메뉴 건너뛰기




Volumn 1626, Issue 1-3, 2003, Pages 10-18

HIF-2α regulates glyceraldehyde-3-phosphate dehydrogenase expression in endothelial cells

Author keywords

Endothelium; Glycolysis; Hep3B cell; Hypoxia; Hypoxia inducible factor 1 (HIF 1)

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; MESSENGER RNA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; HIF1A PROTEIN, HUMAN;

EID: 0037446250     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(03)00049-6     Document Type: Article
Times cited : (30)

References (45)
  • 2
    • 0029039195 scopus 로고
    • Transcriptional regulation of the rat vascular endothelial growth factor gene by hypoxia
    • Levy A.P., Levy N.S., Wegner S., Goldberg M.A. Transcriptional regulation of the rat vascular endothelial growth factor gene by hypoxia. J. Biol. Chem. 270:1995;13333-13340.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13333-13340
    • Levy, A.P.1    Levy, N.S.2    Wegner, S.3    Goldberg, M.A.4
  • 3
    • 0027979247 scopus 로고
    • Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells
    • Czyzyk-Krzeska M.F., Furnari B.A., Lawson E.E., Millhorn D.E. Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells. J. Biol. Chem. 269:1994;760-764.
    • (1994) J. Biol. Chem. , vol.269 , pp. 760-764
    • Czyzyk-Krzeska, M.F.1    Furnari, B.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 4
    • 0026002686 scopus 로고
    • Hypoxia induces endothelin gene expression and secretion in cultured human endothelium
    • Kourembanas S., Marsden P.A., McQuillan L.P., Faller D.V. Hypoxia induces endothelin gene expression and secretion in cultured human endothelium. J. Clin. Invest. 88:1991;1054-1057.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1054-1057
    • Kourembanas, S.1    Marsden, P.A.2    McQuillan, L.P.3    Faller, D.V.4
  • 5
    • 0028805375 scopus 로고
    • Hypoxia and mitochondrial inhibitors regulate expression of glucose transporter-1 via distinct Cis-acting sequences
    • Ebert B.L., Firth J.D., Ratcliffe P.J. Hypoxia and mitochondrial inhibitors regulate expression of glucose transporter-1 via distinct Cis-acting sequences. J. Biol. Chem. 270:1995;29083-29089.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29083-29089
    • Ebert, B.L.1    Firth, J.D.2    Ratcliffe, P.J.3
  • 6
    • 0027971167 scopus 로고
    • Regulation of endothelial cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia
    • Graven K.K., Troxler R.F., Kornfeld H., Panchenko M.V., Farber H.W. Regulation of endothelial cell glyceraldehyde-3-phosphate dehydrogenase expression by hypoxia. J. Biol. Chem. 269:1994;24446-24453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24446-24453
    • Graven, K.K.1    Troxler, R.F.2    Kornfeld, H.3    Panchenko, M.V.4    Farber, H.W.5
  • 7
    • 0028359320 scopus 로고
    • Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes: Similarities with the erythropoietin 3′ enhancer
    • Firth J.D., Ebert B.L., Pugh C.W., Ratcliffe P.J. Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes: similarities with the erythropoietin 3′ enhancer. Proc. Natl. Acad. Sci. U. S. A. 91:1994;6496-6500.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6496-6500
    • Firth, J.D.1    Ebert, B.L.2    Pugh, C.W.3    Ratcliffe, P.J.4
  • 8
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza G.L., Roth P.H., Fang H.M., Wang G.L. 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.L.1    Roth, P.H.2    Fang, H.M.3    Wang, G.L.4
  • 9
    • 0029788974 scopus 로고    scopus 로고
    • Induction of phosphoglycerate kinase 1 gene expression by hypoxia. Roles of Arnt and HIF1alpha
    • Li H., Ko H.P., Whitlock J.P. Induction of phosphoglycerate kinase 1 gene expression by hypoxia. Roles of Arnt and HIF1alpha. J. Biol. Chem. 271:1996;21262-21267.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21262-21267
    • Li, H.1    Ko, H.P.2    Whitlock, J.P.3
  • 12
    • 0036138398 scopus 로고    scopus 로고
    • Regulation of HIF by the von Hippel-Lindau tumour suppressor: Implications for cellular oxygen sensing
    • Mole D.R., Maxwell P.H., Pugh C.W., Ratcliffe P.J. 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.R.1    Maxwell, P.H.2    Pugh, C.W.3    Ratcliffe, P.J.4
  • 13
    • 0033233243 scopus 로고    scopus 로고
    • 2 homeostasis by hypoxia-inducible factor 1
    • 2 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
  • 15
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • Huang L.E., Arany Z., Livingston D.M., Bunn H.F. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J. Biol. Chem. 271:1996;32253-32259.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 16
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda S., Caro J. Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J. Biol. Chem. 272:1997;22642-22647.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 18
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang L.E., Gu J., Schau M., Bunn H.F. Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. U. S. A. 95:1998;7987-7992.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 19
    • 0033526781 scopus 로고    scopus 로고
    • Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins
    • Srinivas V., Zhang L.P., Zhu X.H., Caro J. Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins. Biochem. Biophys. Res. Commun. 260:1999;557-561.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 557-561
    • Srinivas, V.1    Zhang, L.P.2    Zhu, X.H.3    Caro, J.4
  • 22
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando D., Peet D.J., Whelan D.A., Gorman J.J., Whitelaw M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science. 295:2002;858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 24
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick R.K., McKnight S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 294:2001;1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 25
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H., McKnight S.L., Russell D.W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11:1997;72-82.
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 26
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema M., Taya S., Yokotani N., Sogawa K., Matsuda Y., Fujii-Kuriyama Y. A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. Proc. Natl. Acad. Sci. U. S. A. 94:1997;4273-4278.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 4273-4278
    • Ema, M.1    Taya, S.2    Yokotani, N.3    Sogawa, K.4    Matsuda, Y.5    Fujii-Kuriyama, Y.6
  • 27
    • 0343683375 scopus 로고    scopus 로고
    • HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1 alpha and developmentally expressed in blood vessels
    • Flamme I., Frohlich T., von Reutern M., Kappel A., Damert A., Risau W. HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is closely related to hypoxia-inducible factor-1 alpha and developmentally expressed in blood vessels. Mech. Dev. 63:1997;51-60.
    • (1997) Mech. Dev. , vol.63 , pp. 51-60
    • Flamme, I.1    Frohlich, T.2    Von Reutern, M.3    Kappel, A.4    Damert, A.5    Risau, W.6
  • 28
    • 0031971047 scopus 로고    scopus 로고
    • Expression of ARNT, ARNT2, HIF1 alpha, HIF2 alpha and Ah receptor mRNAs in the developing mouse
    • Jain S., Maltepe E., Lu M.M., Simon C., Bradfield C.A. Expression of ARNT, ARNT2, HIF1 alpha, HIF2 alpha and Ah receptor mRNAs in the developing mouse. Mech. Dev. 73:1998;117-123.
    • (1998) Mech. Dev. , vol.73 , pp. 117-123
    • Jain, S.1    Maltepe, E.2    Lu, M.M.3    Simon, C.4    Bradfield, C.A.5
  • 29
    • 0030887045 scopus 로고    scopus 로고
    • Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway
    • Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.Z., Pray-Grant M., Perdew G.H., Bradfield C.A. Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. J. Biol. Chem. 272:1997;8581-8593.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8581-8593
    • Hogenesch, J.B.1    Chan, W.K.2    Jackiw, V.H.3    Brown, R.C.4    Gu, Y.Z.5    Pray-Grant, M.6    Perdew, G.H.7    Bradfield, C.A.8
  • 31
    • 0033870281 scopus 로고    scopus 로고
    • The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages
    • Talks K.L., Turley H., Gatter K.C., Maxwell P.H., Pugh C.W., Ratcliffe P.J., Harris A.L. The expression and distribution of the hypoxia-inducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages. Am. J. Pathol. 157:2000;411-421.
    • (2000) Am. J. Pathol. , vol.157 , pp. 411-421
    • Talks, K.L.1    Turley, H.2    Gatter, K.C.3    Maxwell, P.H.4    Pugh, C.W.5    Ratcliffe, P.J.6    Harris, A.L.7
  • 33
    • 0032741858 scopus 로고    scopus 로고
    • Identification of an oxygen responsive enhancer element in the glyceraldehyde-3-phosphate dehydrogenase gene
    • Graven K.K., Yu Q., Pan D., Roncarati J.S., Farber H.W. Identification of an oxygen responsive enhancer element in the glyceraldehyde-3-phosphate dehydrogenase gene. Biochim. Biophys. Acta. 1447:1999;208-218.
    • (1999) Biochim. Biophys. Acta , vol.1447 , pp. 208-218
    • Graven, K.K.1    Yu, Q.2    Pan, D.3    Roncarati, J.S.4    Farber, H.W.5
  • 34
    • 0023622082 scopus 로고
    • Effect of ambient oxygen on cultured endothelial cells from different vascular beds
    • Farber H.W., Center D.M., Rounds S. Effect of ambient oxygen on cultured endothelial cells from different vascular beds. Am. J. Physiol. 253:1987;H878-H883.
    • (1987) Am. J. Physiol. , vol.253 , pp. 878-H883
    • Farber, H.W.1    Center, D.M.2    Rounds, S.3
  • 35
    • 0031912776 scopus 로고    scopus 로고
    • Hypoxic regulation of endothelial glyceraldehyde-3-phosphate dehydrogenase
    • Graven K.K., McDonald R.J., Farber H.W. Hypoxic regulation of endothelial glyceraldehyde-3-phosphate dehydrogenase. Am. J. Physiol. 274:1998;C347-C355.
    • (1998) Am. J. Physiol. , vol.274 , pp. 347-C355
    • Graven, K.K.1    McDonald, R.J.2    Farber, H.W.3
  • 36
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 37
    • 0025329308 scopus 로고
    • Enhancement by hypoxia of human erythropoietin gene transcription in vitro
    • Costa-Giomi P., Caro J., Weinmann R. Enhancement by hypoxia of human erythropoietin gene transcription in vitro. J. Biol. Chem. 265:1990;10185-10188.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10185-10188
    • Costa-Giomi, P.1    Caro, J.2    Weinmann, R.3
  • 38
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang G.L., Semenza G.L. Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J. Biol. Chem. 268:1993;21513-21518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 39
    • 0028967752 scopus 로고
    • The orphan receptor hepatic nuclear factor 4 functions as a transcriptional activator for tissue-specific and hypoxia-specific erythropoietin gene expression and is antagonized by EAR3/COUP-TF1
    • Galson D.L., Tsuchiya T., Tendler D.S., Huang L.E., Ren Y., Ogura T., Bunn H.F. The orphan receptor hepatic nuclear factor 4 functions as a transcriptional activator for tissue-specific and hypoxia-specific erythropoietin gene expression and is antagonized by EAR3/COUP-TF1. Mol. Cell. Biol. 15:1995;2135-2144.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2135-2144
    • Galson, D.L.1    Tsuchiya, T.2    Tendler, D.S.3    Huang, L.E.4    Ren, Y.5    Ogura, T.6    Bunn, H.F.7
  • 40
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian H., Hammer R.E., Matsumoto A.M., Russell D.W., McKnight S.L. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 12:1998;3320-3324.
    • (1998) Genes Dev. , vol.12 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 41
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling
    • Peng J., Zhang L., Drysdale L., Fong G.H. The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling. Proc. Natl. Acad. Sci. U. S. A. 97:2000;8386-8391.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 42
    • 0019298432 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes. Kinetic mechanism and competitive substrate inhibition by glyceraldehyde 3-phosphate
    • Wang C.S., Alaupovic P. Glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes. Kinetic mechanism and competitive substrate inhibition by glyceraldehyde 3-phosphate. Arch. Biochem. Biophys. 205:1980;136-145.
    • (1980) Arch. Biochem. Biophys. , vol.205 , pp. 136-145
    • Wang, C.S.1    Alaupovic, P.2
  • 43
    • 0020478636 scopus 로고
    • Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase
    • Tsai I.H., Murthy S.N., Steck T.L. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 257:1982;1438-1442.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1438-1442
    • Tsai, I.H.1    Murthy, S.N.2    Steck, T.L.3
  • 45
    • 0029691198 scopus 로고    scopus 로고
    • Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover M.A. Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 58:1996;2271-2277.
    • (1996) Life Sci. , vol.58 , pp. 2271-2277
    • Sirover, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.