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Volumn 91, Issue 8, 2013, Pages 1066-1075

In vitro ischemia suppresses hypoxic induction of hypoxia-inducible factor-1α by inhibition of synthesis and not enhanced degradation

Author keywords

HIF 1 ; Ischemia; Oxygen and glucose deprivation; Prolylhydroxylase

Indexed keywords

ADENOSINE TRIPHOSPHATE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; DACTINOMYCIN; FIREFLY LUCIFERASE; GLUCOSE; HYBRID PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; MESSENGER RNA; OXYGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEASOME INHIBITOR; PROTOCATECHUIC ACID;

EID: 84879603441     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.23204     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 13544251744 scopus 로고    scopus 로고
    • Prosurvival and prodeath effects of hypoxia-inducible factor-1alpha stabilization in a murine hippocampal cell line
    • Aminova LR, Chavez JC, Lee J, Ryu H, Kung A, Lamanna JC, Ratan RR. 2005. Prosurvival and prodeath effects of hypoxia-inducible factor-1alpha stabilization in a murine hippocampal cell line. J Biol Chem 280:3996-4003.
    • (2005) J Biol Chem , vol.280 , pp. 3996-4003
    • Aminova, L.R.1    Chavez, J.C.2    Lee, J.3    Ryu, H.4    Kung, A.5    Lamanna, J.C.6    Ratan, R.R.7
  • 2
    • 34250021865 scopus 로고    scopus 로고
    • Neuron-specific inactivation of the hypoxia inducible factor 1 alpha increases brain injury in a mouse model of transient focal cerebral ischemia
    • Baranova O, Miranda LF, Pichiule P, Dragatsis I, Johnson RS, Chavez JC. 2007. Neuron-specific inactivation of the hypoxia inducible factor 1 alpha increases brain injury in a mouse model of transient focal cerebral ischemia. J Neurosci 27:6320-6332.
    • (2007) J Neurosci , vol.27 , pp. 6320-6332
    • Baranova, O.1    Miranda, L.F.2    Pichiule, P.3    Dragatsis, I.4    Johnson, R.S.5    Chavez, J.C.6
  • 3
    • 0021740750 scopus 로고
    • Inhibition of autoimmune neuropathological process by treatment with an iron-chelating agent
    • Bowern N, Ramshaw IA, Clark IA, Doherty PC. 1984. Inhibition of autoimmune neuropathological process by treatment with an iron-chelating agent. J Exp Med 160:1532-1543.
    • (1984) J Exp Med , vol.160 , pp. 1532-1543
    • Bowern, N.1    Ramshaw, I.A.2    Clark, I.A.3    Doherty, P.C.4
  • 4
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick RK, McKnight SL. 2001. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 5
    • 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 JC, LaManna JC. 2002. 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 22:8922-8931.
    • (2002) J Neurosci , vol.22 , pp. 8922-8931
    • Chavez, J.C.1    LaManna, J.C.2
  • 6
    • 49349109477 scopus 로고    scopus 로고
    • HIF-1alpha inhibition ameliorates neonatal brain injury in a rat pup hypoxic-ischemic model
    • Chen W, Jadhav V, Tang J, Zhang JH. 2008. HIF-1alpha inhibition ameliorates neonatal brain injury in a rat pup hypoxic-ischemic model. Neurobiol Dis 31:433-441.
    • (2008) Neurobiol Dis , vol.31 , pp. 433-441
    • Chen, W.1    Jadhav, V.2    Tang, J.3    Zhang, J.H.4
  • 8
    • 20344386238 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling
    • Emerling BM, Platanias LC, Black E, Nebreda AR, Davis RJ, Chandel NS. 2005. Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling. Mol Cell Biol 25:4853-4862.
    • (2005) Mol Cell Biol , vol.25 , pp. 4853-4862
    • Emerling, B.M.1    Platanias, L.C.2    Black, E.3    Nebreda, A.R.4    Davis, R.J.5    Chandel, N.S.6
  • 10
    • 79953190404 scopus 로고    scopus 로고
    • Use of the ODD-luciferase transgene for the non-invasive imaging of spontaneous tumors in mice
    • Goldman SJ, Chen E, Taylor R, Zhang S, Petrosky W, Reiss M, Jin S. 2011. Use of the ODD-luciferase transgene for the non-invasive imaging of spontaneous tumors in mice. PLoS One 6:e18269.
    • (2011) PLoS One , vol.6
    • Goldman, S.J.1    Chen, E.2    Taylor, R.3    Zhang, S.4    Petrosky, W.5    Reiss, M.6    Jin, S.7
  • 11
    • 59449100497 scopus 로고    scopus 로고
    • Specific inhibition of hypoxia inducible factor 1 exaggerates cell injury induced by in vitro ischemia through deteriorating cellular redox environment
    • Guo S, Miyake M, Liu KJ, Shi H. 2009. Specific inhibition of hypoxia inducible factor 1 exaggerates cell injury induced by in vitro ischemia through deteriorating cellular redox environment. J Neurochem 108:1309-1321.
    • (2009) J Neurochem , vol.108 , pp. 1309-1321
    • Guo, S.1    Miyake, M.2    Liu, K.J.3    Shi, H.4
  • 12
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia
    • Guzy RD, Schumacker PT. 2006. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 91:807-819.
    • (2006) Exp Physiol , vol.91 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 13
    • 79951689572 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α contributes to brain edema after stroke by regulating aquaporins and glycerol distribution in brain
    • Higashida T, Peng C, Li J, Dornbos D3rd, Teng K, Li X, Kinni H, Guthikonda M, Ding Y. 2011. Hypoxia-inducible factor-1α contributes to brain edema after stroke by regulating aquaporins and glycerol distribution in brain. Curr Neurovasc Res 8:44-51.
    • (2011) Curr Neurovasc Res , vol.8 , pp. 44-51
    • Higashida, T.1    Peng, C.2    Li, J.3    Dornbos, D.4    Teng, K.5    Li, X.6    Kinni, H.7    Guthikonda, M.8    Ding, Y.9
  • 16
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang BH, Rue E, Wang GL, Roe R, Semenza GL. 1996. Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J Biol Chem 271:17771-17778.
    • (1996) J Biol Chem , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 17
    • 3042654997 scopus 로고    scopus 로고
    • Does cellular iron dysregulation play a causative role in Parkinson's disease?
    • Kaur D, Andersen J. 2004. Does cellular iron dysregulation play a causative role in Parkinson's disease?Ageing Res Rev 3:327-343.
    • (2004) Ageing Res Rev , vol.3 , pp. 327-343
    • Kaur, D.1    Andersen, J.2
  • 18
    • 79958748164 scopus 로고    scopus 로고
    • Adaptation to moderate hypoxia protects cortical neurons against ischemia-reperfusion injury and excitotoxicity independently of HIF-1α
    • Li D, Bai T, Brorson JR. 2011. Adaptation to moderate hypoxia protects cortical neurons against ischemia-reperfusion injury and excitotoxicity independently of HIF-1α. Exp Neurol 230:302-310.
    • (2011) Exp Neurol , vol.230 , pp. 302-310
    • Li, D.1    Bai, T.2    Brorson, J.R.3
  • 19
    • 77955551367 scopus 로고    scopus 로고
    • Adenosine monophosphate activated protein kinase inhibition is protective in both sexes after experimental stroke
    • Li J, Benashski SE, Siegel C, Liu F, McCullough LD. 2010. Adenosine monophosphate activated protein kinase inhibition is protective in both sexes after experimental stroke. Neurosci Lett 482:62-65.
    • (2010) Neurosci Lett , vol.482 , pp. 62-65
    • Li, J.1    Benashski, S.E.2    Siegel, C.3    Liu, F.4    McCullough, L.D.5
  • 20
  • 21
    • 36248945117 scopus 로고    scopus 로고
    • Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation
    • Lomb DJ, Straub JA, Freeman RS. 2007. Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation. J Neurochem 103:1897-1906.
    • (2007) J Neurochem , vol.103 , pp. 1897-1906
    • Lomb, D.J.1    Straub, J.A.2    Freeman, R.S.3
  • 25
    • 75149154666 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: therapeutic implications for Huntington's disease and Alzheimer's disease
    • Niatsetskaya Z, Basso M, Speer RE, McConoughey SJ, Coppola G, Ma TC, and Ratan RR. 2010. HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: therapeutic implications for Huntington's disease and Alzheimer's disease. Antiox Redox Signal 12:435-443.
    • (2010) Antiox Redox Signal , vol.12 , pp. 435-443
    • Niatsetskaya, Z.1    Basso, M.2    Speer, R.E.3    McConoughey, S.J.4    Coppola, G.5    Ma, T.C.6    Ratan, R.R.7
  • 27
    • 77954177298 scopus 로고    scopus 로고
    • Glucose is necessary for stabilization of hypoxia-inducible factor-1α under hypoxia: contribution of the pentose phosphate pathway to this stabilization
    • Osada-Oka M, Hashiba Y, Akiba S, Imaoka S, Sato T. 2010. Glucose is necessary for stabilization of hypoxia-inducible factor-1α under hypoxia: contribution of the pentose phosphate pathway to this stabilization. FEBS Lett 584:3073-3079.
    • (2010) FEBS Lett , vol.584 , pp. 3073-3079
    • Osada-Oka, M.1    Hashiba, Y.2    Akiba, S.3    Imaoka, S.4    Sato, T.5
  • 28
    • 33846493729 scopus 로고    scopus 로고
    • HIF-1a and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases
    • Paltoglou S, Roberts BJ. 2007. HIF-1a and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases. Oncogene 26:604-609.
    • (2007) Oncogene , vol.26 , pp. 604-609
    • Paltoglou, S.1    Roberts, B.J.2
  • 30
    • 79953170581 scopus 로고    scopus 로고
    • Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent
    • Ryu JH, Li SH, Park HS, Park JW, Lee B, Chun YS. 2011. Hypoxia-inducible factor α subunit stabilization by NEDD8 conjugation is reactive oxygen species-dependent. J Biol Chem 286:6963-6970.
    • (2011) J Biol Chem , vol.286 , pp. 6963-6970
    • Ryu, J.H.1    Li, S.H.2    Park, H.S.3    Park, J.W.4    Lee, B.5    Chun, Y.S.6
  • 31
    • 30444445382 scopus 로고    scopus 로고
    • Mouse model for noninvasive imaging of HIF prolyl hydroxylase activity: assessment of an oral agent that stimulates erythropoietin production
    • Safran M, Kim WY, O'Connell F, Flippin L, Gunzler V, Horner JW, Depinho RA, Kaelin WGJr. 2006. Mouse model for noninvasive imaging of HIF prolyl hydroxylase activity: assessment of an oral agent that stimulates erythropoietin production. Proc Natl Acad Sci U S A 103:105-110.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 105-110
    • Safran, M.1    Kim, W.Y.2    O'Connell, F.3    Flippin, L.4    Gunzler, V.5    Horner, J.W.6    Depinho, R.A.7    Kaelin, W.G.8
  • 33
    • 67650481882 scopus 로고    scopus 로고
    • Selective inhibition of hypoxia-inducible factor (HIF) prolyl-hydroxylase 1 mediates neuroprotection against normoxic oxidative death via HIF- and CREB-independent pathways
    • Siddiq A, Aminova LR, Troy CM, Suh K, Messer Z, Semenza GL, Ratan RR. 2009. Selective inhibition of hypoxia-inducible factor (HIF) prolyl-hydroxylase 1 mediates neuroprotection against normoxic oxidative death via HIF- and CREB-independent pathways. J Neurosci 29:8828-8838.
    • (2009) J Neurosci , vol.29 , pp. 8828-8838
    • Siddiq, A.1    Aminova, L.R.2    Troy, C.M.3    Suh, K.4    Messer, Z.5    Semenza, G.L.6    Ratan, R.R.7
  • 35
    • 78649375395 scopus 로고    scopus 로고
    • Translational regulation of gene expression during conditions of cell stress
    • Spriggs KA, Bushell M, Willis AE. 2010. Translational regulation of gene expression during conditions of cell stress. Mol Cell 40:228-237.
    • (2010) Mol Cell , vol.40 , pp. 228-237
    • Spriggs, K.A.1    Bushell, M.2    Willis, A.E.3
  • 38
    • 39749188133 scopus 로고    scopus 로고
    • The good, the bad, and the cell type-specific roles of hypoxia inducible factor-1 alpha in neurons and astrocytes
    • Vangeison G, Carr D, Federoff HJ, Rempe DA. 2008. The good, the bad, and the cell type-specific roles of hypoxia inducible factor-1 alpha in neurons and astrocytes. J Neurosci 28:1988-1993.
    • (2008) J Neurosci , vol.28 , pp. 1988-1993
    • Vangeison, G.1    Carr, D.2    Federoff, H.J.3    Rempe, D.A.4
  • 39
    • 84855559622 scopus 로고    scopus 로고
    • Preconditioning induces sustained neuroprotection by downregulation of adenosine 5′-monophosphate-activated protein kinase
    • Venna VR, Li J, Benashski SE, Tarabishy S, McCullough LD. 2012. Preconditioning induces sustained neuroprotection by downregulation of adenosine 5′-monophosphate-activated protein kinase. Neuroscience 201:280-287.
    • (2012) Neuroscience , vol.201 , pp. 280-287
    • Venna, V.R.1    Li, J.2    Benashski, S.E.3    Tarabishy, S.4    McCullough, L.D.5
  • 40
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang GL, Semenza GL. 1993. Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J Biol Chem 268:21513-21518.
    • (1993) J Biol Chem , vol.268 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 42
    • 79954594089 scopus 로고    scopus 로고
    • Selective inhibition of early-but not late-expressed HIF-1α is neuroprotective in rats after focal ischemic brain damage
    • Yeh SH, Ou LC, Gean PW, Hung JJ, Chang WC. 2011. Selective inhibition of early-but not late-expressed HIF-1α is neuroprotective in rats after focal ischemic brain damage. Brain Pathol 21:249-262.
    • (2011) Brain Pathol , vol.21 , pp. 249-262
    • Yeh, S.H.1    Ou, L.C.2    Gean, P.W.3    Hung, J.J.4    Chang, W.C.5
  • 43
    • 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 KI, Miller MP, Marquis JC, Baraban JM, Semenza GL, Ratan RR. 1999. 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 19:9821-9830.
    • (1999) J Neurosci , vol.19 , pp. 9821-9830
    • Zaman, K.1    Ryu, H.2    Hall, D.3    O'Donovan, K.4    Lin, K.I.5    Miller, M.P.6    Marquis, J.C.7    Baraban, J.M.8    Semenza, G.L.9    Ratan, R.R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.