 4159-4170
    • Bergeron, M.1    Yu, A.2    Solway, K.3    Semenza, G.4    Sharp, F.5
  • 51
    • 0037131170 scopus 로고    scopus 로고
    • Brain genomic response following hypoxia and re-oxygenation in the neonatal rat. Identification of genes that might contribute to hypoxia-induced ischemic tolerance
    • Bernaudin M., Tang Y., Reilly M., Petit E., and Sharp F. Brain genomic response following hypoxia and re-oxygenation in the neonatal rat. Identification of genes that might contribute to hypoxia-induced ischemic tolerance. 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.5
  • 52
    • 0029070924 scopus 로고
    • Essential role of adenosine, adenosine A1 receptors, and ATP-sensitive K+ channels in cerebral ischemic preconditioning
    • Heurteaux C., Lauritzen I., Widmann C., and Lazdunski M. Essential role of adenosine, adenosine A1 receptors, and ATP-sensitive K+ channels in cerebral ischemic preconditioning. Proc Natl Acad Sci USA 92 (1995) 4666-4670
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4666-4670
    • Heurteaux, C.1    Lauritzen, I.2    Widmann, C.3    Lazdunski, M.4
  • 53
    • 0027166979 scopus 로고
    • Ischaemic and hypoxic preconditioning enhance postischaemic recovery of function in the rat heart
    • Lasley R., Anderson G., and Mentzer Jr. R. Ischaemic and hypoxic preconditioning enhance postischaemic recovery of function in the rat heart. Cardiovasc Res 27 (1993) 565-570
    • (1993) Cardiovasc Res , vol.27 , pp. 565-570
    • Lasley, R.1    Anderson, G.2    Mentzer Jr., R.3
  • 54
    • 0035205029 scopus 로고    scopus 로고
    • Blood genomic responses differ after stroke, seizures, hypoglycemia, and hypoxia: blood genomic fingerprints of disease
    • Tang Y., Lu A., Aronow B., and Sharp F. Blood genomic responses differ after stroke, seizures, hypoglycemia, and hypoxia: blood genomic fingerprints of disease. Ann Neurol 50 (2001) 699-707
    • (2001) Ann Neurol , vol.50 , pp. 699-707
    • Tang, Y.1    Lu, A.2    Aronow, B.3    Sharp, F.4
  • 55
    • 0036460425 scopus 로고    scopus 로고
    • Genomic responses of the brain to ischemic stroke, intracerebral haemorrhage, kainate seizures, hypoglycemia, and hypoxia
    • Tang Y., Lu A., Aronow B., Wagner K., and Sharp F. Genomic responses of the brain to ischemic stroke, intracerebral haemorrhage, kainate seizures, hypoglycemia, and hypoxia. Eur J Neurosci 15 (2002) 1937-1952
    • (2002) Eur J Neurosci , vol.15 , pp. 1937-1952
    • Tang, Y.1    Lu, A.2    Aronow, B.3    Wagner, K.4    Sharp, F.5
  • 57
    • 0028902781 scopus 로고
    • Cloning of rat grp75, an hsp70-family member, and its expression in normal and ischemic brain
    • Massa S., Longo F., Zuo J., Wang S., Chen J., and Sharp F. Cloning of rat grp75, an hsp70-family member, and its expression in normal and ischemic brain. J Neurosci Res 40 (1995) 807-819
    • (1995) J Neurosci Res , vol.40 , pp. 807-819
    • Massa, S.1    Longo, F.2    Zuo, J.3    Wang, S.4    Chen, J.5    Sharp, F.6
  • 58
    • 0036708853 scopus 로고    scopus 로고
    • Signaling cross-talk between hypoxia and glucose via hypoxia-inducible factor 1 and glucose response elements
    • Kietzmann T., Krones-Herzig A., and Jungermann K. Signaling cross-talk between hypoxia and glucose via hypoxia-inducible factor 1 and glucose response elements. Biochem Pharmacol 64 (2002) 903-911
    • (2002) Biochem Pharmacol , vol.64 , pp. 903-911
    • Kietzmann, T.1    Krones-Herzig, A.2    Jungermann, K.3
  • 59
    • 0035009567 scopus 로고    scopus 로고
    • Cross-talk between the signals hypoxia and glucose at the glucose response element of the L-type pyruvate kinase gene
    • Krones A., Jungermann K., and Kietzmann T. Cross-talk between the signals hypoxia and glucose at the glucose response element of the L-type pyruvate kinase gene. Endocrinology 142 (2001) 2707-2718
    • (2001) Endocrinology , vol.142 , pp. 2707-2718
    • Krones, A.1    Jungermann, K.2    Kietzmann, T.3
  • 61
    • 0036196081 scopus 로고    scopus 로고
    • Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1α and VEGF
    • Poulaki V., Qin W., Joussen A., Hurlbut P., Wiegand S., Rudge J., Yancopoulos G., and Adamis A. Acute intensive insulin therapy exacerbates diabetic blood-retinal barrier breakdown via hypoxia-inducible factor-1α and VEGF. J Clin Invest 109 (2002) 805-815
    • (2002) J Clin Invest , vol.109 , pp. 805-815
    • Poulaki, V.1    Qin, W.2    Joussen, A.3    Hurlbut, P.4    Wiegand, S.5    Rudge, J.6    Yancopoulos, G.7    Adamis, A.8
  • 62
    • 0031783965 scopus 로고    scopus 로고
    • Stress genes protect brain
    • Sharp F. Stress genes protect brain. Ann Neurol 44 (1998) 581-583
    • (1998) Ann Neurol , vol.44 , pp. 581-583
    • Sharp, F.1
  • 63
    • 0033932195 scopus 로고    scopus 로고
    • Multiple molecular penumbras after focal cerebral ischemia
    • Sharp F., Lu A., Tang Y., and Millhorn D. Multiple molecular penumbras after focal cerebral ischemia. J Cereb Blood Flow Metab 20 (2000) 1011-1032
    • (2000) J Cereb Blood Flow Metab , vol.20 , pp. 1011-1032
    • Sharp, F.1    Lu, A.2    Tang, Y.3    Millhorn, D.4
  • 64
    • 0032053169 scopus 로고    scopus 로고
    • Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression
    • Ratcliffe P., O'Rourke J., Maxwell P., and Pugh C. Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression. J Exp Biol 201 (1998) 1153-1162
    • (1998) J Exp Biol , vol.201 , pp. 1153-1162
    • Ratcliffe, P.1    O'Rourke, J.2    Maxwell, P.3    Pugh, C.4
  • 65
    • 0034901463 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology
    • Semenza G. Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology. Trends Mol Med 7 (2001) 345-350
    • (2001) Trends Mol Med , vol.7 , pp. 345-350
    • Semenza, G.1
  • 66
    • 0035783502 scopus 로고    scopus 로고
    • Glial expression of heat shock proteins (HSPs) and oxygen-regulated proteins (ORPs)
    • Sharp F., Bernaudin M., Bartels M., and Wagner K. Glial expression of heat shock proteins (HSPs) and oxygen-regulated proteins (ORPs). Prog Brain Res 132 (2001) 427-440
    • (2001) Prog Brain Res , vol.132 , pp. 427-440
    • Sharp, F.1    Bernaudin, M.2    Bartels, M.3    Wagner, K.4
  • 67
    • 0034185064 scopus 로고    scopus 로고
    • Effects of hypoxia preconditioning on expression of metallothionein-1, 2 and heme oxygenase-1 before and after kainic acid-induced seizures
    • Emerson M., Samson F., and Pazdernik T. Effects of hypoxia preconditioning on expression of metallothionein-1, 2 and heme oxygenase-1 before and after kainic acid-induced seizures. Cell Mol Biol (Noisy-le-grand) 46 (2000) 619-626
    • (2000) Cell Mol Biol (Noisy-le-grand) , vol.46 , pp. 619-626
    • Emerson, M.1    Samson, F.2    Pazdernik, T.3
  • 68
    • 0034870753 scopus 로고    scopus 로고
    • Downregulation of nitric oxide in the brain of mice during their hypoxic preconditioning
    • Lu G., and Liu H. Downregulation of nitric oxide in the brain of mice during their hypoxic preconditioning. J Appl Physiol 91 (2001) 1193-1198
    • (2001) J Appl Physiol , vol.91 , pp. 1193-1198
    • Lu, G.1    Liu, H.2
  • 69
    • 85047677579 scopus 로고
    • Hypoxic preconditioning of ischaemic myocardium
    • Marber M., and Yellon D. Hypoxic preconditioning of ischaemic myocardium. Cardiovasc Res 26 (1992) 556-557
    • (1992) Cardiovasc Res , vol.26 , pp. 556-557
    • Marber, M.1    Yellon, D.2
  • 70
    • 0034711664 scopus 로고    scopus 로고
    • Hypoxia, hyperoxia, ischemia, and brain necrosis
    • Miyamoto O., and Auer R. Hypoxia, hyperoxia, ischemia, and brain necrosis. Neurology 54 (2000) 362-371
    • (2000) Neurology , vol.54 , pp. 362-371
    • Miyamoto, O.1    Auer, R.2
  • 71
  • 72
    • 0030894345 scopus 로고    scopus 로고
    • Increased hypoxic tolerance by chemical inhibition of oxidative phosphorylation: "chemical preconditioning"
    • Riepe M., Esclaire F., Kasischke K., Schreiber S., Nakase H., Kempski O., et al. Increased hypoxic tolerance by chemical inhibition of oxidative phosphorylation: "chemical preconditioning". J Cereb Blood Flow Metab 17 (1997) 257-264
    • (1997) J Cereb Blood Flow Metab , vol.17 , pp. 257-264
    • Riepe, M.1    Esclaire, F.2    Kasischke, K.3    Schreiber, S.4    Nakase, H.5    Kempski, O.6
  • 73
    • 0032566706 scopus 로고    scopus 로고
    • Induction of hypoxia inducible factor 1 by oxygen glucose deprivation is attenuated by hypoxic preconditioning in rat cultured neurons
    • Ruscher K., Isaev N., Trendelenburg G., Weih M., Iurato L., Meisel A., and Dirnagl U. Induction of hypoxia inducible factor 1 by oxygen glucose deprivation is attenuated by hypoxic preconditioning in rat cultured neurons. Neurosci Lett 254 (1998) 117-120
    • (1998) Neurosci Lett , vol.254 , pp. 117-120
    • Ruscher, K.1    Isaev, N.2    Trendelenburg, G.3    Weih, M.4    Iurato, L.5    Meisel, A.6    Dirnagl, U.7
  • 74
    • 85047678002 scopus 로고
    • Hypoxic preconditioning of ischaemic canine myocardium
    • Shizukuda Y., Mallet R., Lee S., and Downey H. Hypoxic preconditioning of ischaemic canine myocardium. Cardiovasc Res 26 (1992) 534-542
    • (1992) Cardiovasc Res , vol.26 , pp. 534-542
    • Shizukuda, Y.1    Mallet, R.2    Lee, S.3    Downey, H.4
  • 75
    • 0034712939 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations
    • Sutter C., Laughner E., and Semenza G. Hypoxia-inducible factor 1α protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations. Proc Natl Acad Sci USA 97 (2000) 4748-4753
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4748-4753
    • Sutter, C.1    Laughner, E.2    Semenza, G.3
  • 76
    • 0037490210 scopus 로고    scopus 로고
    • Hypoxia-inducible factor and its biomedical relevance
    • Huang L., and Bunn H. Hypoxia-inducible factor and its biomedical relevance. J Biol Chem 278 (2003) 19575-19578
    • (2003) J Biol Chem , vol.278 , pp. 19575-19578
    • Huang, L.1    Bunn, H.2
  • 77
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • Semenza G. 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.1
  • 78
    • 0036896201 scopus 로고    scopus 로고
    • Erythropoietin is a paracrine mediator of ischemic tolerance in the brain: evidence from an in vitro model
    • Ruscher K., Freyer D., Karsch M., Isaev N., Megow D., Sawitzki B., et al. Erythropoietin is a paracrine mediator of ischemic tolerance in the brain: evidence from an in vitro model. J Neurosci 22 (2002) 10291-10301
    • (2002) J Neurosci , vol.22 , pp. 10291-10301
    • Ruscher, K.1    Freyer, D.2    Karsch, M.3    Isaev, N.4    Megow, D.5    Sawitzki, B.6
  • 79
  • 80
    • 0036904660 scopus 로고    scopus 로고
    • Rat MYH, a glycosylase for repair of oxidatively damaged DNA, has brain-specific isoforms that localize to neuronal mitochondria
    • Englander E., Hu Z., Sharma A., Lee H., Wu Z., and Greeley G. Rat MYH, a glycosylase for repair of oxidatively damaged DNA, has brain-specific isoforms that localize to neuronal mitochondria. J Neurochem 83 (2002) 1471-1480
    • (2002) J Neurochem , vol.83 , pp. 1471-1480
    • Englander, E.1    Hu, Z.2    Sharma, A.3    Lee, H.4    Wu, Z.5    Greeley, G.6
  • 81
    • 0036312376 scopus 로고    scopus 로고
    • Hypoxia induces mitochondrial DNA damage and stimulates expression of a DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH), in vivo, in the rat brain
    • Lee H., Wang C., Hu Z., Greeley G., Makalowski W., Hellmich H., and Englander E. Hypoxia induces mitochondrial DNA damage and stimulates expression of a DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH), in vivo, in the rat brain. J Neurochem 80 (2002) 928-937
    • (2002) J Neurochem , vol.80 , pp. 928-937
    • Lee, H.1    Wang, C.2    Hu, Z.3    Greeley, G.4    Makalowski, W.5    Hellmich, H.6    Englander, E.7
  • 82
    • 0034658267 scopus 로고    scopus 로고
    • Mitochondrial DNA damage and a hypoxic response are induced by CoCl(2) in rat neuronal PC12 cells
    • Wang G., Hazra T., Mitra S., Lee H., and Englander E. Mitochondrial DNA damage and a hypoxic response are induced by CoCl(2) in rat neuronal PC12 cells. Nucleic Acids Res 28 (2000) 2135-2140
    • (2000) Nucleic Acids Res , vol.28 , pp. 2135-2140
    • Wang, G.1    Hazra, T.2    Mitra, S.3    Lee, H.4    Englander, E.5
  • 83
    • 0030876019 scopus 로고    scopus 로고
    • Hypoxia-ischemia, but not hypoxia alone, induces the expression of heme oxygenase-1 (HSP32) in newborn rat brain
    • Bergeron M., Ferriero D., Vreman H., Stevenson D., and Sharp F. Hypoxia-ischemia, but not hypoxia alone, induces the expression of heme oxygenase-1 (HSP32) in newborn rat brain. J Cereb Blood Flow Metab 17 (1997) 647-658
    • (1997) J Cereb Blood Flow Metab , vol.17 , pp. 647-658
    • Bergeron, M.1    Ferriero, D.2    Vreman, H.3    Stevenson, D.4    Sharp, F.5
  • 84
    • 0036138398 scopus 로고    scopus 로고
    • Regulation of HIF by the von Hippel-Lindau tumour suppressor: implications for cellular oxygen sensing
    • Mole D., Maxwell P., Pugh C., and Ratcliffe P. Regulation of HIF by the von Hippel-Lindau tumour suppressor: implications for cellular oxygen sensing. IUBMB Life 52 (2001) 43-47
    • (2001) IUBMB Life , vol.52 , pp. 43-47
    • Mole, D.1    Maxwell, P.2    Pugh, C.3    Ratcliffe, P.4
  • 85
    • 0037223852 scopus 로고    scopus 로고
    • New insights into an enigmatic tumour suppressor
    • Ratcliffe P. New insights into an enigmatic tumour suppressor. Nat Cell Biol 5 (2003) 7-8
    • (2003) Nat Cell Biol , vol.5 , pp. 7-8
    • Ratcliffe, P.1
  • 87
    • 0026075610 scopus 로고
    • Hypoxia-inducible nuclear factors bind to an enhancer element located 3′ to the human erythropoietin gene
    • Semenza G., Nejfelt M., Chi S., and Antonarakis S. Hypoxia-inducible nuclear factors bind to an enhancer element located 3′ to the human erythropoietin gene. Proc Natl Acad Sci USA 88 (1991) 5680-5684
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5680-5684
    • Semenza, G.1    Nejfelt, M.2    Chi, S.3    Antonarakis, S.4
  • 88
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza G., Roth P., Fang H., and Wang G. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J Biol Chem 269 (1994) 23757-23763
    • (1994) J Biol Chem , vol.269 , pp. 23757-23763
    • Semenza, G.1    Roth, P.2    Fang, H.3    Wang, G.4
  • 89
    • 0035899491 scopus 로고    scopus 로고
    • The pVHL-associated SCF ubiquitin ligase complex: molecular genetic analysis of elongin B and C, Rbx1 and HIF-1α in renal cell carcinoma
    • Clifford S., Astuti D., Hooper L., Maxwell P., Ratcliffe P., and Maher E. The pVHL-associated SCF ubiquitin ligase complex: molecular genetic analysis of elongin B and C, Rbx1 and HIF-1α in renal cell carcinoma. Oncogene 20 (2001) 5067-5074
    • (2001) Oncogene , vol.20 , pp. 5067-5074
    • Clifford, S.1    Astuti, D.2    Hooper, L.3    Maxwell, P.4    Ratcliffe, P.5    Maher, E.6
  • 90
    • 0034682783 scopus 로고    scopus 로고
    • Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein
    • Cockman M., Masson N., Mole D., Jaakkola P., Chang G., Clifford S., et al. Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. J Biol Chem 275 (2000) 25733-25741
    • (2000) J Biol Chem , vol.275 , pp. 25733-25741
    • Cockman, M.1    Masson, N.2    Mole, D.3    Jaakkola, P.4    Chang, G.5    Clifford, S.6
  • 91
    • 18444368709 scopus 로고    scopus 로고
    • Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
    • Hon W., Wilson M., Harlos K., Claridge T., Schofield C., Pugh C., et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL. Nature 417 (2002) 975-978
    • (2002) Nature , vol.417 , pp. 975-978
    • Hon, W.1    Wilson, M.2    Harlos, K.3    Claridge, T.4    Schofield, C.5    Pugh, C.6
  • 92
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang L., Gu J., Schau M., and Bunn H. Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 95 (1998) 7987-7992
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7987-7992
    • Huang, L.1    Gu, J.2    Schau, M.3    Bunn, H.4
  • 93
    • 0029785321 scopus 로고    scopus 로고
    • Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein
    • Iliopoulos O., Levy A., Jiang C., Kaelin Jr. W., and Goldberg M. Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein. Proc Natl Acad Sci USA 93 (1996) 10595-10599
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10595-10599
    • Iliopoulos, O.1    Levy, A.2    Jiang, C.3    Kaelin Jr., W.4    Goldberg, M.5
  • 94
    • 0035253381 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein
    • Ivan M., and Kaelin Jr. W. The von Hippel-Lindau tumor suppressor protein. Curr Opin Genet Dev 11 (2001) 27-34
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 27-34
    • Ivan, M.1    Kaelin Jr., W.2
  • 95
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola P., Mole D., Tian Y., Wilson M., Gielbert J., Gaskell S., et al. Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292 (2001) 468-472
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.2    Tian, Y.3    Wilson, M.4    Gielbert, J.5    Gaskell, S.6
  • 96
    • 0032535364 scopus 로고    scopus 로고
    • The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
    • Kamura T., Sato S., Haque D., Liu L., Kaelin Jr. W., Conaway R., and Conaway J. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev 12 (1998) 3872-3881
    • (1998) Genes Dev , vol.12 , pp. 3872-3881
    • Kamura, T.1    Sato, S.2    Haque, D.3    Liu, L.4    Kaelin Jr., W.5    Conaway, R.6    Conaway, J.7
  • 97
    • 0031445126 scopus 로고    scopus 로고
    • von Hippel-Lindau disease
    • Maher E., and Kaelin Jr. W. von Hippel-Lindau disease. Med (Baltimore) 76 (1997) 381-391
    • (1997) Med (Baltimore) , vol.76 , pp. 381-391
    • Maher, E.1    Kaelin Jr., W.2
  • 98
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell P., Wiesener M., Chang G., Clifford S., Vaux E., Cockman M., et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399 (1999) 271-275
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.1    Wiesener, M.2    Chang, G.3    Clifford, S.4    Vaux, E.5    Cockman, M.6
  • 99
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
    • Ohh M., Park C., Ivan M., Hoffman M., Kim T., Huang L., Pavletich N., Chau V., and Kaelin W. Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat Cell Biol 2 (2000) 423-427
    • (2000) Nat Cell Biol , vol.2 , pp. 423-427
    • Ohh, M.1    Park, C.2    Ivan, M.3    Hoffman, M.4    Kim, T.5    Huang, L.6    Pavletich, N.7    Chau, V.8    Kaelin, W.9
  • 100
    • 0033404668 scopus 로고    scopus 로고
    • Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein
    • Ohh M., Takagi Y., Aso T., Stebbins C., Pavletich N., Zbar B., et al. Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein. J Clin Invest 104 (1999) 1583-1591
    • (1999) J Clin Invest , vol.104 , pp. 1583-1591
    • Ohh, M.1    Takagi, Y.2    Aso, T.3    Stebbins, C.4    Pavletich, N.5    Zbar, B.6
  • 102
    • 0034529914 scopus 로고    scopus 로고
    • Suppression of tumor growth through disruption of hypoxia-inducible transcription
    • Kung A., Wang S., Klco J., Kaelin W., and Livingston D. Suppression of tumor growth through disruption of hypoxia-inducible transcription. Nat Med 6 (2000) 1335-1340
    • (2000) Nat Med , vol.6 , pp. 1335-1340
    • Kung, A.1    Wang, S.2    Klco, J.3    Kaelin, W.4    Livingston, D.5
  • 104
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • Semenza G., Jiang B., Leung S., Passantino R., Concordet J., Maire P., and Giallongo A. Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1. J Biol Chem 271 (1996) 32529-32537
    • (1996) J Biol Chem , vol.271 , pp. 32529-32537
    • Semenza, G.1    Jiang, B.2    Leung, S.3    Passantino, R.4    Concordet, J.5    Maire, P.6    Giallongo, A.7
  • 105
    • 0035941195 scopus 로고    scopus 로고
    • Selection of mutant CHO cells with constitutive activation of the HIF system and inactivation of the von Hippel-Lindau tumor suppressor
    • Vaux E., Wood S., Cockman M., Nicholls L., Yeates K., Pugh C., et al. Selection of mutant CHO cells with constitutive activation of the HIF system and inactivation of the von Hippel-Lindau tumor suppressor. J Biol Chem 276 (2001) 44323-44330
    • (2001) J Biol Chem , vol.276 , pp. 44323-44330
    • Vaux, E.1    Wood, S.2    Cockman, M.3    Nicholls, L.4    Yeates, K.5    Pugh, C.6
  • 106
    • 0034840276 scopus 로고    scopus 로고
    • Hypoxic preconditioning induces changes in HIF-1 target genes in neonatal rat brain
    • Jones N., and Bergeron M. Hypoxic preconditioning induces changes in HIF-1 target genes in neonatal rat brain. J Cereb Blood Flow Metab 21 (2001) 1105-1114
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 1105-1114
    • Jones, N.1    Bergeron, M.2
  • 107
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α
    • Elkins J., Hewitson K., McNeill L., Seibel J., Schlemminger I., Pugh C., et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α. J Biol Chem 278 (2003) 1802-1806
    • (2003) J Biol Chem , vol.278 , pp. 1802-1806
    • Elkins, J.1    Hewitson, K.2    McNeill, L.3    Seibel, J.4    Schlemminger, I.5    Pugh, C.6
  • 108
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein A., Gleadle J., McNeill L., Hewitson K., O'Rourke J., Mole D., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107 (2001) 43-54
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.1    Gleadle, J.2    McNeill, L.3    Hewitson, K.4    O'Rourke, J.5    Mole, D.6
  • 110
    • 18544386401 scopus 로고    scopus 로고
    • Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
    • Hewitson K., McNeill L., Riordan M., Tian Y., Bullock A., Welford R., et al. Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J Biol Chem 277 (2002) 26351-26355
    • (2002) J Biol Chem , vol.277 , pp. 26351-26355
    • Hewitson, K.1    McNeill, L.2    Riordan, M.3    Tian, Y.4    Bullock, A.5    Welford, R.6
  • 111
    • 0037108807 scopus 로고    scopus 로고
    • Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor
    • Ivan M., Haberberger T., Gervasi D., Michelson K., Gunzler V., Kondo K., et al. Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci USA 99 (2002) 13459-13464
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13459-13464
    • Ivan, M.1    Haberberger, T.2    Gervasi, D.3    Michelson, K.4    Gunzler, V.5    Kondo, K.6
  • 112
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation
    • Masson N., Willam C., Maxwell P., Pugh C., and Ratcliffe P. Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation. Embo J 20 (2001) 5197-5206
    • (2001) Embo J , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.3    Pugh, C.4    Ratcliffe, P.5
  • 113
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α -pVHL complex: hydroxyproline recognition in signaling
    • Min J., Yang H., Ivan M., Gertler F., Kaelin Jr. W., and Pavletich N. Structure of an HIF-1α -pVHL complex: hydroxyproline recognition in signaling. Science 296 (2002) 1886-1889
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.5    Pavletich, N.6
  • 114
    • 0035918327 scopus 로고    scopus 로고
    • Signal transduction. How do cells sense oxygen?
    • Zhu H., and Bunn H. Signal transduction. How do cells sense oxygen?. Science 292 (2001) 449-451
    • (2001) Science , vol.292 , pp. 449-451
    • Zhu, H.1    Bunn, H.2
  • 115
    • 0037872699 scopus 로고    scopus 로고
    • Angiogenesis in ischemic and neoplastic disorders
    • Semenza G. Angiogenesis in ischemic and neoplastic disorders. Annu Rev Med 54 (2003) 17-28
    • (2003) Annu Rev Med , vol.54 , pp. 17-28
    • Semenza, G.1
  • 116
    • 0001572828 scopus 로고    scopus 로고
    • Oxygen-regulated transcription factors and their role in pulmonary disease
    • Semenza G. Oxygen-regulated transcription factors and their role in pulmonary disease. Respir Res 1 (2000) 159-162
    • (2000) Respir Res , vol.1 , pp. 159-162
    • Semenza, G.1
  • 117
    • 0037109768 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1 in the rat cerebral cortex after transient global ischemia: potential role of insulin-like growth factor-1
    • Chavez J., and LaManna J. Activation of hypoxia-inducible factor-1 in the rat cerebral cortex after transient global ischemia: potential role of insulin-like growth factor-1. J Neurosci 22 (2002) 8922-8931
    • (2002) J Neurosci , vol.22 , pp. 8922-8931
    • Chavez, J.1    LaManna, J.2
  • 119
    • 0035941117 scopus 로고    scopus 로고
    • Hypoxia induces transcription factor ETS-1 via the activity of hypoxia-inducible factor-1
    • Oikawa M., Abe M., Kurosawa H., Hida W., Shirato K., and Sato Y. Hypoxia induces transcription factor ETS-1 via the activity of hypoxia-inducible factor-1. Biochem Biophys Res Commun 289 (2001) 39-43
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 39-43
    • Oikawa, M.1    Abe, M.2    Kurosawa, H.3    Hida, W.4    Shirato, K.5    Sato, Y.6
  • 120
    • 0035914297 scopus 로고    scopus 로고
    • Synergistic cooperation between hypoxia and transforming growth factor-β pathways on human vascular endothelial growth factor gene expression
    • Sanchez-Elsner T., Botella L., Velasco B., Corbi A., Attisano L., and Bernabeu C. Synergistic cooperation between hypoxia and transforming growth factor-β pathways on human vascular endothelial growth factor gene expression. J Biol Chem 276 (2001) 38527-38535
    • (2001) J Biol Chem , vol.276 , pp. 38527-38535
    • Sanchez-Elsner, T.1    Botella, L.2    Velasco, B.3    Corbi, A.4    Attisano, L.5    Bernabeu, C.6
  • 121
    • 0034627231 scopus 로고    scopus 로고
    • iNOS expression inhibits hypoxia-inducible factor-1 activity
    • Yin J., Yang D., Ku G., and Hsu C. iNOS expression inhibits hypoxia-inducible factor-1 activity. Biochem Biophys Res Commun 279 (2000) 30-34
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 30-34
    • Yin, J.1    Yang, D.2    Ku, G.3    Hsu, C.4
  • 122
    • 0035656824 scopus 로고    scopus 로고
    • Extinguishing Egr-1-dependent inflammatory and thrombotic cascades after lung transplantation
    • Okada M., Fujita T., Sakaguchi T., Olson K., Collins T., Stern D., Yan S., and Pinsky D. Extinguishing Egr-1-dependent inflammatory and thrombotic cascades after lung transplantation. FASEB J 15 (2001) 2757-2759
    • (2001) FASEB J , vol.15 , pp. 2757-2759
    • Okada, M.1    Fujita, T.2    Sakaguchi, T.3    Olson, K.4    Collins, T.5    Stern, D.6    Yan, S.7    Pinsky, D.8
  • 123
    • 0034533374 scopus 로고    scopus 로고
    • Egr-1, a master switch coordinating upregulation of divergent gene families underlying ischemic stress
    • Yan S., Fujita T., Lu J., Okada K., Shan Zou Y., Mackman N., et al. Egr-1, a master switch coordinating upregulation of divergent gene families underlying ischemic stress. Nat Med 6 (2000) 1355-1361
    • (2000) Nat Med , vol.6 , pp. 1355-1361
    • Yan, S.1    Fujita, T.2    Lu, J.3    Okada, K.4    Shan Zou, Y.5    Mackman, N.6
  • 124
    • 0033591346 scopus 로고    scopus 로고
    • Hypoxia-associated induction of early growth response-1 gene expression
    • Yan S., Lu J., Zou Y., Soh-Won J., Cohen D., Buttrick P., et al. Hypoxia-associated induction of early growth response-1 gene expression. J Biol Chem 274 (1999) 15030-15040
    • (1999) J Biol Chem , vol.274 , pp. 15030-15040
    • Yan, S.1    Lu, J.2    Zou, Y.3    Soh-Won, J.4    Cohen, D.5    Buttrick, P.6
  • 125
    • 0033635663 scopus 로고    scopus 로고
    • A pathway leading to hypoxia-induced vascular fibrin deposition
    • Yan S., Pinsky D., and Stern D. A pathway leading to hypoxia-induced vascular fibrin deposition. Semin Thromb Hemost 26 (2000) 479-483
    • (2000) Semin Thromb Hemost , vol.26 , pp. 479-483
    • Yan, S.1    Pinsky, D.2    Stern, D.3
  • 126
    • 13144257677 scopus 로고    scopus 로고
    • Tissue factor transcription driven by Egr-1 is a critical mechanism of murine pulmonary fibrin deposition in hypoxia
    • Yan S., Zou Y., Gao Y., Zhai C., Mackman N., Lee S., et al. Tissue factor transcription driven by Egr-1 is a critical mechanism of murine pulmonary fibrin deposition in hypoxia. Proc Natl Acad Sci USA 95 (1998) 8298-8303
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8298-8303
    • Yan, S.1    Zou, Y.2    Gao, Y.3    Zhai, C.4    Mackman, N.5    Lee, S.6
  • 128
    • 0037389490 scopus 로고    scopus 로고
    • Regulation of tyrosine hydroxylase promoter activity by the von Hippel-Lindau tumor suppressor protein and hypoxia-inducible transcription factors
    • Schnell P., Ignacak M., Bauer A., Striet J., Paulding W., and Czyzyk-Krzeska M. Regulation of tyrosine hydroxylase promoter activity by the von Hippel-Lindau tumor suppressor protein and hypoxia-inducible transcription factors. J Neurochem 85 (2003) 483-491
    • (2003) J Neurochem , vol.85 , pp. 483-491
    • Schnell, P.1    Ignacak, M.2    Bauer, A.3    Striet, J.4    Paulding, W.5    Czyzyk-Krzeska, M.6
  • 129
    • 0033230181 scopus 로고    scopus 로고
    • HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
    • Bianchi L., Tacchini L., and Cairo G. HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation. Nucleic Acids Res 27 (1999) 4223-4227
    • (1999) Nucleic Acids Res , vol.27 , pp. 4223-4227
    • Bianchi, L.1    Tacchini, L.2    Cairo, G.3
  • 130
    • 0037307621 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 and hypoxia response elements mediate the induction of plasminogen activator inhibitor-1 gene expression by insulin in primary rat hepatocytes
    • Kietzmann T., Samoylenko A., Roth U., and Jungermann K. Hypoxia-inducible factor-1 and hypoxia response elements mediate the induction of plasminogen activator inhibitor-1 gene expression by insulin in primary rat hepatocytes. Blood 101 (2003) 907-914
    • (2003) Blood , vol.101 , pp. 907-914
    • Kietzmann, T.1    Samoylenko, A.2    Roth, U.3    Jungermann, K.4
  • 131
    • 0037133736 scopus 로고    scopus 로고
    • Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter
    • Lu S., Gu X., Hoestje S., and Epner D. Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter. Biochim Biophys Acta 1574 (2002) 152-156
    • (2002) Biochim Biophys Acta , vol.1574 , pp. 152-156
    • Lu, S.1    Gu, X.2    Hoestje, S.3    Epner, D.4
  • 132
    • 0033936370 scopus 로고    scopus 로고
    • Regulation of endothelin-1 gene expression in human microvascular endothelial cells by hypoxia and cobalt: role of hypoxia responsive element
    • Minchenko A., and Caro J. Regulation of endothelin-1 gene expression in human microvascular endothelial cells by hypoxia and cobalt: role of hypoxia responsive element. Mol Cell Biochem 208 (2000) 53-62
    • (2000) Mol Cell Biochem , vol.208 , pp. 53-62
    • Minchenko, A.1    Caro, J.2
  • 133
    • 0037033095 scopus 로고    scopus 로고
    • Identification of functional hypoxia response elements in the promoter region of the DEC1 and DEC2 genes
    • Miyazaki K., Kawamoto T., Tanimoto K., Nishiyama M., Honda H., and Kato Y. Identification of functional hypoxia response elements in the promoter region of the DEC1 and DEC2 genes. J Biol Chem 277 (2002) 47014-47021
    • (2002) J Biol Chem , vol.277 , pp. 47014-47021
    • Miyazaki, K.1    Kawamoto, T.2    Tanimoto, K.3    Nishiyama, M.4    Honda, H.5    Kato, Y.6
  • 136
    • 0034641710 scopus 로고    scopus 로고
    • Erythropoietin crosses the blood-brain barrier to protect against experimental brain injury
    • Brines M., Ghezzi P., Keenan S., Agnello D., de Lanerolle N., Cerami C., et al. Erythropoietin crosses the blood-brain barrier to protect against experimental brain injury. Proc Natl Acad Sci USA 97 (2000) 10526-10531
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10526-10531
    • Brines, M.1    Ghezzi, P.2    Keenan, S.3    Agnello, D.4    de Lanerolle, N.5    Cerami, C.6
  • 138
    • 0037447256 scopus 로고    scopus 로고
    • Recombinant human erythropoietin protects the myocardium from ischemia-reperfusion injury and promotes beneficial remodeling
    • Calvillo L., Latini R., Kajstura J., Leri A., Anversa P., Ghezzi P., et al. Recombinant human erythropoietin protects the myocardium from ischemia-reperfusion injury and promotes beneficial remodeling. Proc Natl Acad Sci USA 100 (2003) 4802-4806
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4802-4806
    • Calvillo, L.1    Latini, R.2    Kajstura, J.3    Leri, A.4    Anversa, P.5    Ghezzi, P.6
  • 139
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • Carmeliet P., Dor Y., Herbert J., Fukumura D., Brusselmans K., Dewerchin M., et al. Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis. Nature 394 (1998) 485-490
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.3    Fukumura, D.4    Brusselmans, K.5    Dewerchin, M.6
  • 140
    • 0037154573 scopus 로고    scopus 로고
    • Erythropoietin prevents cognition impairment induced by transient brain ischemia in gerbils
    • Catania M., Marciano M., Parisi A., Sturiale A., Buemi M., Grasso G., et al. Erythropoietin prevents cognition impairment induced by transient brain ischemia in gerbils. Eur J Pharmacol 437 (2002) 147-150
    • (2002) Eur J Pharmacol , vol.437 , pp. 147-150
    • Catania, M.1    Marciano, M.2    Parisi, A.3    Sturiale, A.4    Buemi, M.5    Grasso, G.6
  • 141
    • 0037133191 scopus 로고    scopus 로고
    • Erythropoietin prevents motor neuron apoptosis and neurologic disability in experimental spinal cord ischemic injury
    • Celik M., Gokmen N., Erbayraktar S., Akhisaroglu M., Konakc S., Ulukus C., et al. Erythropoietin prevents motor neuron apoptosis and neurologic disability in experimental spinal cord ischemic injury. Proc Natl Acad Sci USA 99 (2002) 2258-2263
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2258-2263
    • Celik, M.1    Gokmen, N.2    Erbayraktar, S.3    Akhisaroglu, M.4    Konakc, S.5    Ulukus, C.6
  • 143
    • 0034928578 scopus 로고    scopus 로고
    • Neuroprotective effect of recombinant human erythropoietin in experimental subarachnoid hemorrhage
    • Grasso G. Neuroprotective effect of recombinant human erythropoietin in experimental subarachnoid hemorrhage. J Neurosurg Sci 45 (2001) 7-14
    • (2001) J Neurosurg Sci , vol.45 , pp. 7-14
    • Grasso, G.1
  • 144
    • 0037225493 scopus 로고    scopus 로고
    • Neuroprotective effect of erythropoietin on hypoxic-ischemic brain injury in neonatal rats
    • Kumral A., Ozer E., Yilmaz O., Akhisaroglu M., Gokmen N., Duman N., et al. Neuroprotective effect of erythropoietin on hypoxic-ischemic brain injury in neonatal rats. Biol Neonate 83 (2003) 224-228
    • (2003) Biol Neonate , vol.83 , pp. 224-228
    • Kumral, A.1    Ozer, E.2    Yilmaz, O.3    Akhisaroglu, M.4    Gokmen, N.5    Duman, N.6
  • 145
    • 0032501397 scopus 로고    scopus 로고
    • Erythropoietin prevents place navigation disability and cortical infarction in rats with permanent occlusion of the middle cerebral artery
    • Sadamoto Y., Igase K., Sakanaka M., Sato K., Otsuka H., Sakaki S., et al. Erythropoietin prevents place navigation disability and cortical infarction in rats with permanent occlusion of the middle cerebral artery. Biochem Biophys Res Commun 253 (1998) 26-32
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 26-32
    • Sadamoto, Y.1    Igase, K.2    Sakanaka, M.3    Sato, K.4    Otsuka, H.5    Sakaki, S.6
  • 148
    • 0034677718 scopus 로고    scopus 로고
    • An adenoviral vector expressing the glucose transporter protects cultured striatal neurons from 3-nitropropionic acid
    • Fink S., Ho D., McLaughlin J., and Sapolsky R. An adenoviral vector expressing the glucose transporter protects cultured striatal neurons from 3-nitropropionic acid. Brain Res 859 (2000) 21-25
    • (2000) Brain Res , vol.859 , pp. 21-25
    • Fink, S.1    Ho, D.2    McLaughlin, J.3    Sapolsky, R.4
  • 149
    • 0035838277 scopus 로고    scopus 로고
    • Neuroprotective effects of an adenoviral vector expressing the glucose transporter: a detailed description of the mediating cellular events
    • Gupta A., Ho D., Brooke S., Franklin L., Roy M., McLaughlin J., Fink S., and Sapolsky R. Neuroprotective effects of an adenoviral vector expressing the glucose transporter: a detailed description of the mediating cellular events. Brain Res 908 (2001) 49-57
    • (2001) Brain Res , vol.908 , pp. 49-57
    • Gupta, A.1    Ho, D.2    Brooke, S.3    Franklin, L.4    Roy, M.5    McLaughlin, J.6    Fink, S.7    Sapolsky, R.8
  • 150
    • 0029160882 scopus 로고
    • Herpes simplex virus vectors overexpressing the glucose transporter gene protect against seizure-induced neuron loss
    • Lawrence M., Ho D., Dash R., and Sapolsky R. Herpes simplex virus vectors overexpressing the glucose transporter gene protect against seizure-induced neuron loss. Proc Natl Acad Sci USA 92 (1995) 7247-7251
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7247-7251
    • Lawrence, M.1    Ho, D.2    Dash, R.3    Sapolsky, R.4
  • 151
    • 0029761644 scopus 로고    scopus 로고
    • Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
    • Forsythe J., Jiang B., Iyer N., Agani F., Leung S., Koos R., and Semenza G. Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1. Mol Cell Biol 16 (1996) 4604-4613
    • (1996) Mol Cell Biol , vol.16 , pp. 4604-4613
    • Forsythe, J.1    Jiang, B.2    Iyer, N.3    Agani, F.4    Leung, S.5    Koos, R.6    Semenza, G.7
  • 152
    • 0034978562 scopus 로고    scopus 로고
    • Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration
    • Oosthuyse B., Moons L., Storkebaum E., Beck H., Nuyens D., Brusselmans K., et al. Deletion of the hypoxia-response element in the vascular endothelial growth factor promoter causes motor neuron degeneration. Nat Genet 28 (2001) 131-138
    • (2001) Nat Genet , vol.28 , pp. 131-138
    • Oosthuyse, B.1    Moons, L.2    Storkebaum, E.3    Beck, H.4    Nuyens, D.5    Brusselmans, K.6
  • 153
    • 0033571939 scopus 로고    scopus 로고
    • Protection from oxidative stress-induced apoptosis in cortical neuronal cultures by iron chelators is associated with enhanced DNA binding of hypoxia-inducible factor-1 and ATF-1/CREB and increased expression of glycolytic enzymes, p21(waf1/cip1), and erythropoietin
    • Zaman K., Ryu H., Hall D., O'Donovan K., Lin K., Miller M., et al. Protection from oxidative stress-induced apoptosis in cortical neuronal cultures by iron chelators is associated with enhanced DNA binding of hypoxia-inducible factor-1 and ATF-1/CREB and increased expression of glycolytic enzymes, p21(waf1/cip1), and erythropoietin. J Neurosci 19 (1999) 9821-9830
    • (1999) J Neurosci , vol.19 , pp. 9821-9830
    • Zaman, K.1    Ryu, H.2    Hall, D.3    O'Donovan, K.4    Lin, K.5    Miller, M.6
  • 154
    • 0035499204 scopus 로고    scopus 로고
    • Hypoxia in cartilage: HIF-1α is essential for chondrocyte growth arrest and survival
    • Schipani E., Ryan H., Didrickson S., Kobayashi T., Knight M., and Johnson R. Hypoxia in cartilage: HIF-1α is essential for chondrocyte growth arrest and survival. Genes Dev 15 (2001) 2865-2876
    • (2001) Genes Dev , vol.15 , pp. 2865-2876
    • Schipani, E.1    Ryan, H.2    Didrickson, S.3    Kobayashi, T.4    Knight, M.5    Johnson, R.6
  • 155
    • 0036606747 scopus 로고    scopus 로고
    • Gene promoter of apoptosis inhibitory protein IAP2: identification of enhancer elements and activation by severe hypoxia
    • Dong Z., Nishiyama J., Yi X., Venkatachalam M., Denton M., Gu S., Li S., and Qiang M. Gene promoter of apoptosis inhibitory protein IAP2: identification of enhancer elements and activation by severe hypoxia. Biochem J 364 (2002) 413-421
    • (2002) Biochem J , vol.364 , pp. 413-421
    • Dong, Z.1    Nishiyama, J.2    Yi, X.3    Venkatachalam, M.4    Denton, M.5    Gu, S.6    Li, S.7    Qiang, M.8
  • 156
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I κB α activates NF κB through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation
    • Fan C., Li Q., Ross D., and Engelhardt J. Tyrosine phosphorylation of I κB α activates NF κB through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation. J Biol Chem 278 (2003) 2072-2080
    • (2003) J Biol Chem , vol.278 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.4
  • 157
    • 0035866806 scopus 로고    scopus 로고
    • Placenta growth factor gene expression is induced by hypoxia in fibroblasts: a central role for metal transcription factor-1
    • Green C., Lichtlen P., Huynh N., Yanovsky M., Laderoute K., Schaffner W., and Murphy B. Placenta growth factor gene expression is induced by hypoxia in fibroblasts: a central role for metal transcription factor-1. Cancer Res 61 (2001) 2696-2703
    • (2001) Cancer Res , vol.61 , pp. 2696-2703
    • Green, C.1    Lichtlen, P.2    Huynh, N.3    Yanovsky, M.4    Laderoute, K.5    Schaffner, W.6    Murphy, B.7
  • 158
    • 0037444823 scopus 로고    scopus 로고
    • Hypoxia-inducible factor induction by tumour necrosis factor in normoxic cells requires receptor-interacting protein-dependent nuclear factor κB activation
    • Jung Y., Isaacs J., Lee S., Trepel J., Liu Z., and Neckers L. Hypoxia-inducible factor induction by tumour necrosis factor in normoxic cells requires receptor-interacting protein-dependent nuclear factor κB activation. Biochem J 370 (2003) 1011-1017
    • (2003) Biochem J , vol.370 , pp. 1011-1017
    • Jung, Y.1    Isaacs, J.2    Lee, S.3    Trepel, J.4    Liu, Z.5    Neckers, L.6
  • 159
    • 0037470172 scopus 로고    scopus 로고
    • Microtubule disruption utilizes an NFκB-dependent pathway to stabilize HIF-1α protein
    • Jung Y., Isaacs J., Lee S., Trepel J., and Neckers L. Microtubule disruption utilizes an NFκB-dependent pathway to stabilize HIF-1α protein. J Biol Chem 278 (2003) 7445-7452
    • (2003) J Biol Chem , vol.278 , pp. 7445-7452
    • Jung, Y.1    Isaacs, J.2    Lee, S.3    Trepel, J.4    Neckers, L.5
  • 160
    • 0029103274 scopus 로고
    • Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 5′ enhancer
    • Liu Y., Cox S., Morita T., and Kourembanas S. Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 5′ enhancer. Circ Res 77 (1995) 638-643
    • (1995) Circ Res , vol.77 , pp. 638-643
    • Liu, Y.1    Cox, S.2    Morita, T.3    Kourembanas, S.4
  • 163
    • 0036836544 scopus 로고    scopus 로고
    • Stimulation of the murine type II transforming growth factor-beta receptor promoter by the transcription factor Egr-1
    • Wilder P., Bernadt C., Kim J., and Rizzino A. Stimulation of the murine type II transforming growth factor-beta receptor promoter by the transcription factor Egr-1. Mol Reprod Dev 63 (2002) 282-290
    • (2002) Mol Reprod Dev , vol.63 , pp. 282-290
    • Wilder, P.1    Bernadt, C.2    Kim, J.3    Rizzino, A.4
  • 167
    • 0035914436 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2α (HIF-2α) is involved in the apoptotic response to hypoglycemia but not to hypoxia
    • Brusselmans K., Bono F., Maxwell P., Dor Y., Dewerchin M., Collen D., et al. Hypoxia-inducible factor-2α (HIF-2α) is involved in the apoptotic response to hypoglycemia but not to hypoxia. J Biol Chem 276 (2001) 39192-39196
    • (2001) J Biol Chem , vol.276 , pp. 39192-39196
    • Brusselmans, K.1    Bono, F.2    Maxwell, P.3    Dor, Y.4    Dewerchin, M.5    Collen, D.6
  • 168
    • 0033566792 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α mediates hypoxia-induced delayed neuronal death that involves p53
    • Halterman M., Miller C., and Federoff H. Hypoxia-inducible factor-1α mediates hypoxia-induced delayed neuronal death that involves p53. J Neurosci 19 (1999) 6818-6824
    • (1999) J Neurosci , vol.19 , pp. 6818-6824
    • Halterman, M.1    Miller, C.2    Federoff, H.3
  • 169
    • 0035283082 scopus 로고    scopus 로고
    • Tissue plasminogen activator protects hippocampal neurons from oxygen-glucose deprivation injury
    • Flavin M., and Zhao G. Tissue plasminogen activator protects hippocampal neurons from oxygen-glucose deprivation injury. J Neurosci Res 63 (2001) 388-394
    • (2001) J Neurosci Res , vol.63 , pp. 388-394
    • Flavin, M.1    Zhao, G.2
  • 170
    • 0033594338 scopus 로고    scopus 로고
    • Tissue plasminogen activator does not increase neuronal damage in rat models of global and focal ischemia
    • Klein G., Li H., Sun P., and Buchan A. Tissue plasminogen activator does not increase neuronal damage in rat models of global and focal ischemia. Neurology 52 (1999) 1381-1384
    • (1999) Neurology , vol.52 , pp. 1381-1384
    • Klein, G.1    Li, H.2    Sun, P.3    Buchan, A.4
  • 171
    • 0036549939 scopus 로고    scopus 로고
    • Tissue plasminogen activator as a modulator of neuronal survival and function
    • Tsirka S. Tissue plasminogen activator as a modulator of neuronal survival and function. Biochem Soc Trans 30 (2002) 222-225
    • (2002) Biochem Soc Trans , vol.30 , pp. 222-225
    • Tsirka, S.1
  • 172
    • 0031951510 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice
    • Wang Y., Tsirka S., Strickland S., Stieg P., Soriano S., and Lipton S. Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice. Nat Med 4 (1998) 228-231
    • (1998) Nat Med , vol.4 , pp. 228-231
    • Wang, Y.1    Tsirka, S.2    Strickland, S.3    Stieg, P.4    Soriano, S.5    Lipton, S.6


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