메뉴 건너뛰기




Volumn 9, Issue 6, 2003, Pages 677-684

Regulation of angiogenesis by hypoxia: Role of the HIF system

Author keywords

[No Author keywords available]

Indexed keywords

HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR HYDROXYLASE; OXYGENASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0038037735     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0603-677     Document Type: Review
Times cited : (2178)

References (117)
  • 1
    • 84911539247 scopus 로고
    • The number and distribution of capillaries in muscles with calculations of the oxygen pressure head necessary for supplying the tissue
    • Krogh, A. The number and distribution of capillaries in muscles with calculations of the oxygen pressure head necessary for supplying the tissue. J. Physiol. (London) 52, 409-415 (1919).
    • (1919) J. Physiol. (London) , vol.52 , pp. 409-415
    • Krogh, A.1
  • 2
    • 0020201870 scopus 로고
    • Early changes in fiber profile and capillary density in long-term stimulated muscles
    • Hudlicka, O., Dodd, L., Renkin, E.M. & Gray, S.D. Early changes in fiber profile and capillary density in long-term stimulated muscles. Am. J. Physiol. 243, H528-H535 (1982).
    • (1982) Am. J. Physiol. , vol.243 , pp. H528-H535
    • Hudlicka, O.1    Dodd, L.2    Renkin, E.M.3    Gray, S.D.4
  • 3
    • 0018829439 scopus 로고
    • Capillary density of tenotomized skeletal muscles. II. Observations on human muscles after spontaneous rupture of tendon
    • Jozsa, L., Balint, J., Reffy, A., Jarvinen, M. & Kvist, M. Capillary density of tenotomized skeletal muscles. II. Observations on human muscles after spontaneous rupture of tendon. Eur. J. Appl. Physiol. Occup. Physiol. 44, 183-188 (1980).
    • (1980) Eur. J. Appl. Physiol. Occup. Physiol. , vol.44 , pp. 183-188
    • Jozsa, L.1    Balint, J.2    Reffy, A.3    Jarvinen, M.4    Kvist, M.5
  • 4
    • 84906416572 scopus 로고
    • Effect of oxygen on developing retinal vessels with particular reference to the problem of retrolental fibroplasia
    • Ashton, N., Ward, B. & Serpell, G. Effect of oxygen on developing retinal vessels with particular reference to the problem of retrolental fibroplasia. Br. J. Ophthalmol. 38, 397-432 (1954).
    • (1954) Br. J. Ophthalmol. , vol.38 , pp. 397-432
    • Ashton, N.1    Ward, B.2    Serpell, G.3
  • 5
    • 84966192535 scopus 로고
    • The histological structure of some human lung cancers and the possible implications for radio-therapy
    • Thomlinson, R.H. & Gray, L.H. The histological structure of some human lung cancers and the possible implications for radio-therapy. Br. J. Cancer 9, 539-549 (1955).
    • (1955) Br. J. Cancer , vol.9 , pp. 539-549
    • Thomlinson, R.H.1    Gray, L.H.2
  • 6
    • 0015008620 scopus 로고
    • Isolation of a tumor factor responsible for angiogenesis
    • Folkman, J., Merler, E., Abernathy, C. & Williams, G. Isolation of a tumor factor responsible for angiogenesis. J. Exp. Med. 133. 275-288 (1971).
    • (1971) J. Exp. Med. , vol.133 , pp. 275-288
    • Folkman, J.1    Merler, E.2    Abernathy, C.3    Williams, G.4
  • 7
    • 0019446580 scopus 로고
    • Regulation of wound-healing angiogenesis effect of oxygen gradients and inspired oxygen concentration
    • Knighton, D.R., Silver, I.A. & Hunt, T.K. Regulation of wound-healing angiogenesis effect of oxygen gradients and inspired oxygen concentration. Surgery 90, 262-270 (1981).
    • (1981) Surgery , vol.90 , pp. 262-270
    • Knighton, D.R.1    Silver, I.A.2    Hunt, T.K.3
  • 8
    • 0020557197 scopus 로고
    • Oxygen tension regulates the expression of angiogenesis factor by macrophages
    • Knighton, D.R. et al. Oxygen tension regulates the expression of angiogenesis factor by macrophages. Science 221, 1283-1285 (1983).
    • (1983) Science , vol.221 , pp. 1283-1285
    • Knighton, D.R.1
  • 9
    • 0025050735 scopus 로고
    • Oxygen tension regulates the expression of the platelet-derived growth factor-β chain gene in human endothelial cells
    • Kourembanas, S., Hannan, R.L. & Faller, D.V. Oxygen tension regulates the expression of the platelet-derived growth factor-β chain gene in human endothelial cells. J. Clin. Invest. 86, 670-674 (1990).
    • (1990) J. Clin. Invest. , vol.86 , pp. 670-674
    • Kourembanas, S.1    Hannan, R.L.2    Faller, D.V.3
  • 10
    • 0026485002 scopus 로고
    • Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis
    • Shweiki, D., Itin, A., Soffer, D. & Keshet, E. Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis. Nature 359, 843-845 (1992).
    • (1992) Nature , vol.359 , pp. 843-845
    • Shweiki, D.1    Itin, A.2    Soffer, D.3    Keshet, E.4
  • 11
    • 0026446102 scopus 로고
    • Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo
    • Plate, K.H., Breier, G., Weich, H.A. & Risau, W. Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo. Nature 359, 845-848 (1992).
    • (1992) Nature , vol.359 , pp. 845-848
    • Plate, K.H.1    Breier, G.2    Weich, H.A.3    Risau, W.4
  • 12
    • 0025080230 scopus 로고
    • Growth regulation of the vascular system: Evidence for a metabolic hypothesis
    • Adair, T.H., Gay, W.J. & Montani, J.-P. Growth regulation of the vascular system: evidence for a metabolic hypothesis. Am. J. Physiol. 259, R393-R404 (1990).
    • (1990) Am. J. Physiol. , vol.259 , pp. R393-R404
    • Adair, T.H.1    Gay, W.J.2    Montani, J.-P.3
  • 13
    • 0026526168 scopus 로고
    • Erythropoietin: Structure, control of production, and function
    • Jelkmann, W. Erythropoietin: structure, control of production, and function. Physiol. Rev. 72, 449-489 (1992).
    • (1992) Physiol. Rev. , vol.72 , pp. 449-489
    • Jelkmann, W.1
  • 14
    • 0015333307 scopus 로고
    • Unresponsiveness of erythropoietin-producing cells to cyanide
    • Necas, E. & Thorling, E.B. Unresponsiveness of erythropoietin-producing cells to cyanide. Am. J. Physiol. 222, 1187-1190 (1972).
    • (1972) Am. J. Physiol. , vol.222 , pp. 1187-1190
    • Necas, E.1    Thorling, E.B.2
  • 15
    • 0002226997 scopus 로고
    • Studies on erythropoiesis V: The effect of cobalt on the production of erythropoietin
    • Goldwasser, E., Jacobson, L.O., Fried, W. & Plazk, L.F. Studies on erythropoiesis V: The effect of cobalt on the production of erythropoietin. Blood 13, 55-60 (1958).
    • (1958) Blood , vol.13 , pp. 55-60
    • Goldwasser, E.1    Jacobson, L.O.2    Fried, W.3    Plazk, L.F.4
  • 16
    • 0028095127 scopus 로고
    • Similarities between the oxygen-sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin
    • Goldberg, M.A. & Schneider, T.J. Similarities between the oxygen-sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin. J. Biol. Chem. 269, 4355-4359 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4355-4359
    • Goldberg, M.A.1    Schneider, T.J.2
  • 17
    • 0028843411 scopus 로고
    • Regulation of angiogenic growth factor expression by hypoxia, transition metals, and chelating agents
    • Gleadle, J.M., Ebert, B.L., Firth, J.D. & Ratcliffe, P.J. Regulation of angiogenic growth factor expression by hypoxia, transition metals, and chelating agents. Am. J. Physiol. 268, C1362-C1368 (1995).
    • (1995) Am. J. Physiol. , vol.268 , pp. C1362-C1368
    • Gleadle, J.M.1    Ebert, B.L.2    Firth, J.D.3    Ratcliffe, P.J.4
  • 18
    • 0029103274 scopus 로고
    • Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells
    • Liu, Y., Cox, S.R., Morita, T. & Kourembanas, S. Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Circ. Res. 77, 638-643 (1995).
    • (1995) Circ. Res. , vol.77 , pp. 638-643
    • Liu, Y.1    Cox, S.R.2    Morita, T.3    Kourembanas, S.4
  • 19
    • 0029761644 scopus 로고    scopus 로고
    • Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
    • Forsythe, J.A. et al. Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1. Mol. Cell. Biol. 16, 4604-4613 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4604-4613
    • Forsythe, J.A.1
  • 20
    • 0026468180 scopus 로고
    • A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
    • Semenza, G.L. & Wang, G.L. A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol. Cell. Biol. 12, 5447-5454 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 22
    • 0027461553 scopus 로고
    • Inducible operation of the erythropoietin 3′ enhancer in multiple cell lines; evidence for a widespread oxygen sensing mechanism
    • Maxwell, P.H., Pugh, C.W. & Ratcliffe, P.J. Inducible operation of the erythropoietin 3′ enhancer in multiple cell lines; evidence for a widespread oxygen sensing mechanism. Proc. Natl. Acad. Sci. USA 90, 2423-2427 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2423-2427
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 23
    • 0034663989 scopus 로고    scopus 로고
    • HIF-1 and human disease: One highly involved factor
    • Semenza, G.L. HIF-1 and human disease: one highly involved factor. Genes Dev. 14, 1983-1991 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1983-1991
    • Semenza, G.L.1
  • 24
    • 0036320934 scopus 로고    scopus 로고
    • 2-regulated gene expression
    • 2-regulated gene expression. FASEB J. 16, 1151-1162 (2002).
    • (2002) FASEB J. , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 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, 72-82 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 26
    • 0032189844 scopus 로고    scopus 로고
    • Induction of endothelial PAS domain protein-1 by hypoxia: Characterization and comparison with hypoxia-inducible factor-1α
    • Wiesener, M.S. et al. Induction of endothelial PAS domain protein-1 by hypoxia: characterization and comparison with hypoxia-inducible factor-1α. Blood 92, 2260-2268 (1998).
    • (1998) Blood , vol.92 , pp. 2260-2268
    • Wiesener, M.S.1
  • 27
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
    • Makino, Y. et al. Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature 414, 550-554 (2001).
    • (2001) Nature , vol.414 , pp. 550-554
    • Makino, Y.1
  • 28
    • 0035917313 scopus 로고    scopus 로고
    • 2 sensing
    • 2 sensing. Science 292, 464-468 (2001).
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1
  • 29
    • 0035917808 scopus 로고    scopus 로고
    • 2-regulated prolyl hydroxylation
    • 2-regulated prolyl hydroxylation. Science 292, 468-472 (2001).
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 30
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
    • Yu, F., White, S.B., Zhao, Q. & Lee, F.S. HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc. Natl. Acad. Sci. USA 98, 9630-9635 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Zhao, Q.3    Lee, F.S.4
  • 31
    • 17944375360 scopus 로고    scopus 로고
    • C. Elegans EGL-9 and mammalian homologues define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein, A.C.R. et al. C. Elegans EGL-9 and mammalian homologues define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54 (2001).
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.R.1
  • 32
    • 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, 1337-1340 (2001).
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 33
    • 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.S. 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, 26351-26355 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26351-26355
    • Hewitson, K.S.1
  • 34
    • 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.H., Pugh, C.W. & Ratcliffe, P.J. Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 35
    • 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, 858-861 (2002).
    • (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
  • 36
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D. et al. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1
  • 37
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon, P.C., Hirota, K. & Semenza, G.L. FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15, 2675-2686 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 38
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield, C.J. & Zhang, Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9, 722-731 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 39
    • 0028301631 scopus 로고
    • Regulation of fos and jun immediate-early genes by redox or metabolic stress in cardiac myocytes
    • Webster, K.A., Discher, D.J. & Bishopric, N.H. Regulation of fos and jun immediate-early genes by redox or metabolic stress in cardiac myocytes. Circ. Res. 74, 679-686 (1994).
    • (1994) Circ. Res. , vol.74 , pp. 679-686
    • Webster, K.A.1    Discher, D.J.2    Bishopric, N.H.3
  • 40
    • 0028268629 scopus 로고
    • Hypoxia causes the activation of nuclear factor κB through the phosphorylation of IκBα on tyrosine residues
    • Koong, A.C., Chen, E.Y. & Giaccia, A.J. Hypoxia causes the activation of nuclear factor κB through the phosphorylation of IκBα on tyrosine residues. Cancer Res. 54, 1425-1430 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 1425-1430
    • Koong, A.C.1    Chen, E.Y.2    Giaccia, A.J.3
  • 41
    • 0028110809 scopus 로고
    • Hypoxia induces accumulation of p53 protein, but activation of a Gl-phase checkpoint by low-oxygen conditions is independent of p 53 status
    • Graeber, T.G. et al. Hypoxia induces accumulation of p53 protein, but activation of a Gl-phase checkpoint by low-oxygen conditions is independent of p53 status. Mol. Cell. Biol. 14, 6264-6277 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6264-6277
    • Graeber, T.G.1
  • 42
    • 0033572417 scopus 로고    scopus 로고
    • Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation
    • Alarcon, R., Koumenis, C., Geyer, R.K., Maki, C.G. & Giaccia, A.J. Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation. Cancer Res. 59, 6046-6051 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 6046-6051
    • Alarcon, R.1    Koumenis, C.2    Geyer, R.K.3    Maki, C.G.4    Giaccia, A.J.5
  • 43
    • 0344838401 scopus 로고    scopus 로고
    • Von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination
    • Kuznetsova, A.V. et al. von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination. Proc. Natl. Acad. Sci. USA 100, 2706-2711 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2706-2711
    • Kuznetsova, A.V.1
  • 44
    • 0035895737 scopus 로고    scopus 로고
    • Molecular mechanisms of blood vessel growth
    • Conway, E.M., Collen, D. & Carmeliet, P. Molecular mechanisms of blood vessel growth. Cardiovasc. Res. 49, 507-521 (2001).
    • (2001) Cardiovasc. Res. , vol.49 , pp. 507-521
    • Conway, E.M.1    Collen, D.2    Carmeliet, P.3
  • 45
    • 0028786601 scopus 로고
    • A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter
    • Melillo, G. et al. A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter. J. Exp. Med. 182, 1683-1693 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 1683-1693
    • Melillo, G.1
  • 46
    • 8544249876 scopus 로고    scopus 로고
    • Comparison of VEGF, VEGF-B, VEGF-C and Ang-1 mRNA regulation by serum, growth factors, oncoproteins and hypoxia
    • Enholm, B. et al. Comparison of VEGF, VEGF-B, VEGF-C and Ang-1 mRNA regulation by serum, growth factors, oncoproteins and hypoxia. Oncogene 14, 2475-2483 (1997).
    • (1997) Oncogene , vol.14 , pp. 2475-2483
    • Enholm, B.1
  • 47
    • 0036899416 scopus 로고    scopus 로고
    • Expression of the angiopoietins and their receptor Tie2 in human renal clear cell carcinomas; regulation by the von Hippel-Lindau gene and hypoxia
    • Currie, M.J. et al. Expression of the angiopoietins and their receptor Tie2 in human renal clear cell carcinomas; regulation by the von Hippel-Lindau gene and hypoxia. J. Pathol. 198, 502-510 (2002).
    • (2002) J. Pathol. , vol.198 , pp. 502-510
    • Currie, M.J.1
  • 48
    • 0028940664 scopus 로고
    • Increased gene expression for VEGF and the VEGF receptors KDR/Flk and Flt in lungs exposed to acute or to chronic hypoxia
    • Tuder, R.M., Flook, B.E. & Voelkel, N.F. Increased gene expression for VEGF and the VEGF receptors KDR/Flk and Flt in lungs exposed to acute or to chronic hypoxia. J. Clin. Invest. 95, 1798-1807 (1995).
    • (1995) J. Clin. Invest. , vol.95 , pp. 1798-1807
    • Tuder, R.M.1    Flook, B.E.2    Voelkel, N.F.3
  • 49
    • 0030751493 scopus 로고    scopus 로고
    • Differential transcriptional regulation of the two vascular endothelial growth factor receptor genes
    • Gerber, H.-P., Condorelli, F., Park, J. & Ferrara, N. Differential transcriptional regulation of the two vascular endothelial growth factor receptor genes. J. Biol. Chem. 272, 23659-23667 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23659-23667
    • Gerber, H.-P.1    Condorelli, F.2    Park, J.3    Ferrara, N.4
  • 50
    • 0029758798 scopus 로고    scopus 로고
    • Functional upregulation of the vascular endothelial growth factor receptor KDR by hypoxia
    • Waltenberger, J., Mayr, U., Pentz, S. & Hombach, V. Functional upregulation of the vascular endothelial growth factor receptor KDR by hypoxia. Circulation 94, 1647-1654 (1996).
    • (1996) Circulation , vol.94 , pp. 1647-1654
    • Waltenberger, J.1    Mayr, U.2    Pentz, S.3    Hombach, V.4
  • 51
    • 0032985888 scopus 로고    scopus 로고
    • Hypoxia and vascular endothelial growth factor selectively up-regulate angiopoietin-2 in bovine microvascular endothelial cells
    • Oh, H. et al. Hypoxia and vascular endothelial growth factor selectively up-regulate angiopoietin-2 in bovine microvascular endothelial cells. J. Biol. Chem. 274, 15732-15739 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 15732-15739
    • Oh, H.1
  • 52
    • 0033888525 scopus 로고    scopus 로고
    • Hypoxia-inducible angiopoietin-2 expression is mimicked by iodonium compounds and occurs in the rat brain and skin in response to systemic hypoxia and tissue ischaemia
    • Mandriota, S. et al. Hypoxia-inducible angiopoietin-2 expression is mimicked by iodonium compounds and occurs in the rat brain and skin in response to systemic hypoxia and tissue ischaemia. Am. J. Pathol. 156, 1-13 (2000).
    • (2000) Am. J. Pathol. , vol.156 , pp. 1-13
    • Mandriota, S.1
  • 53
    • 0037134413 scopus 로고    scopus 로고
    • Regulation of endothelial matrix metalloproteinase-2 by hypoxia/reoxygenation
    • Ben-Yosef, Y. et al. Regulation of endothelial matrix metalloproteinase-2 by hypoxia/reoxygenation. Circ. Res. 90, 784-791 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 784-791
    • Ben-Yosef, Y.1
  • 54
    • 0033662026 scopus 로고    scopus 로고
    • Hypoxia promotes fibrogenesis in human renal fibroblasts
    • Norman, J.T., Clark, I.M. & Garcia, P.L. Hypoxia promotes fibrogenesis in human renal fibroblasts. Kidney Int. 58, 2351-2366 (2000).
    • (2000) Kidney Int. , vol.58 , pp. 2351-2366
    • Norman, J.T.1    Clark, I.M.2    Garcia, P.L.3
  • 55
    • 0034640269 scopus 로고    scopus 로고
    • Hypoxic induction of prolyl 4-hydroxylase α(I) in cultured cells
    • Takahashi, Y., Takahashi, S., Shiga, Y., Yoshimi, T. & Miura, T. Hypoxic induction of prolyl 4-hydroxylase α(I) in cultured cells. J. Biol. Chem. 275, 14139-14146 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14139-14146
    • Takahashi, Y.1    Takahashi, S.2    Shiga, Y.3    Yoshimi, T.4    Miura, T.5
  • 56
    • 0032795850 scopus 로고    scopus 로고
    • Induction of the plasminogen activator inhibitor-1 gene expression by mild hypoxia via a hypoxia response element binding the hypoxia-inducible factor-1 in rat hepatocytes
    • Kietzmann, T., Roth, U. & Jungermann, K. Induction of the plasminogen activator inhibitor-1 gene expression by mild hypoxia via a hypoxia response element binding the hypoxia-inducible factor-1 in rat hepatocytes. Blood 94, 4177-4185 (1999).
    • (1999) Blood , vol.94 , pp. 4177-4185
    • Kietzmann, T.1    Roth, U.2    Jungermann, K.3
  • 57
    • 0032079312 scopus 로고    scopus 로고
    • Hypoxia stimulates urokinase receptor expression through a heme protein-dependent pathway
    • Graham, C.H., Fitzpatrick, T.E. & McCrae, K.R. Hypoxia stimulates urokinase receptor expression through a heme protein-dependent pathway. Blood 91, 3300-3307 (1998).
    • (1998) Blood , vol.91 , pp. 3300-3307
    • Graham, C.H.1    Fitzpatrick, T.E.2    McCrae, K.R.3
  • 58
    • 0032387693 scopus 로고    scopus 로고
    • Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells
    • Phelan, M.W., Forman, L.W., Perrine, S.P. & Faller, D.V. Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells. J. Lab. Clin. Med. 132, 519-529 (1998).
    • (1998) J. Lab. Clin. Med. , vol.132 , pp. 519-529
    • Phelan, M.W.1    Forman, L.W.2    Perrine, S.P.3    Faller, D.V.4
  • 59
    • 0029070920 scopus 로고
    • Hypoxia-mediated induction of acidic/basic fibroblast growth factor and platelet-derived growth factor in mononuclear phagocytes stimulates growth of hypoxic endothelial cells
    • Kuwubara, K. et al. Hypoxia-mediated induction of acidic/basic fibroblast growth factor and platelet-derived growth factor in mononuclear phagocytes stimulates growth of hypoxic endothelial cells. Proc. Natl. Acad. Sci. USA 92, 4606-4610 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4606-4610
    • Kuwubara, K.1
  • 60
    • 0031801052 scopus 로고    scopus 로고
    • Hypoxia down-regulates MCP-1 expression: Implications for macrophage distribution in tumors
    • Negus, R.P., Turner, L., Burke, F. & Balkwill, F.R. Hypoxia down-regulates MCP-1 expression: implications for macrophage distribution in tumors. J. Leukoc. Biol. 63, 758-765 (1998).
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 758-765
    • Negus, R.P.1    Turner, L.2    Burke, F.3    Balkwill, F.R.4
  • 61
    • 0034649507 scopus 로고    scopus 로고
    • Identification of novel hypoxia-dependent and independent target genes of the von Hippel-Lindau (VHL) tumor suppressor by mRNA differential expression profiling
    • Wykoff, C.C., Pugh, C.W., Maxwell, P.H., Harris, A.L. & Ratcliffe, P.J. Identification of novel hypoxia-dependent and independent target genes of the von Hippel-Lindau (VHL) tumor suppressor by mRNA differential expression profiling. Oncogene 19, 6297-6305 (2000).
    • (2000) Oncogene , vol.19 , pp. 6297-6305
    • Wykoff, C.C.1    Pugh, C.W.2    Maxwell, P.H.3    Harris, A.L.4    Ratcliffe, P.J.5
  • 62
    • 0027089909 scopus 로고
    • Media conditioned by smooth muscle cells cultured in a variety of hypoxic environments stimulates in vitro angiogenesis. A relationship to transforming growth factor-β 1
    • Sakuda, H., Nakashima, Y., Kuriyama, S. & Sueishi, K. Media conditioned by smooth muscle cells cultured in a variety of hypoxic environments stimulates in vitro angiogenesis. A relationship to transforming growth factor-β1. Am. J. Pathol. 141, 1507-1516 (1992).
    • (1992) Am. J. Pathol. , vol.141 , pp. 1507-1516
    • Sakuda, H.1    Nakashima, Y.2    Kuriyama, S.3    Sueishi, K.4
  • 63
    • 0029034799 scopus 로고
    • Hypoxia induces capillary network formation in cultured bovine pulmonary microvessel endothelial cells
    • Phillips, P.G., Birnby, L.M. & Narendran, A. Hypoxia induces capillary network formation in cultured bovine pulmonary microvessel endothelial cells. Am. J. Physiol. 268, L789-L800 (1995).
    • (1995) Am. J. Physiol. , vol.268 , pp. L789-L800
    • Phillips, P.G.1    Birnby, L.M.2    Narendran, A.3
  • 64
    • 0037374289 scopus 로고    scopus 로고
    • Regulation of colon carcinoma cell invasion by hypoxia-inducible factor 1
    • Krishnamachary, B. et al. Regulation of colon carcinoma cell invasion by hypoxia-inducible factor 1. Cancer Res. 63, 1138-1143 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 1138-1143
    • Krishnamachary, B.1
  • 65
    • 0023814896 scopus 로고
    • Adenosine and hypoxia stimulate proliferation and migration of endothelial cells
    • Meininger, C.J., Schelling, M.E. & Granger, H.J. Adenosine and hypoxia stimulate proliferation and migration of endothelial cells. Am. J. Physiol. 255, H554-H562 (1988).
    • (1988) Am. J. Physiol. , vol.255 , pp. H554-H562
    • Meininger, C.J.1    Schelling, M.E.2    Granger, H.J.3
  • 66
    • 0025981672 scopus 로고
    • Macrovascular and microvascular endothelium during long-term hypoxia: Alterations in cell growth, monolayer permeability, and cell surface coagulant properties
    • Shreeniwas, R. et al. Macrovascular and microvascular endothelium during long-term hypoxia: alterations in cell growth, monolayer permeability, and cell surface coagulant properties. J. Cell. Physiol. 146, 8-17 (1991).
    • (1991) J. Cell. Physiol. , vol.146 , pp. 8-17
    • Shreeniwas, R.1
  • 67
    • 0030927308 scopus 로고    scopus 로고
    • Distinct effect of hypoxia on endothelial cell proliferation and cycling
    • Tucci, M. et al. Distinct effect of hypoxia on endothelial cell proliferation and cycling. Am. J. Physiol. 272, C1700-C1708 (1997).
    • (1997) Am. J. Physiol. , vol.272 , pp. C1700-C1708
    • Tucci, M.1
  • 68
    • 15444342958 scopus 로고    scopus 로고
    • 2 homeostasis by hypoxia-inducible factor 1α
    • 2 homeostasis by hypoxia-inducible factor 1α. Genes Dev. 12, 149-162 (1997).
    • (1997) Genes Dev. , vol.12 , pp. 149-162
    • Iyer, N.V.1
  • 69
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • Carmeliet, P. et al. Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis. Nature 394, 485-490 (1998).
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1
  • 70
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1α is required for solid tumor formation and embryonic vascularization
    • Ryan, H.E., Lo, J. & Johnson, R.S. HIF-1α is required for solid tumor formation and embryonic vascularization. EMBO J. 17, 3005-3015 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 71
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy, N.S., Chung, S., Furneaux, H. & Levy, A.P. Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J. Biol. Chem. 273, 6417-6423 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 72
    • 0031869662 scopus 로고    scopus 로고
    • Translation of vascular endothelial growth factor mRNA by internal ribosome entry: Implications for translation under hypoxia
    • Stein, I. et al. Translation of vascular endothelial growth factor mRNA by internal ribosome entry: implications for translation under hypoxia. Mol. Cell. Biol. 18, 3112-3119 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3112-3119
    • Stein, I.1
  • 73
    • 0030609013 scopus 로고    scopus 로고
    • Vascular endothelial growth factor up-regulates its receptor fms-like tyrosine kinase 1 (FLT-1) and a soluble variant of FLT-1 in human vascular endothelial cells
    • Barleon, B. et al. Vascular endothelial growth factor up-regulates its receptor fms-like tyrosine kinase 1 (FLT-1) and a soluble variant of FLT-1 in human vascular endothelial cells. Cancer Res. 57, 5421-5425 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 5421-5425
    • Barleon, B.1
  • 74
    • 0033562569 scopus 로고    scopus 로고
    • Defective vascularization of HIF-1α-null embryos is not associated with VEGF deficiency but with mesenchymal cell death
    • Kotch, L.E., Iyer, N.V., Laughner, E. & Semenza, G.L. Defective vascularization of HIF-1α-null embryos is not associated with VEGF deficiency but with mesenchymal cell death. Dev. Biol. 209, 254-267 (1999).
    • (1999) Dev. Biol. , vol.209 , pp. 254-267
    • Kotch, L.E.1    Iyer, N.V.2    Laughner, E.3    Semenza, G.L.4
  • 75
    • 0030943461 scopus 로고    scopus 로고
    • Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT
    • Maltepe, E., Schmidt, J.V., Baunoch, D., Bradfield, C.A. & Simon, M.C. Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT. Nature 386, 403-407 (1997).
    • (1997) Nature , vol.386 , pp. 403-407
    • Maltepe, E.1    Schmidt, J.V.2    Baunoch, D.3    Bradfield, C.A.4    Simon, M.C.5
  • 76
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS1/hypoxia-inducible factor 2α plays an important role in vascular remodeling
    • Peng, J., Zhang, L., Drysdale, L. & Fong, G.H. The transcription factor EPAS1/hypoxia-inducible factor 2α plays an important role in vascular remodeling. Proc. Natl. Acad. Sci. USA 97, 8386-8391 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 77
    • 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, 3320-3324 (1998).
    • (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
  • 78
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle, V. et al. Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. Nat. Med. 8, 702-710 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 702-710
    • Compernolle, V.1
  • 79
    • 0035142809 scopus 로고    scopus 로고
    • Determination of hypoxic region by hypoxia marker in developing mouse embryos in vivo: A possible signal for vessel development
    • Lee, Y.M. et al. Determination of hypoxic region by hypoxia marker in developing mouse embryos in vivo: a possible signal for vessel development. Dev. Dyn. 220, 175-186 (2001).
    • (2001) Dev. Dyn. , vol.220 , pp. 175-186
    • Lee, Y.M.1
  • 80
    • 0037416792 scopus 로고    scopus 로고
    • HLF/HIF-2α is a key factor in retinopathy of prematurity in association with erythropoietin
    • Morita, M. et al. HLF/HIF-2α is a key factor in retinopathy of prematurity in association with erythropoietin. EMBO J. 22, 1134-1146 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1134-1146
    • Morita, M.1
  • 81
    • 0036064271 scopus 로고    scopus 로고
    • HIF-1-induced erythropoietin in the hypoxic retina protects against light-induced retinal degeneration
    • Grimm, C. et al. HIF-1-induced erythropoietin in the hypoxic retina protects against light-induced retinal degeneration. Nat. Med. 8, 718-724 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 718-724
    • Grimm, C.1
  • 82
    • 18444380862 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor-1α and -2α in hypoxic and ischemic rat kidneys
    • Rosenberger, C. et al. Expression of hypoxia-inducible factor-1α and -2α in hypoxic and ischemic rat kidneys. J. Am. Soc. Nephrol. 13, 1721-1732 (2002).
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 1721-1732
    • Rosenberger, C.1
  • 83
    • 0034594876 scopus 로고    scopus 로고
    • Early expression of angiogenesis factors in acute myocardial ischemia and infarction
    • Lee, S.H. et al. Early expression of angiogenesis factors in acute myocardial ischemia and infarction. N. Engl. J. Med. 342, 626-633 (2000).
    • (2000) N. Engl. J. Med. , vol.342 , pp. 626-633
    • Lee, S.H.1
  • 84
    • 0035159670 scopus 로고    scopus 로고
    • HIF-1 is expressed in normoxic tissue and displays an organ-specific regulation under systemic hypoxia
    • Stroka, D.M. et al. HIF-1 is expressed in normoxic tissue and displays an organ-specific regulation under systemic hypoxia. FASEB J. 15, 2445-2453 (2001).
    • (2001) FASEB J. , vol.15 , pp. 2445-2453
    • Stroka, D.M.1
  • 85
    • 0037315337 scopus 로고    scopus 로고
    • Widespread, hypoxia-inducible expression of HIF-2α in distinct cell populations of different organs
    • Wiesener, M.S. et al. Widespread, hypoxia-inducible expression of HIF-2α in distinct cell populations of different organs. FASEB J. 17, 271-273 (2002).
    • (2002) FASEB J. , vol.17 , pp. 271-273
    • Wiesener, M.S.1
  • 86
    • 0038710247 scopus 로고    scopus 로고
    • Impaired oxygen-dependent reduction of HIF-1α and -2α proteins in pre-eclamptic placentae
    • Rajakumar, A., Doty, K., Daftary, A., Harger, G. & Conrad, K.P. Impaired oxygen-dependent reduction of HIF-1α and -2α proteins in pre-eclamptic placentae. Placenta 24, 199-208 (2003).
    • (2003) Placenta , vol.24 , pp. 199-208
    • Rajakumar, A.1    Doty, K.2    Daftary, A.3    Harger, G.4    Conrad, K.P.5
  • 87
    • 0034936994 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor lalpha by macrophages in the rheumatoid synovium: Implications for targeting of therapeutic genes to the inflamed joint
    • Hollander, A.P., Corke, K.P., Freemont, A, J. & Lewis, C.E. Expression of hypoxia-inducible factor lalpha by macrophages in the rheumatoid synovium: implications for targeting of therapeutic genes to the inflamed joint. Arthritis Rheum. 44, 1540-1544 (2001).
    • (2001) Arthritis Rheum. , vol.44 , pp. 1540-1544
    • Hollander, A.P.1    Corke, K.P.2    Freemont, A.J.3    Lewis, C.E.4
  • 88
    • 0032932138 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1α is increased in ischemic retina: Temporal and spatial correlation with VEGF expression
    • Ozaki, H. et al, Hypoxia inducible factor-1α is increased in ischemic retina: temporal and spatial correlation with VEGF expression. Invest. Ophthalmol. Vis. Sci, 40, 182-189 (1999).
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 182-189
    • Ozaki, H.1
  • 89
    • 0034326273 scopus 로고    scopus 로고
    • Coordinate up-regulation of hypoxia inducible factor (HIF)-1α and HIF-1 target genes during multistage epidermal carcinogenesis and wound healing
    • Elson, D.A., Ryan, H.E., Snow, J.W., Johnson, R. & Arbeit, J.M. Coordinate up-regulation of hypoxia inducible factor (HIF)-1α and HIF-1 target genes during multistage epidermal carcinogenesis and wound healing. Cancer Res, 60, 6189-6195 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 6189-6195
    • Elson, D.A.1    Ryan, H.E.2    Snow, J.W.3    Johnson, R.4    Arbeit, J.M.5
  • 90
    • 0035476509 scopus 로고    scopus 로고
    • Induction of hypervascularity without leakage or inflammation in transgenic mice overexpressing hypoxia-inducible factor-1α
    • Elson, D.A. et al. Induction of hypervascularity without leakage or inflammation in transgenic mice overexpressing hypoxia-inducible factor-1α. Genes Dev. 15, 2520-2532 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2520-2532
    • Elson, D.A.1
  • 91
    • 0034739533 scopus 로고    scopus 로고
    • Angiogenesis is induced in a rabbit model of hindlimb ischemia by naked DNA encoding an HIF-1α/VP 16 hybrid transcription factor
    • Vincent, K.A. et al. Angiogenesis is induced in a rabbit model of hindlimb ischemia by naked DNA encoding an HIF-1α/VP16 hybrid transcription factor. Circulation 102, 2255-2261 (2000).
    • (2000) Circulation , vol.102 , pp. 2255-2261
    • Vincent, K.A.1
  • 92
    • 0036275028 scopus 로고    scopus 로고
    • Intramyocardial injection of naked DNA encoding HIF-1α/VP 16 hybrid to enhance angio genesis in an acute myocardial infarction model in the rat
    • Shyu, K.G. et al. Intramyocardial injection of naked DNA encoding HIF-1α/VP16 hybrid to enhance angiogenesis in an acute myocardial infarction model in the rat. Cardiovasc. Res. 54, 576-583 (2002).
    • (2002) Cardiovasc. Res. , vol.54 , pp. 576-583
    • Shyu, K.G.1
  • 93
    • 0033970878 scopus 로고    scopus 로고
    • PR 39, a peptide regulator of angiogenesis
    • Li, J. et al. PR39, a peptide regulator of angiogenesis. Nat. Med. 6, 49-55 (2000).
    • (2000) Nat. Med. , vol.6 , pp. 49-55
    • Li, J.1
  • 94
    • 0036667348 scopus 로고    scopus 로고
    • Peptide blockade of HIFα degradation modulates cellular metabolism and angiogenesis
    • Willam, C. et al. Peptide blockade of HIFα degradation modulates cellular metabolism and angiogenesis. Proc. Natl. Acad. Sci. USA 99, 10423-10428 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10423-10428
    • Willam, C.1
  • 95
    • 0035975982 scopus 로고    scopus 로고
    • Inhibition of collagen synthesis with prolyl 4-hydroxylase inhibitor improves left ventricular function and alters the pattern of left ventricular dilatation after myocardial infarction
    • Nwogu, N.I. et al. Inhibition of collagen synthesis with prolyl 4-hydroxylase inhibitor improves left ventricular function and alters the pattern of left ventricular dilatation after myocardial infarction. Circulation 104, 2216-2221 (2001).
    • (2001) Circulation , vol.104 , pp. 2216-2221
    • Nwogu, N.I.1
  • 96
    • 0037108807 scopus 로고    scopus 로고
    • Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor
    • Tian, M. et al. Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc. Natl. Acad. Sci. USA 99, 13459-13464 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13459-13464
    • Tian, M.1
  • 97
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • Aravind, L. & Koonin, E.V. The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. Genome Biol. 2, 0007.1-0007.8 (2001).
    • (2001) Genome Biol. , vol.2 , pp. 71-78
    • Aravind, L.1    Koonin, E.V.2
  • 98
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α
    • Elkins, J.M. et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α. J. Biol. Chem. 278, 1802-1806 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 1802-1806
    • Elkins, J.M.1
  • 99
    • 0034021690 scopus 로고    scopus 로고
    • Hypoxia, clonal selection, and the role of HIF-1 in tumor progression
    • Semenza, G.L. Hypoxia, clonal selection, and the role of HIF-1 in tumor progression. Crit. Rev. Biochem. Mol. Biol. 35, 71-103 (2000).
    • (2000) Crit. Rev. Biochem. Mol. Biol. , vol.35 , pp. 71-103
    • Semenza, G.L.1
  • 101
    • 0032725554 scopus 로고    scopus 로고
    • P42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1
    • Richard, D.E., Berra, E., Gothie, E., Roux, D. & Pouysségur, J. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1. J. Biol. Chem. 274, 32631-32637 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouysségur, J.5
  • 102
    • 0034050050 scopus 로고    scopus 로고
    • Loss of PTEN facilitates HIF-1-mediated gene expression
    • Zundel, W. et al. Loss of PTEN facilitates HIF-1-mediated gene expression. Genes Dev. 14, 391-396 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 391-396
    • Zundel, W.1
  • 103
    • 0037131271 scopus 로고    scopus 로고
    • Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α
    • Chan, D.A., Sutphin, P.D., Denko, N.C. & Giaccia, A.J. Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1α. J. Biol. Chem. 277, 40112-40117 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 40112-40117
    • Chan, D.A.1    Sutphin, P.D.2    Denko, N.C.3    Giaccia, A.J.4
  • 104
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia inducible factor (HIF) in cancer cells
    • Knowles, H.J., Raval, R.R., Harris, A.L. & Ratcliffe, P.J. Effect of ascorbate on the activity of hypoxia inducible factor (HIF) in cancer cells. Cancer Res. 63, 1764-1768 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 105
    • 0037009846 scopus 로고    scopus 로고
    • The role of iron in cell cycle progression and the proliferation of neoplastic cells
    • Le, N.T.V. & Richardson, D.R. The role of iron in cell cycle progression and the proliferation of neoplastic cells. Biochim. Biophys. Acta 1603, 31-46 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1603 , pp. 31-46
    • Le, N.T.V.1    Richardson, D.R.2
  • 106
    • 0030816109 scopus 로고    scopus 로고
    • Hypoxia inducible factor-rop21 modulates gene expression in solid tumors and influences both angiogenesis and tumor growth
    • Maxwell, P.H. et al. Hypoxia inducible factor-1 modulates gene expression in solid tumors and influences both angiogenesis and tumor growth. Proc. Natl. Acad. Sci. USA 94, 8104-8109 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8104-8109
    • Maxwell, P.H.1
  • 107
    • 0034529914 scopus 로고    scopus 로고
    • Suppression of tumor growth through disruption of hypoxia-inducible transcription
    • Kung, A.L., Wang, S., Klco, J.M., Kaelin, W.G. & Livingston, D.M. Suppression of tumor growth through disruption of hypoxia-inducible transcription, Nat. Med. 6, 1335-1340 (2000).
    • (2000) Nat. Med. , vol.6 , pp. 1335-1340
    • Kung, A.L.1    Wang, S.2    Klco, J.M.3    Kaelin, W.G.4    Livingston, D.M.5
  • 108
    • 0037093107 scopus 로고    scopus 로고
    • Rescue of hypoxia-inducible factor-1α-deficient tumor growth by wild-type cells is independent of vascular endothelial growth factor
    • Hopfl, G. et al, Rescue of hypoxia-inducible factor-1α-deficient tumor growth by wild-type cells is independent of vascular endothelial growth factor. Cancer Res. 62, 2962-2970 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 2962-2970
    • Hopfl, G.1
  • 109
    • 0033870727 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1α is a positive factor in solid tumor growth
    • Ryan, H.E. et al. Hypoxia-inducible factor-1α is a positive factor in solid tumor growth. Cancer Res. 60, 4010-4015 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4010-4015
    • Ryan, H.E.1
  • 110
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin, W.G. Molecular basis of the VHL hereditary cancer syndrome. Nat. Rev. Cancer 2, 673-682 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 673-682
    • Kaelin, W.G.1
  • 111
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell, P.H. et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271-275 (1999).
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1
  • 112
    • 0029090338 scopus 로고
    • Tumour supression by the human von Hippel-Lindau gene product
    • Iliopoulos, O., Kibel, A., Gray, S. & Kaelin, W.G., Jr. Tumour supression by the human von Hippel-Lindau gene product. Nat. Med. 1, 822-826 (1995).
    • (1995) Nat. Med. , vol.1 , pp. 822-826
    • Iliopoulos, O.1    Kibel, A.2    Gray, S.3    Kaelin, W.G.4
  • 113
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • Kondo, K., Kico, J., Nakamura, E., Lechpammer, M. & Kaelin, W.G.J. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell 1, 237-246 (2002).
    • (2002) Cancer Cell , vol.1 , pp. 237-246
    • Kondo, K.1    Kico, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin, W.G.J.5
  • 114
    • 0036527785 scopus 로고    scopus 로고
    • The contribution of VHL substrate binding and HIF1-1α to the phenotype of VHL loss in renal cell carcinoma
    • Maranchie, J.K. et al. The contribution of VHL substrate binding and HIF1-1α to the phenotype of VHL loss in renal cell carcinoma. Cancer Cell 1, 247-255 (2002).
    • (2002) Cancer Cell , vol.1 , pp. 247-255
    • Maranchie, J.K.1
  • 115
    • 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.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, 44323-44330 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44323-44330
    • Vaux, E.C.1
  • 116
    • 0038383678 scopus 로고    scopus 로고
    • Loss of pVHL is sufficient to cause HIF dysregulation in primary cells but does not promote tumor growth
    • Mack, F.A. et al. Loss of pVHL is sufficient to cause HIF dysregulation in primary cells but does not promote tumor growth. Cancer Cell 3, 75-88 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 75-88
    • Mack, F.A.1
  • 117
    • 0034511179 scopus 로고    scopus 로고
    • Chasing the cancer demon
    • Knudson, A.G. Chasing the cancer demon. Annu. Rev. Genet. 34, 1-19 (2000).
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 1-19
    • Knudson, A.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.