메뉴 건너뛰기




Volumn 19, Issue 1, 2008, Pages 86-94

Hypoxia-inducible factor-1α stabilization in nonhypoxic conditions: Role of oxidation and intracellular ascorbate depletion

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; HYDROGEN PEROXIDE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; OXYGENASE; PROLINE;

EID: 38749106115     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-06-0612     Document Type: Article
Times cited : (149)

References (62)
  • 1
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R. J., Tian, Y. M., Raval, R. R., Turley, H., Harris, A. L., Pugh, C. W., Ratcliffe, P. J., and Gleadle, J. M. (2004). Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279, 38458-38465.
    • (2004) J. Biol. Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.M.2    Raval, R.R.3    Turley, H.4    Harris, A.L.5    Pugh, C.W.6    Ratcliffe, P.J.7    Gleadle, J.M.8
  • 2
    • 2542506333 scopus 로고    scopus 로고
    • Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells
    • BelAiba, R. S., Djordjevic, T., Bonello, S., Flugel, D., Hess, J., Kietzmann, T., and Gorlach, A. (2004). Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells. Biol. Chem. 385, 249-257.
    • (2004) Biol. Chem , vol.385 , pp. 249-257
    • BelAiba, R.S.1    Djordjevic, T.2    Bonello, S.3    Flugel, D.4    Hess, J.5    Kietzmann, T.6    Gorlach, A.7
  • 3
    • 34250745912 scopus 로고    scopus 로고
    • The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
    • Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R., and Chandel, N. S. (2007). The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. J. Cell Biol. 177, 1029-1036.
    • (2007) J. Cell Biol , vol.177 , pp. 1029-1036
    • Bell, E.L.1    Klimova, T.A.2    Eisenbart, J.3    Moraes, C.T.4    Murphy, M.P.5    Budinger, G.R.6    Chandel, N.S.7
  • 4
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • Berra, E., Benizri, E., Ginouves, A., Volmat, V., Roux, D., and Pouyssegur, J. (2003). HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J. 22, 4082-4090.
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 6
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R. K., and McKnight, S. L. (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
  • 8
    • 0037131271 scopus 로고    scopus 로고
    • Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1alpha
    • Chan, D. A., Sutphin, P. D., Denko, N. C., and Giaccia, A. J. (2002). Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1alpha. J. Biol. Chem. 277, 40112-40117.
    • (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
  • 9
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 alpha
    • Chan, D. A., Sutphin, P. D., Yen, S. E., and Giaccia, A. J. (2005). Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 alpha. Mol. Cell. Biol. 25, 6415-6426.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.E.3    Giaccia, A.J.4
  • 11
    • 33745191406 scopus 로고    scopus 로고
    • Reactive oxygen species signaling in vascular smooth muscle cells
    • Clempus, R. E., and Griendling, K. K. (2006). Reactive oxygen species signaling in vascular smooth muscle cells. Cardiovasc. Res. 71, 216-225.
    • (2006) Cardiovasc. Res , vol.71 , pp. 216-225
    • Clempus, R.E.1    Griendling, K.K.2
  • 13
    • 0019905709 scopus 로고
    • Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation
    • de Jong, L., Albracht, S. P., and Kemp, A. (1982). Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation. Biochim. Biophys. Acta 704, 326-332.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 326-332
    • de Jong, L.1    Albracht, S.P.2    Kemp, A.3
  • 14
    • 17944375360 scopus 로고    scopus 로고
    • Epstein, A. C. et al. (2001). C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54.
    • Epstein, A. C. et al. (2001). C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54.
  • 15
    • 0034466201 scopus 로고    scopus 로고
    • Reactive oxygen species as regulators of oxygen dependent gene expression
    • Fandrey, J., and Genius, J. (2000). Reactive oxygen species as regulators of oxygen dependent gene expression. Adv. Exp. Med. Biol. 475, 153-159.
    • (2000) Adv. Exp. Med. Biol , vol.475 , pp. 153-159
    • Fandrey, J.1    Genius, J.2
  • 16
    • 0033566693 scopus 로고    scopus 로고
    • Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2
    • Feldser, D., Agani, F., Iyer, N. V., Pak, B., Ferreira, G., and Semenza, G. L. (1999). Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2. Cancer Res. 59, 3915-3918.
    • (1999) Cancer Res , vol.59 , pp. 3915-3918
    • Feldser, D.1    Agani, F.2    Iyer, N.V.3    Pak, B.4    Ferreira, G.5    Semenza, G.L.6
  • 18
    • 0035816732 scopus 로고    scopus 로고
    • Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: Role of the p22(phox)-containing NADPH oxidase
    • Gorlach, A., Diebold, I., Schini-Kerth, V. B., Berchner-Pfannschmidt, U., Roth, U., Brandes, R. P., Kietzmann, T., and Busse, R. (2001). Thrombin activates the hypoxia-inducible factor-1 signaling pathway in vascular smooth muscle cells: role of the p22(phox)-containing NADPH oxidase. Circ. Res. 89, 47-54.
    • (2001) Circ. Res , vol.89 , pp. 47-54
    • Gorlach, A.1    Diebold, I.2    Schini-Kerth, V.B.3    Berchner-Pfannschmidt, U.4    Roth, U.5    Brandes, R.P.6    Kietzmann, T.7    Busse, R.8
  • 19
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling, K. K., Minieri, C. A., Ollerenshaw, J. D., and Alexander, R. W. (1994). Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 74, 1141-1148.
    • (1994) Circ. Res , vol.74 , pp. 1141-1148
    • Griendling, K.K.1    Minieri, C.A.2    Ollerenshaw, J.D.3    Alexander, R.W.4
  • 20
    • 0036314978 scopus 로고    scopus 로고
    • Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein
    • Groulx, I., and Lee, S. (2002). Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein. Mol. Cell. Biol. 22, 5319-5336.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5319-5336
    • Groulx, I.1    Lee, S.2
  • 21
    • 0037022303 scopus 로고    scopus 로고
    • Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis
    • Heessen, S., Leonchiks, A., Issaeva, N., Sharipo, A., Selivanova, G., Masucci, M. G., and Dantuma, N. P. (2002). Functional p53 chimeras containing the Epstein-Barr virus Gly-Ala repeat are protected from Mdm2- and HPV-E6-induced proteolysis. Proc. Natl. Acad. Sci. USA 99, 1532-1537.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1532-1537
    • Heessen, S.1    Leonchiks, A.2    Issaeva, N.3    Sharipo, A.4    Selivanova, G.5    Masucci, M.G.6    Dantuma, N.P.7
  • 22
    • 0033181324 scopus 로고    scopus 로고
    • Interleukin-1beta and tumor necrosis factor-alpha stimulate DNA binding of hypoxia-inducible factor-1
    • Hellwig-Burgel, T., Rutkowski, K., Metzen, E., Fandrey, J., and Jelkmann, W. (1999). Interleukin-1beta and tumor necrosis factor-alpha stimulate DNA binding of hypoxia-inducible factor-1. Blood 94, 1561-1567.
    • (1999) Blood , vol.94 , pp. 1561-1567
    • Hellwig-Burgel, T.1    Rutkowski, K.2    Metzen, E.3    Fandrey, J.4    Jelkmann, W.5
  • 23
    • 0033778504 scopus 로고    scopus 로고
    • Ascorbate transport in pig coronary artery smooth muscle: Na(+) removal and oxidative stress increase loss of accumulated cellular ascorbate
    • Holmes, M. E., Samson, S. E., Wilson, J. X., Dixon, S. J., and Grover, A. K. (2000). Ascorbate transport in pig coronary artery smooth muscle: Na(+) removal and oxidative stress increase loss of accumulated cellular ascorbate. J. Vasc. Res. 37, 390-398.
    • (2000) J. Vasc. Res , vol.37 , pp. 390-398
    • Holmes, M.E.1    Samson, S.E.2    Wilson, J.X.3    Dixon, S.J.4    Grover, A.K.5
  • 24
    • 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., and Bunn, H. F. (1998). Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 95, 7987-7992.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 26
    • 0035917808 scopus 로고    scopus 로고
    • 2-regulated prolyl hydroxylation
    • 2-regulated prolyl hydroxylation. Science 292, 468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 27
    • 33947233726 scopus 로고    scopus 로고
    • The role of ascorbate in the modulation of HIF-1alpha protein and HIF-dependent transcription by chromium(VI) and nickel(II)
    • Kaczmarek, M., Timofeeva, O. A., Karaczyn, A., Malyguine, A., Kasprzak, K. S., and Salnikow, K. (2007). The role of ascorbate in the modulation of HIF-1alpha protein and HIF-dependent transcription by chromium(VI) and nickel(II). Free Radic. Biol. Med. 42, 1246-1257.
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 1246-1257
    • Kaczmarek, M.1    Timofeeva, O.A.2    Karaczyn, A.3    Malyguine, A.4    Kasprzak, K.S.5    Salnikow, K.6
  • 28
    • 33645218975 scopus 로고    scopus 로고
    • Ascorbate depletion mediates up-regulation of hypoxia-associated proteins by cell density and nickel
    • Karaczyn, A., Ivanov, S., Reynolds, M., Zhitkovich, A., Kasprzak, K. S., and Salnikow, K. (2006). Ascorbate depletion mediates up-regulation of hypoxia-associated proteins by cell density and nickel. J. Cell Biochem. 97, 1025-1035.
    • (2006) J. Cell Biochem , vol.97 , pp. 1025-1035
    • Karaczyn, A.1    Ivanov, S.2    Reynolds, M.3    Zhitkovich, A.4    Kasprzak, K.S.5    Salnikow, K.6
  • 29
    • 14644418500 scopus 로고    scopus 로고
    • Mitochondria-derived reactive oxygen species and vascular MAP kinases: Comparison of angiotensin II and diazoxide
    • Kimura, S., Zhang, G. X., Nishiyama, A., Shokoji, T., Yao, L., Fan, Y. Y., Rahman, M., and Abe, Y. (2005). Mitochondria-derived reactive oxygen species and vascular MAP kinases: comparison of angiotensin II and diazoxide. Hypertension 45, 438-444.
    • (2005) Hypertension , vol.45 , pp. 438-444
    • Kimura, S.1    Zhang, G.X.2    Nishiyama, A.3    Shokoji, T.4    Yao, L.5    Fan, Y.Y.6    Rahman, M.7    Abe, Y.8
  • 30
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • Kivirikko, K. I., and Myllyharju, J. (1998). Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 16, 357-368.
    • (1998) Matrix Biol , vol.16 , pp. 357-368
    • Kivirikko, K.I.1    Myllyharju, J.2
  • 31
    • 33645080666 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1alpha by modulation of the labile iron pool in differentiating U937 macrophages: Effect of natural resistance-associated macrophage protein 1
    • Knowles, H. J., Mole, D. R., Ratcliffe, P. J., and Harris, A. L. (2006). Normoxic stabilization of hypoxia-inducible factor-1alpha by modulation of the labile iron pool in differentiating U937 macrophages: effect of natural resistance-associated macrophage protein 1. Cancer Res. 66, 2600-2607.
    • (2006) Cancer Res , vol.66 , pp. 2600-2607
    • Knowles, H.J.1    Mole, D.R.2    Ratcliffe, P.J.3    Harris, A.L.4
  • 32
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles, H. J., Raval, R. R., Harris, A. L., and Ratcliffe, P. J. (2003). Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res. 63, 1764-1768.
    • (2003) Cancer Res , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 33
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: Novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • Laughner, E., Taghavi, P., Chiles, K., Mahon, P. C., and Semenza, G. L. (2001). HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol. Cell. Biol. 21, 3995-4004.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3    Mahon, P.C.4    Semenza, G.L.5
  • 34
    • 34547136942 scopus 로고    scopus 로고
    • Differential regulation of hypoxia-inducible factor-1 (HIF-1) through receptor tyrosine kinase transactivation in vascular smooth muscle cells
    • Lauzier, M. C., Page, E. L., Michaud, M. D., and Richard, D. E. (2007). Differential regulation of hypoxia-inducible factor-1 (HIF-1) through receptor tyrosine kinase transactivation in vascular smooth muscle cells. Endocrinology 148, 4023-4031.
    • (2007) Endocrinology , vol.148 , pp. 4023-4031
    • Lauzier, M.C.1    Page, E.L.2    Michaud, M.D.3    Richard, D.E.4
  • 35
    • 0035380584 scopus 로고    scopus 로고
    • Purification of poly-ubiquitinated proteins by S5a-affinity chromatography
    • Layfield, R., Tooth, D., Landon, M., Dawson, S., Mayer, J., and Alban, A. (2001). Purification of poly-ubiquitinated proteins by S5a-affinity chromatography. Proteomics 1, 773-777.
    • (2001) Proteomics , vol.1 , pp. 773-777
    • Layfield, R.1    Tooth, D.2    Landon, M.3    Dawson, S.4    Mayer, J.5    Alban, A.6
  • 36
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia
    • Lee, P. J., Jiang, B. H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., and Choi, A. M. (1997). Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia. J. Biol. Chem. 272, 5375-5381.
    • (1997) J. Biol. Chem , vol.272 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, B.Y.3    Iyer, N.V.4    Alam, J.5    Semenza, G.L.6    Choi, A.M.7
  • 37
    • 0035859936 scopus 로고    scopus 로고
    • A new recommended dietary allowance of vitamin C for healthy young women
    • Levine, M., Wang, Y., Padayatty, S. J., and Morrow, J. (2001). A new recommended dietary allowance of vitamin C for healthy young women. Proc. Natl. Acad. Sci. USA 98, 9842-9846.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9842-9846
    • Levine, M.1    Wang, Y.2    Padayatty, S.J.3    Morrow, J.4
  • 38
    • 33746611555 scopus 로고    scopus 로고
    • Modulation of vascular smooth muscle signaling by reactive oxygen species
    • Lyle, A. N., and Griendling, K. K. (2006). Modulation of vascular smooth muscle signaling by reactive oxygen species. Physiology (Bethesda) 21, 269-280.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 269-280
    • Lyle, A.N.1    Griendling, K.K.2
  • 39
    • 0023021512 scopus 로고
    • Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase
    • Majamaa, K., Gunzler, V., Hanauske-Abel, H. M., Myllyla, R., and Kivirikko, K. I. (1986). Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J. Biol. Chem. 261, 7819-7823.
    • (1986) J. Biol. Chem , vol.261 , pp. 7819-7823
    • Majamaa, K.1    Gunzler, V.2    Hanauske-Abel, H.M.3    Myllyla, R.4    Kivirikko, K.I.5
  • 40
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation
    • Mansfield, K. D., Guzy, R. D., Pan, Y., Young, R. M., Cash, T. P., Schumacker, P. T., and Simon, M. C. (2005). Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation. Cell Metab. 1, 393-399.
    • (2005) Cell Metab , vol.1 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 41
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., and Ratcliffe, P. J. (2001). Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206.
    • (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
  • 43
    • 33747691662 scopus 로고    scopus 로고
    • Transforming growth factor beta1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression
    • McMahon, S., Charbonneau, M., Grandmont, S., Richard, D. E., and Dubois, C. M. (2006). Transforming growth factor beta1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression. J. Biol. Chem. 281, 24171-24181.
    • (2006) J. Biol. Chem , vol.281 , pp. 24171-24181
    • McMahon, S.1    Charbonneau, M.2    Grandmont, S.3    Richard, D.E.4    Dubois, C.M.5
  • 44
    • 18844408840 scopus 로고    scopus 로고
    • Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: Identification of a functional hypoxia-responsive element
    • Metzen, E., Stiehl, D. P., Doege, K., Marxsen, J. H., Hellwig-Burgel, T., and Jelkmann, W. (2005). Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element. Biochem. J. 387, 711-717.
    • (2005) Biochem. J , vol.387 , pp. 711-717
    • Metzen, E.1    Stiehl, D.P.2    Doege, K.3    Marxsen, J.H.4    Hellwig-Burgel, T.5    Jelkmann, W.6
  • 45
    • 0022568961 scopus 로고
    • Expression of smooth muscle-specific alpha-isoactin in cultured vascular smooth muscle cells: Relationship between growth and cytodifferentiation
    • Owens, G. K., Loeb, A., Gordon, D., and Thompson, M. M. (1986). Expression of smooth muscle-specific alpha-isoactin in cultured vascular smooth muscle cells: relationship between growth and cytodifferentiation. J. Cell Biol. 102, 343-352.
    • (1986) J. Cell Biol , vol.102 , pp. 343-352
    • Owens, G.K.1    Loeb, A.2    Gordon, D.3    Thompson, M.M.4
  • 46
    • 0037073695 scopus 로고    scopus 로고
    • Induction of hypoxia-inducible factor-1alpha by transcriptional and translational mechanisms
    • Page, E. L., Robitaille, G. A., Pouyssegur, J., and Richard, D. E. (2002). Induction of hypoxia-inducible factor-1alpha by transcriptional and translational mechanisms. J. Biol. Chem. 277, 48403-48409.
    • (2002) J. Biol. Chem , vol.277 , pp. 48403-48409
    • Page, E.L.1    Robitaille, G.A.2    Pouyssegur, J.3    Richard, D.E.4
  • 47
    • 33846630894 scopus 로고    scopus 로고
    • Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro
    • Pan, Y., Mansfield, K. D., Bertozzi, C. C., Rudenko, V., Chan, D. A., Giaccia, A. J., and Simon, M. C. (2007). Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol. Cell. Biol. 27, 912-925.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 912-925
    • Pan, Y.1    Mansfield, K.D.2    Bertozzi, C.C.3    Rudenko, V.4    Chan, D.A.5    Giaccia, A.J.6    Simon, M.C.7
  • 48
    • 33847390672 scopus 로고    scopus 로고
    • Queval, G., and Noctor, G. (2007). A plate reader method for the measurement of NAD, NADP, glutathione, and ascorbate in tissue extracts: application to redox profiling during Arabidopsis rosette development. Anal. Biochem. 363, 58-69.
    • Queval, G., and Noctor, G. (2007). A plate reader method for the measurement of NAD, NADP, glutathione, and ascorbate in tissue extracts: application to redox profiling during Arabidopsis rosette development. Anal. Biochem. 363, 58-69.
  • 49
    • 0032725554 scopus 로고    scopus 로고
    • p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1
    • Richard, D. E., Berra, E., Gothie, E., Roux, D., and Pouyssegur, J. (1999). p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1. J. Biol. Chem. 274, 32631-32637.
    • (1999) J. Biol. Chem , vol.274 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3    Roux, D.4    Pouyssegur, J.5
  • 50
    • 0034282388 scopus 로고    scopus 로고
    • Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1alpha in vascular smooth muscle cells
    • Richard, D. E., Berra, E., and Pouyssegur, J. (2000). Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1alpha in vascular smooth muscle cells. J. Biol. Chem. 275, 26765-26771.
    • (2000) J. Biol. Chem , vol.275 , pp. 26765-26771
    • Richard, D.E.1    Berra, E.2    Pouyssegur, J.3
  • 51
    • 18844387660 scopus 로고    scopus 로고
    • Angiotensin II activates the Smad pathway in vascular smooth muscle cells by a transforming growth factor-beta-independent mechanism
    • Rodriguez-Vita, J., Sanchez-Lopez, E., Esteban, V., Ruperez, M., Egido, J., and Ruiz-Ortega, M. (2005). Angiotensin II activates the Smad pathway in vascular smooth muscle cells by a transforming growth factor-beta-independent mechanism. Circulation 111, 2509-2517.
    • (2005) Circulation , vol.111 , pp. 2509-2517
    • Rodriguez-Vita, J.1    Sanchez-Lopez, E.2    Esteban, V.3    Ruperez, M.4    Egido, J.5    Ruiz-Ortega, M.6
  • 52
    • 34548496478 scopus 로고    scopus 로고
    • Angiotensin II induced reactive oxygen species and the kidney
    • Sachse, A., and Wolf, G. (2007). Angiotensin II induced reactive oxygen species and the kidney. J. Am. Soc. Nephrol. 18, 2439-2446.
    • (2007) J. Am. Soc. Nephrol , vol.18 , pp. 2439-2446
    • Sachse, A.1    Wolf, G.2
  • 53
    • 4644260710 scopus 로고    scopus 로고
    • Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress
    • Salnikow, K., Donald, S. P., Bruick, R. K., Zhitkovich, A., Phang, J. M., and Kasprzak, K. S. (2004). Depletion of intracellular ascorbate by the carcinogenic metals nickel and cobalt results in the induction of hypoxic stress. J. Biol. Chem. 279, 40337-40344.
    • (2004) J. Biol. Chem , vol.279 , pp. 40337-40344
    • Salnikow, K.1    Donald, S.P.2    Bruick, R.K.3    Zhitkovich, A.4    Phang, J.M.5    Kasprzak, K.S.6
  • 55
    • 0026075610 scopus 로고
    • Hypoxia-inducible nuclear factors bind to an enhancer element located 3′ to the human erythropoietin gene
    • Semenza, G. L., Nejfelt, M. K., Chi, S. M., and Antonarakis, S. E. (1991). Hypoxia-inducible nuclear factors bind to an enhancer element located 3′ to the human erythropoietin gene. Proc. Natl. Acad. Sci. USA 88, 5680-5684.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5680-5684
    • Semenza, G.L.1    Nejfelt, M.K.2    Chi, S.M.3    Antonarakis, S.E.4
  • 56
    • 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., and Wang, G. L. (1992). 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) Mol. Cell. Biol , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 57
    • 84934442193 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species are required for hypoxic HIF alpha stabilization
    • Simon, M. C. (2006). Mitochondrial reactive oxygen species are required for hypoxic HIF alpha stabilization. Adv. Exp. Med. Biol. 588, 165-170.
    • (2006) Adv. Exp. Med. Biol , vol.588 , pp. 165-170
    • Simon, M.C.1
  • 58
    • 33847051180 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor-1 alpha in cultured primary cells by intracellular ascorbate
    • Vissers, M. C., Gunningham, S. P., Morrison, M. J., Dachs, G. U., and Currie, M. J. (2007). Modulation of hypoxia-inducible factor-1 alpha in cultured primary cells by intracellular ascorbate. Free Radic. Biol. Med. 42, 765-772.
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 765-772
    • Vissers, M.C.1    Gunningham, S.P.2    Morrison, M.J.3    Dachs, G.U.4    Currie, M.J.5
  • 59
    • 34247854781 scopus 로고    scopus 로고
    • Ascorbate deficiency results in impaired neutrophil apoptosis and clearance and is associated with upregulation of hypoxia-inducible factor 1alpha
    • Vissers, M. C., and Wilkie, R. P. (2007). Ascorbate deficiency results in impaired neutrophil apoptosis and clearance and is associated with upregulation of hypoxia-inducible factor 1alpha. J. Leukoc. Biol. 42, 1236-1244.
    • (2007) J. Leukoc. Biol , vol.42 , pp. 1236-1244
    • Vissers, M.C.1    Wilkie, R.P.2
  • 62
    • 38749086236 scopus 로고    scopus 로고
    • Role of mitochondria in angiotensin II-induced reactive oxygen species and mitogen-activated protein kinase activation
    • Zhang, G. X., Lu, X. M., Kimura, S., and Nishiyama, A. (2007). Role of mitochondria in angiotensin II-induced reactive oxygen species and mitogen-activated protein kinase activation. Cardiovasc. Res. 7, 6204-6212.
    • (2007) Cardiovasc. Res , vol.7 , pp. 6204-6212
    • Zhang, G.X.1    Lu, X.M.2    Kimura, S.3    Nishiyama, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.